id: Q01989
gene_symbol: jar
product_type: PROTEIN
status: DRAFT
taxon:
  id: NCBITaxon:7227
  label: Drosophila melanogaster
description: >-
  jar (jaguar) encodes the sole Drosophila class VI unconventional myosin (Myosin
  heavy chain 95F).
  Myosin VI is unique among myosins in moving toward the minus (pointed) end of actin
  filaments.
  jar is a pleiotropic motor protein with essential roles in spermatid individualization
  (stabilizing
  actin cones), cytoplasmic particle transport in embryos, syncytial blastoderm organization,
  oogenesis transport through ring canals, neuroblast asymmetric division (basal targeting
  of
  Miranda), border cell migration (stabilizing E-cadherin), dorsal closure, epithelial
  morphogenesis,
  and coordination of actin-microtubule crosstalk via interaction with D-CLIP-190.
  It binds
  Androcam as a testis-specific light chain and calmodulin in other tissues.
alternative_products:
- name: B (G, J, K, Em-3)
  id: Q01989-1
- name: H (C, Em-1)
  id: Q01989-2
  sequence_note: VSP_003343
- name: I (D, Em-5)
  id: Q01989-3
  sequence_note: VSP_003344, VSP_003345
- name: 145 kDa
  id: Q01989-4
  sequence_note: Not described
existing_annotations:
# ============================================================
# IBA annotations (phylogenetic inference from GO_Central)
# ============================================================
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for cytoplasmic localization. Directly supported by multiple
      IDA
      experiments in Drosophila showing jar localizes to the peripheral cytoplasm
      in
      punctate patterns in embryos.
    action: ACCEPT
    reason: >-
      Consistent with experimental data from multiple studies. jar was detected in
      the
      cytoplasm by immunolocalization in embryos (PMID:1429838), syncytial blastoderm
      (PMID:7790355), and other tissues (PMID:10523504, PMID:12586070).
    supported_by:
    - reference_id: PMID:7790355
      supporting_text: "The 95F myosin, a class VI unconventional myosin, associates
        with particles in the cytoplasm of the Drosophila syncytial blastoderm"

- term:
    id: GO:0000146
    label: microfilament motor activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for microfilament motor activity. jar is a class VI unconventional
      myosin
      that catalyzes actin-based ATP-dependent particle translocation. The BioReason
      deep
      research correctly identifies this activity from the domain architecture.
    action: ACCEPT
    reason: >-
      Directly supported by experimental evidence that jar catalyzes actin-based,
      ATP-dependent
      transport of cytoplasmic particles in living embryos (PMID:8202156). The motor
      domain
      contains conserved ATP-binding and actin-binding motifs (PMID:1429838).
    supported_by:
    - reference_id: PMID:8202156
      supporting_text: "this transport is actin-based, ATP-dependent and catalysed
        by one such unconventional myosin, the 95F myosin"
    - reference_id: file:DROME/jar/jar-deep-research-bioreason-sft.md
      supporting_text: "An actin-based, minus-end-directed motor that uses an ATP-hydrolyzing
        head and a calmodulin-regulated lever arm to generate force on actin filaments"
    - reference_id: file:DROME/jar/jar-deep-research-falcon.md
      supporting_text: |-
        As a myosin, jar/myosin VI is an **ATP-dependent actin motor**: it uses ATP hydrolysis to generate force and movement along **actin filaments**.

- term:
    id: GO:0006897
    label: endocytosis
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for endocytosis based on phylogenetic inference from vertebrate
      myosin VI
      roles in endocytosis. In Drosophila, jar associates with D-CLIP-190, which is
      a homolog of
      CLIP-170, a protein that links endocytic vesicles to microtubules.
    action: ACCEPT
    reason: >-
      Supported by the association with D-CLIP-190 (endocytic vesicle-microtubule
      linker)
      and localization to endocytic vesicles (PMID:9472041). The vertebrate ortholog
      MYO6
      has well-established endocytic functions.
    supported_by:
    - reference_id: PMID:9472041
      supporting_text: "it is the first homologue identified of cytoplasmic linker
        protein (CLIP)-170, a protein that links endocytic vesicles to microtubules"

- term:
    id: GO:0015629
    label: actin cytoskeleton
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for actin cytoskeleton localization. jar is an actin-based motor
      and
      associates with actin structures throughout development.
    action: ACCEPT
    reason: >-
      Extensively supported. jar binds actin filaments directly (PMID:16571671 IDA),
      localizes
      to actin-rich structures including actin caps and furrows (PMID:7790355), actin
      cones during
      spermatid individualization (PMID:10588662), and cortical actin (PMID:12586070).
    supported_by:
    - reference_id: PMID:16571671
      supporting_text: "myosin VI binds to the cone front using its motor domain"

- term:
    id: GO:0051015
    label: actin filament binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for actin filament binding. Redundant with IDA evidence from
      PMID:16571671.
    action: ACCEPT
    reason: >-
      Directly supported by IDA evidence showing jar binds actin filaments in spermatid
      actin cones using its motor domain (PMID:16571671).
    supported_by:
    - reference_id: PMID:16571671
      supporting_text: "myosin VI binds to the cone front using its motor domain"

- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for plasma membrane localization. jar is recruited to cortical
      membrane
      sites in multiple contexts.
    action: ACCEPT
    reason: >-
      Consistent with jar localization to the cell cortex (PMID:12586070 IDA), membrane
      furrows
      in syncytial blastoderm (PMID:7790355), and leading edges of epithelial sheets
      during
      dorsal closure (PMID:15454264).
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "Miranda localization requires the unconventional myosin VI
        Jaguar (Jar)"

- term:
    id: GO:0030048
    label: actin filament-based movement
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for actin filament-based movement. jar is a motor that catalyzes
      actin-based transport.
    action: ACCEPT
    reason: >-
      Directly supported by observations that jar catalyzes actin-based, ATP-dependent
      cytoplasmic particle transport in living embryos (PMID:8202156).
    supported_by:
    - reference_id: PMID:8202156
      supporting_text: "Transport of cytoplasmic particles catalysed by an unconventional
        myosin in living Drosophila embryos"

- term:
    id: GO:0007015
    label: actin filament organization
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for actin filament organization. Supported by experimental evidence
      that jar is required for proper actin structure formation.
    action: ACCEPT
    reason: >-
      Strongly supported by IMP evidence that jar mutants have defective actin organization
      during spermatid individualization (PMID:10588662) and syncytial blastoderm
      (PMID:7790355).
      jar stabilizes branched actin networks in actin cones (PMID:16571671).
    supported_by:
    - reference_id: PMID:16571671
      supporting_text: "myosin VI stabilizes a branched actin network in actin structures
        (cones) that mediate the separation of the syncytial spermatids"

- term:
    id: GO:0030139
    label: endocytic vesicle
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for endocytic vesicle localization. Supported by direct experimental
      evidence from Drosophila.
    action: ACCEPT
    reason: >-
      jar co-immunoprecipitates with D-CLIP-190, a homolog of the endocytic
      vesicle-microtubule linker CLIP-170, and both colocalize on vesicle-like
      particulate structures (PMID:9472041).
    supported_by:
    - reference_id: PMID:9472041
      supporting_text: "it is the first homologue identified of cytoplasmic linker
        protein (CLIP)-170, a protein that links endocytic vesicles to microtubules"

# ============================================================
# IEA annotations (electronic/computational)
# ============================================================
- term:
    id: GO:0003774
    label: cytoskeletal motor activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro mapping. jar has a myosin motor domain (IPR001609)
      with
      ATPase activity coupled to actin translocation.
    action: ACCEPT
    reason: >-
      Correct mapping. jar is a bona fide actin-activated ATPase motor, directly demonstrated
      to catalyze particle transport (PMID:8202156).

- term:
    id: GO:0005524
    label: ATP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro mapping. jar has a conserved ATP-binding site in
      the motor domain
      (residues 151-158 in UniProt).
    action: ACCEPT
    reason: >-
      Correct. The motor domain contains the P-loop NTPase fold with ATP-binding motifs
      (PMID:1429838). ATP hydrolysis powers the motor activity.

- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: >-
      IEA annotation from ARBA machine learning. Redundant with multiple IDA and IBA
      annotations.
    action: ACCEPT
    reason: >-
      Correct and well supported by multiple experimental localizations (PMID:7790355,
      PMID:10523504, PMID:12586070, PMID:8202156).

- term:
    id: GO:0005856
    label: cytoskeleton
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: >-
      IEA annotation from UniProt subcellular location mapping. jar is a cytoskeletal
      motor protein.
    action: ACCEPT
    reason: >-
      Correct. jar is a cytoskeletal protein that associates with both actin and microtubule
      cytoskeletons (PMID:9472041).

- term:
    id: GO:0015629
    label: actin cytoskeleton
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: >-
      IEA annotation from ARBA. Redundant with IBA annotation for the same term.
    action: ACCEPT
    reason: >-
      Correct. jar is an actin-based motor that localizes to actin cytoskeletal structures.

- term:
    id: GO:0016459
    label: myosin complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro mapping. jar is a myosin heavy chain that forms
      complexes
      with light chains.
    action: MODIFY
    reason: >-
      While not wrong, the more specific term GO:0016461 (unconventional myosin complex)
      is
      already annotated with IDA evidence (PMID:9472041). The IEA annotation to the
      parent
      term is redundant and less informative.
    proposed_replacement_terms:
    - id: GO:0016461
      label: unconventional myosin complex

- term:
    id: GO:0051015
    label: actin filament binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro mapping. Redundant with IDA and IBA annotations.
    action: ACCEPT
    reason: >-
      Correct, well supported by direct experimental evidence (PMID:16571671 IDA).

# ============================================================
# Experimentally supported annotations (IDA, IMP, IPI, IGI, IEP, TAS, NAS)
# ============================================================

# --- Spermatid individualization complex ---
- term:
    id: GO:0070864
    label: sperm individualization complex
  evidence_type: IDA
  original_reference_id: PMID:12432073
  review:
    summary: >-
      IDA annotation for localization to sperm individualization complex. jar colocalizes
      with
      actin polymerization regulators cortactin and Arp2/3 at the IC.
    action: ACCEPT
    reason: >-
      Directly supported. "myosin VI colocalizes with and is required for the accumulation
      of
      the actin polymerization regulatory proteins, cortactin and arp2/3 complex,
      on actin
      structures that mediate membrane remodeling during spermatogenesis" (PMID:12432073).
    supported_by:
    - reference_id: PMID:12432073
      supporting_text: "myosin VI colocalizes with and is required for the accumulation
        of the actin polymerization regulatory proteins, cortactin and arp2/3 complex,
        on actin structures that mediate membrane remodeling during spermatogenesis"
    - reference_id: file:DROME/jar/jar-deep-research-falcon.md
      supporting_text: "colocalizes with and is required for accumulation of **cortactin**
        and **Arp2/3 complex** on actin structures mediating membrane remodeling"

# --- Investment cone ---
- term:
    id: GO:0070865
    label: investment cone
  evidence_type: IDA
  original_reference_id: PMID:16571671
  review:
    summary: >-
      IDA annotation for localization to investment cone. jar binds to the front of
      actin cones
      using its motor domain and stabilizes the branched actin network.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "myosin VI binds to the cone front using its motor domain"
      and
      "myosin VI stabilizes a branched actin network in actin structures (cones)"
      (PMID:16571671).
    supported_by:
    - reference_id: PMID:16571671
      supporting_text: "myosin VI binds to the cone front using its motor domain"

- term:
    id: GO:0070865
    label: investment cone
  evidence_type: IDA
  original_reference_id: PMID:16790438
  review:
    summary: >-
      IDA annotation for investment cone localization. jar and its light chain Androcam
      precisely colocalize at the leading edge of actin cones.
    action: ACCEPT
    reason: >-
      Directly supported. "Acam and myosin VI precisely colocalize at the leading
      edge of
      the actin cones" (PMID:16790438).
    supported_by:
    - reference_id: PMID:16790438
      supporting_text: "Acam and myosin VI precisely colocalize at the leading edge
        of the actin cones"

- term:
    id: GO:0070865
    label: investment cone
  evidence_type: IDA
  original_reference_id: PMID:21853045
  review:
    summary: >-
      IDA annotation for investment cone localization. Domain analysis showed both
      motor
      and cargo-binding domains are needed for cone front localization.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "The head (motor) and globular tail (cargo-binding) domains
      were
      both needed for localization at the cone front and dense meshwork formation"
      (PMID:21853045).
    supported_by:
    - reference_id: PMID:21853045
      supporting_text: "The head (motor) and globular tail (cargo-binding) domains
        were both needed for localization at the cone front and dense meshwork formation"
    - reference_id: file:DROME/jar/jar-deep-research-falcon.md
      supporting_text: "both the **head (motor) domain** and the **globular tail (cargo-binding)
        domain** are required for myosin VI localization to actin-cone fronts"

# --- Oogenesis transport ---
- term:
    id: GO:0007300
    label: ovarian nurse cell to oocyte transport
  evidence_type: IDA
  original_reference_id: PMID:9351468
  review:
    summary: >-
      IDA annotation based on direct observation of jar involvement in transport of
      particles
      from nurse cells into the oocyte via ring canals.
    action: ACCEPT
    reason: >-
      Directly demonstrated using antibody microinjection and time-lapse microscopy.
      "this
      unconventional myosin of class VI is involved in the transport processes" (PMID:9351468).
    supported_by:
    - reference_id: PMID:9351468
      supporting_text: "this unconventional myosin of class VI is involved in the
        transport processes...Additional myosin-VI molecules located at the rim of
        the ring canals seem to be involved in particle transport into the oocyte"

- term:
    id: GO:0007300
    label: ovarian nurse cell to oocyte transport
  evidence_type: IMP
  original_reference_id: PMID:9351468
  review:
    summary: >-
      IMP annotation based on anti-jar antibody injection blocking transport.
    action: ACCEPT
    reason: >-
      Supported by functional inhibition: antibody injection against jar blocked particle
      transport from nurse cells to oocyte (PMID:9351468).
    supported_by:
    - reference_id: PMID:9351468
      supporting_text: "Video-intensified fluorescence timelapse microscopy, in combination
        with microinjections of antibodies directed against Drosophila 95F myosin,
        have revealed that this unconventional myosin of class VI is involved in the
        transport processes"

# --- Growth cone ---
- term:
    id: GO:0030426
    label: growth cone
  evidence_type: IDA
  original_reference_id: PMID:25694447
  review:
    summary: >-
      IDA annotation for growth cone localization. CLIP-190 forms F-actin-dependent
      patches
      in growth cones mediated by binding to myosin VI, and jar is detected in growth
      cones.
    action: ACCEPT
    reason: >-
      Supported by the finding that CLIP-190 and CLIP-170 form "F-actin-dependent
      patches in
      growth cones, mediated by binding of the coiled-coil domain to myosin-VI" (PMID:25694447).
    supported_by:
    - reference_id: PMID:25694447
      supporting_text: "CLIP-190 and CLIP-170 form F-actin-dependent patches in growth
        cones, mediated by binding of the coiled-coil domain to myosin-VI"

# --- Myosin VI complex ---
- term:
    id: GO:0031476
    label: myosin VI complex
  evidence_type: IPI
  original_reference_id: PMID:16917818
  review:
    summary: >-
      IPI annotation based on co-precipitation of jar with the essential light chain
      (mlc-c).
      Mass spectrometry identified myosin VI among the binding partners of the essential
      light chain.
    action: ACCEPT
    reason: >-
      Supported by mass spectrometry and co-precipitation data identifying jar as
      an
      essential light chain binding partner (PMID:16917818).
    supported_by:
    - reference_id: PMID:16917818
      supporting_text: "We identify four myosins (myosin II, myosin V, myosin VI and
        myosin VIIA)...as binding partners for the essential light chain"

# --- Protein-containing complex ---
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: IPI
  original_reference_id: PMID:21368190
  review:
    summary: >-
      IPI annotation for protein-containing complex based on identification of multiple
      cargo-binding partners including Cornetto.
    action: KEEP_AS_NON_CORE
    reason: >-
      The annotation is correct but overly generic. The specific partners identified
      include
      Cornetto, a microtubule-associated protein involved in Hedgehog secretion (PMID:21368190).
      A more specific term would be preferred but this captures the physical interaction
      data.
    supported_by:
    - reference_id: PMID:21368190
      supporting_text: "the microtubule-associated protein Cornetto bound myosin VI"

# --- Positive regulation of exocytosis ---
- term:
    id: GO:0045921
    label: positive regulation of exocytosis
  evidence_type: IMP
  original_reference_id: PMID:21368190
  review:
    summary: >-
      IMP annotation for positive regulation of exocytosis based on requirement of
      jar
      for Hedgehog secretion.
    action: ACCEPT
    reason: >-
      Supported by the finding that jar and its binding partner Cornetto are both
      required
      for secretion of the lipidated morphogen Hedgehog (PMID:21368190).
    supported_by:
    - reference_id: PMID:21368190
      supporting_text: "we demonstrated a role for both in secretion of the lipidated
        morphogen Hedgehog"

# --- Mitochondrion transport ---
- term:
    id: GO:0047497
    label: mitochondrion transport along microtubule
  evidence_type: IDA
  original_reference_id: PMID:20592219
  review:
    summary: >-
      IDA annotation for mitochondrial transport regulation. RNAi depletion of jar
      selectively
      increased retrograde mitochondrial transport in neurons, suggesting jar opposes
      microtubule-based transport to facilitate docking.
    action: ACCEPT
    reason: >-
      Directly demonstrated by RNAi experiments. "Myosin VI depletion increased the
      same
      movement parameters but was selective for retrograde movement" (PMID:20592219).
      While
      jar opposes rather than promotes this transport, it is still directly involved
      in
      regulating the process.
    supported_by:
    - reference_id: PMID:20592219
      supporting_text: "Myosin VI depletion increased the same movement parameters
        but was selective for retrograde movement"

# --- Intracellular protein localization ---
- term:
    id: GO:0008104
    label: intracellular protein localization
  evidence_type: IMP
  original_reference_id: PMID:19204120
  review:
    summary: >-
      IMP annotation based on the finding that Miranda localization is affected in
      jar mutants,
      and the PP4 phosphatase pathway mediates Miranda complex localization.
    action: ACCEPT
    reason: >-
      Supported by genetic evidence. jar is required for proper basal localization
      of Miranda
      and associated cell fate determinants (PMID:12586070). The PP4 pathway acts
      in
      parallel or downstream (PMID:19204120).
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "Miranda localization requires the unconventional myosin VI
        Jaguar (Jar)"

# --- Calmodulin binding ---
- term:
    id: GO:0005516
    label: calmodulin binding
  evidence_type: IPI
  original_reference_id: PMID:16790438
  review:
    summary: >-
      IPI annotation for calmodulin binding. The IQ domain of jar can bind calmodulin,
      though in the testis, Androcam replaces calmodulin as the light chain.
    action: ACCEPT
    reason: >-
      Supported by in vitro binding data. "Drosophila CaM also shows high affinity
      interactions
      with these peptides" referring to the IQ domain peptides (PMID:16790438). Although
      in the
      testis Androcam replaces CaM, calmodulin binding is a genuine molecular function.
    supported_by:
    - reference_id: PMID:16790438
      supporting_text: "although Drosophila CaM also shows high affinity interactions
        with these peptides, we cannot detect a CaM/myosin VI interaction in the testis"

# --- Actin filament organization (IMP) ---
- term:
    id: GO:0007015
    label: actin filament organization
  evidence_type: IMP
  original_reference_id: PMID:10588662
  review:
    summary: >-
      IMP annotation for actin filament organization based on spermatogenesis mutant
      phenotype.
      jar mutants show defective IC movement and actin structure formation.
    action: ACCEPT
    reason: >-
      Directly supported. jar mutations cause defects in individualization complex
      organization
      and actin cone formation (PMID:10588662).
    supported_by:
    - reference_id: PMID:10588662
      supporting_text: "IC movement is aberrant in these 95F myosin mutants, indicating
        a critical role for 95F myosin in IC movement"

# --- Sperm individualization ---
- term:
    id: GO:0007291
    label: sperm individualization
  evidence_type: IMP
  original_reference_id: PMID:10588662
  review:
    summary: >-
      IMP annotation for sperm individualization. jar mutations cause male sterility
      due to
      defective spermatid individualization.
    action: ACCEPT
    reason: >-
      Core function. "This reduction of 95F myosin causes male sterility as a result
      of defects
      in spermatid individualization" (PMID:10588662). This is one of the best-characterized
      functions of jar.
    supported_by:
    - reference_id: PMID:10588662
      supporting_text: "This reduction of 95F myosin causes male sterility as a result
        of defects in spermatid individualization. Germ line transformation with the
        95F myosin heavy chain cDNA rescues the male sterility phenotype"

- term:
    id: GO:0007291
    label: sperm individualization
  evidence_type: IMP
  original_reference_id: PMID:16571671
  review:
    summary: >-
      IMP annotation for sperm individualization. jar stabilizes actin cones required
      for
      spermatid separation; mutant cones fail to accumulate F-actin.
    action: ACCEPT
    reason: >-
      Strongly supported. "In a myosin VI mutant, the cones do not accumulate F-actin
      during
      cone movement" (PMID:16571671).
    supported_by:
    - reference_id: PMID:16571671
      supporting_text: "In a myosin VI mutant, the cones do not accumulate F-actin
        during cone movement, whereas overexpression of myosin VI leads to bigger
        cones with more F-actin"

# --- Flagellated sperm motility ---
- term:
    id: GO:0030317
    label: flagellated sperm motility
  evidence_type: IMP
  original_reference_id: PMID:10588662
  review:
    summary: >-
      IMP annotation for flagellated sperm motility. jar mutations cause male sterility
      because spermatids fail to individualize and thus cannot become motile.
    action: KEEP_AS_NON_CORE
    reason: >-
      This is an indirect consequence of the individualization defect rather than
      a direct
      role in sperm motility. jar is not a flagellar motor -- it is required for the
      individualization process that is a prerequisite for motile sperm production.
    supported_by:
    - reference_id: PMID:10588662
      supporting_text: "This reduction of 95F myosin causes male sterility as a result
        of defects in spermatid individualization"

# --- Myosin VI complex (PMID:16790438) ---
- term:
    id: GO:0031476
    label: myosin VI complex
  evidence_type: IPI
  original_reference_id: PMID:16790438
  review:
    summary: >-
      IPI annotation for myosin VI complex. jar and Androcam co-immunoprecipitate
      from
      testis and interact in yeast two-hybrid assays.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "myosin VI and Acam co-immunoprecipitate from the testis
      and
      interact in yeast two-hybrid assays" (PMID:16790438).
    supported_by:
    - reference_id: PMID:16790438
      supporting_text: "myosin VI and Acam co-immunoprecipitate from the testis and
        interact in yeast two-hybrid assays"

# --- Regulation of actin filament-based process (IGI) ---
- term:
    id: GO:0032970
    label: regulation of actin filament-based process
  evidence_type: IGI
  original_reference_id: PMID:12432073
  review:
    summary: >-
      IGI annotation for regulation of actin filament-based process. jar and dynamin
      (shibire)
      function in parallel pathways to regulate actin dynamics during spermatogenesis.
    action: ACCEPT
    reason: >-
      Supported by genetic interaction data. "when dynamin and myosin VI function
      are both
      impaired, major defects in actin structures are observed" (PMID:12432073).
    supported_by:
    - reference_id: PMID:12432073
      supporting_text: "when dynamin and myosin VI function are both impaired, major
        defects in actin structures are observed...myosin VI and dynamin function
        in parallel pathways that regulate actin dynamics"

# --- Regulation of actin filament-based process (IMP) ---
- term:
    id: GO:0032970
    label: regulation of actin filament-based process
  evidence_type: IMP
  original_reference_id: PMID:16571671
  review:
    summary: >-
      IMP annotation for regulation of actin filament-based process. jar stabilizes
      actin
      networks in actin cones during spermatid individualization.
    action: ACCEPT
    reason: >-
      Directly supported. jar mutant cones fail to accumulate F-actin; overexpression
      leads to
      larger cones with more F-actin (PMID:16571671).
    supported_by:
    - reference_id: PMID:16571671
      supporting_text: "In a myosin VI mutant, the cones do not accumulate F-actin
        during cone movement, whereas overexpression of myosin VI leads to bigger
        cones with more F-actin"

# --- Actin filament binding (IDA) ---
- term:
    id: GO:0051015
    label: actin filament binding
  evidence_type: IDA
  original_reference_id: PMID:16571671
  review:
    summary: >-
      IDA annotation for actin filament binding. FRAP experiments showed jar binds
      actin
      at cone fronts with slow turnover, consistent with tethering.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "myosin VI binds to the cone front using its motor domain.
      Fluorescence recovery after photobleach experiments...revealed that myosin VI
      remains
      bound to F-actin for minutes" (PMID:16571671).
    supported_by:
    - reference_id: PMID:16571671
      supporting_text: "myosin VI remains bound to F-actin for minutes, suggesting
        its role is tethering, rather than transporting cargo"
    - reference_id: file:DROME/jar/jar-deep-research-falcon.md
      supporting_text: "FRAP of GFP-myosin VI indicates myosin VI can remain actin-bound
        for **minutes**, suggesting stable binding rather than rapid transport"

# --- Myosin VI light chain binding ---
- term:
    id: GO:0070856
    label: myosin VI light chain binding
  evidence_type: IPI
  original_reference_id: PMID:16790438
  review:
    summary: >-
      IPI annotation for myosin VI light chain binding. jar binds Androcam (a calmodulin-related
      protein) as a tissue-specific light chain in the testis.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "Acam binds with high affinity to peptide versions of
      both myosin VI
      light chain binding sites" (PMID:16790438).
    supported_by:
    - reference_id: PMID:16790438
      supporting_text: "Acam binds with high affinity to peptide versions of both
        myosin VI light chain binding sites"

# --- Actin binding (IMP, PMID:7790355) ---
- term:
    id: GO:0003779
    label: actin binding
  evidence_type: IMP
  original_reference_id: PMID:7790355
  review:
    summary: >-
      IMP annotation for actin binding based on the syncytial blastoderm study. Anti-jar
      antibody injection disrupts actin cytoskeleton organization.
    action: ACCEPT
    reason: >-
      Supported by functional evidence. Antibody inhibition of jar leads to "gross
      defects in
      the actin cytoskeleton, including indistinct actin caps and furrows" (PMID:7790355).
      jar was originally identified as a 140-kD ATP-sensitive actin-binding protein.
    supported_by:
    - reference_id: PMID:7790355
      supporting_text: "The 95F myosin, a class VI unconventional myosin, associates
        with particles in the cytoplasm"

# --- Cytoplasm (IDA, PMID:7790355) ---
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:7790355
  review:
    summary: >-
      IDA annotation for cytoplasm localization based on immunolocalization in syncytial
      blastoderm.
    action: ACCEPT
    reason: >-
      Directly observed. jar associates with cytoplasmic particles in the syncytial
      blastoderm (PMID:7790355).
    supported_by:
    - reference_id: PMID:7790355
      supporting_text: "The 95F myosin, a class VI unconventional myosin, associates
        with particles in the cytoplasm of the Drosophila syncytial blastoderm"

# --- Nucleus organization ---
- term:
    id: GO:0006997
    label: nucleus organization
  evidence_type: IMP
  original_reference_id: PMID:7790355
  review:
    summary: >-
      IMP annotation for nucleus organization. jar inhibition leads to aberrant nuclear
      morphology and positioning in the syncytial blastoderm.
    action: ACCEPT
    reason: >-
      Directly supported. "This disorganization is seen as aberrant nuclear morphology
      and
      position" (PMID:7790355). Nuclear defects are a consequence of actin cytoskeleton
      disorganization caused by loss of jar function.
    supported_by:
    - reference_id: PMID:7790355
      supporting_text: "This disorganization is seen as aberrant nuclear morphology
        and position and is suggestive of failures in cytoskeletal function"

# --- Spindle organization ---
- term:
    id: GO:0007051
    label: spindle organization
  evidence_type: IMP
  original_reference_id: PMID:7790355
  review:
    summary: >-
      IMP annotation for spindle organization. Loss of jar function leads to defective
      pseudocleavage furrows that fail to separate adjacent spindles.
    action: KEEP_AS_NON_CORE
    reason: >-
      The spindle defects are secondary to the actin furrow defects. "These furrows
      do not
      separate adjacent mitoses, since microtubules cross over them. These inappropriate
      microtubule interactions lead to aberrant nuclear divisions" (PMID:7790355).
      The primary
      role of jar here is in furrow formation, not directly in spindle assembly.
    supported_by:
    - reference_id: PMID:7790355
      supporting_text: "These furrows do not separate adjacent mitoses, since microtubules
        cross over them. These inappropriate microtubule interactions lead to aberrant
        nuclear divisions"

# --- Actin cytoskeleton organization ---
- term:
    id: GO:0030036
    label: actin cytoskeleton organization
  evidence_type: IMP
  original_reference_id: PMID:7790355
  review:
    summary: >-
      IMP annotation for actin cytoskeleton organization in the syncytial blastoderm.
    action: ACCEPT
    reason: >-
      Directly supported. jar inhibition causes "gross defects in the actin cytoskeleton,
      including indistinct actin caps and furrows, missing actin structures, abnormal
      spacing
      of caps, and abnormally spaced furrows" (PMID:7790355).
    supported_by:
    - reference_id: PMID:7790355
      supporting_text: "Nuclear defects correlate with gross defects in the actin
        cytoskeleton, including indistinct actin caps and furrows, missing actin structures,
        abnormal spacing of caps, and abnormally spaced furrows"

# --- Pseudocleavage ---
- term:
    id: GO:0030589
    label: pseudocleavage involved in syncytial blastoderm formation
  evidence_type: IMP
  original_reference_id: PMID:7790355
  review:
    summary: >-
      IMP annotation for pseudocleavage. jar is required for normal transient membrane
      furrow
      formation during the syncytial blastoderm stage.
    action: ACCEPT
    reason: >-
      Core function in early embryogenesis. "95F myosin function is required to generate
      normal
      actin-based transient membrane furrows" and "actin furrows do not invaginate
      as deeply into
      the embryo as do normal furrows" (PMID:7790355).
    supported_by:
    - reference_id: PMID:7790355
      supporting_text: "We propose that 95F myosin function is required to generate
        normal actin-based transient membrane furrows"

# --- Nucleus localization ---
- term:
    id: GO:0051647
    label: nucleus localization
  evidence_type: IMP
  original_reference_id: PMID:7790355
  review:
    summary: >-
      IMP annotation for nucleus localization. jar inhibition causes abnormal nuclear
      positioning in the syncytial blastoderm.
    action: KEEP_AS_NON_CORE
    reason: >-
      Nuclear positioning defects are secondary to actin cytoskeleton disorganization.
      The primary jar function is in actin furrow formation; nuclear mispositioning
      is
      a downstream consequence.
    supported_by:
    - reference_id: PMID:7790355
      supporting_text: "This disorganization is seen as aberrant nuclear morphology
        and position and is suggestive of failures in cytoskeletal function"

# --- Cytoplasm (IDA, PMID:10523504) ---
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:10523504
  review:
    summary: >-
      IDA annotation for cytoplasm localization based on antibody staining in follicle
      cells.
    action: ACCEPT
    reason: >-
      Directly observed. "Antibody staining shows that the expression of myosin 95F
      is greatly
      decreased in follicle cells when antisense Mhc95F RNA is expressed" -- implying
      antibody
      detection in cytoplasm of follicle cells (PMID:10523504).
    supported_by:
    - reference_id: PMID:10523504
      supporting_text: "Antibody staining shows that the expression of myosin 95F
        is greatly decreased in follicle cells when antisense Mhc95F RNA is expressed"

# --- Follicle cell migration ---
- term:
    id: GO:0007297
    label: follicle cell of egg chamber migration
  evidence_type: IMP
  original_reference_id: PMID:10523504
  review:
    summary: >-
      IMP annotation for follicle cell migration. Antisense knockdown of jar causes
      aberrant
      follicle cell migrations during oogenesis.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "abnormal follicle cell shapes and aberrant follicle
      cell migrations
      are observed when antisense Mhc95F is expressed in follicle cells" (PMID:10523504).
    supported_by:
    - reference_id: PMID:10523504
      supporting_text: "abnormal follicle cell shapes and aberrant follicle cell migrations
        are observed when antisense Mhc95F is expressed in follicle cells during stages
        9 to 10"

# --- Metamorphosis ---
- term:
    id: GO:0007552
    label: metamorphosis
  evidence_type: IMP
  original_reference_id: PMID:10523504
  review:
    summary: >-
      IMP annotation for metamorphosis. Antisense knockdown during development frequently
      results in lethality; surviving flies have malformed legs and wings.
    action: KEEP_AS_NON_CORE
    reason: >-
      The metamorphosis defects are pleiotropic consequences of jar loss rather than
      a specific
      involvement in the metamorphosis program. jar likely contributes via its general
      role in
      epithelial morphogenesis and cell shape maintenance.
    supported_by:
    - reference_id: PMID:10523504
      supporting_text: "Interfering with expression of Drosophila myosin VI at various
        developmental stages frequently results in lethality. During metamorphosis
        it results in adult flies with malformed legs and wings"

# --- Imaginal disc morphogenesis ---
- term:
    id: GO:0007560
    label: imaginal disc morphogenesis
  evidence_type: IMP
  original_reference_id: PMID:10523504
  review:
    summary: >-
      IMP annotation for imaginal disc morphogenesis. jar knockdown results in malformed
      appendages, indicating requirement for imaginal disc morphogenesis.
    action: KEEP_AS_NON_CORE
    reason: >-
      Pleiotropic consequence of jar loss of function. jar is required for imaginal
      disc
      morphogenesis likely through its roles in cell shape, adhesion, and membrane
      dynamics.
    supported_by:
    - reference_id: PMID:10523504
      supporting_text: "myosin VI is essential for imaginal disc morphogenesis"

# --- Larval chitin-based cuticle development ---
- term:
    id: GO:0008363
    label: larval chitin-based cuticle development
  evidence_type: IMP
  original_reference_id: PMID:10523504
  review:
    summary: >-
      IMP annotation for larval cuticle development. jar knockdown is lethal and affects
      larval development.
    action: KEEP_AS_NON_CORE
    reason: >-
      Likely a pleiotropic consequence of jar loss. jar is a general motor protein
      required
      for membrane dynamics and cell morphogenesis; cuticle defects are a secondary
      phenotype.
    supported_by:
    - reference_id: PMID:10523504
      supporting_text: "Interfering with expression of Drosophila myosin VI at various
        developmental stages frequently results in lethality"

# --- Morphogenesis of follicular epithelium ---
- term:
    id: GO:0016333
    label: morphogenesis of follicular epithelium
  evidence_type: IMP
  original_reference_id: PMID:10523504
  review:
    summary: >-
      IMP annotation for follicular epithelium morphogenesis. jar knockdown causes
      abnormal
      follicle cell shapes during oogenesis.
    action: ACCEPT
    reason: >-
      Directly supported. jar is expressed in migrating follicle cells and its loss
      causes
      aberrant cell shapes and migrations (PMID:10523504).
    supported_by:
    - reference_id: PMID:10523504
      supporting_text: "the Drosophila myosin VI is required for follicle cell epithelial
        morphogenesis"

# --- Protein binding (IPI, PMID:12586070) ---
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IPI annotation for protein binding based on direct binding of Miranda to jar.
    action: MODIFY
    reason: >-
      Per curation guidelines, 'protein binding' is uninformative. The specific interaction
      is
      Miranda binding, which is relevant to the basal protein targeting function.
      A more
      specific term would be appropriate.
    proposed_replacement_terms:
    - id: GO:0045309
      label: protein phosphorylated amino acid binding
    additional_reference_ids:
    - PMID:12586070
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "Miranda directly binds to Jar"

# --- Cytoplasm (IDA, PMID:12586070) ---
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IDA annotation for cytoplasm localization in neuroblasts.
    action: ACCEPT
    reason: >-
      Directly observed in immunolocalization studies of neuroblasts (PMID:12586070).
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "Miranda localization requires the unconventional myosin VI
        Jaguar (Jar)"

# --- Cytoplasm (IDA, PMID:8202156) ---
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:8202156
  review:
    summary: >-
      IDA annotation for cytoplasm localization based on observation of jar-associated
      particle transport in living embryos.
    action: ACCEPT
    reason: >-
      Directly observed. jar catalyzes transport of cytoplasmic particles in embryos
      (PMID:8202156).
    supported_by:
    - reference_id: PMID:8202156
      supporting_text: "this transport is actin-based, ATP-dependent and catalysed
        by one such unconventional myosin, the 95F myosin"

# --- Cell cortex ---
- term:
    id: GO:0005938
    label: cell cortex
  evidence_type: IDA
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IDA annotation for cell cortex localization in neuroblasts. jar localizes to
      the
      basal cortex where it recruits Miranda.
    action: ACCEPT
    reason: >-
      Directly demonstrated in neuroblasts. jar localizes cortically and is required
      for
      basal cortical targeting of Miranda (PMID:12586070).
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "Miranda localization requires the unconventional myosin VI
        Jaguar (Jar). In jar null mutant embryos, Miranda is delocalized"

# --- Actin filament-based movement (IDA, PMID:8202156) ---
- term:
    id: GO:0030048
    label: actin filament-based movement
  evidence_type: IDA
  original_reference_id: PMID:8202156
  review:
    summary: >-
      IDA annotation for actin filament-based movement. First direct demonstration
      of
      unconventional myosin-catalyzed transport in living cells.
    action: ACCEPT
    reason: >-
      Landmark study. "this transport is actin-based, ATP-dependent and catalysed
      by one such
      unconventional myosin, the 95F myosin" (PMID:8202156).
    supported_by:
    - reference_id: PMID:8202156
      supporting_text: "this transport is actin-based, ATP-dependent and catalysed
        by one such unconventional myosin, the 95F myosin"

# --- Asymmetric protein localization ---
- term:
    id: GO:0045167
    label: asymmetric protein localization involved in cell fate determination
  evidence_type: IMP
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IMP annotation for asymmetric protein localization in neuroblast cell fate determination.
      jar null mutants have delocalized Miranda.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "In jar null mutant embryos, Miranda is delocalized and
      the spindle
      is misoriented" (PMID:12586070). Miranda is a key adaptor for asymmetric segregation
      of
      cell fate determinants.
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "In jar null mutant embryos, Miranda is delocalized and the
        spindle is misoriented, but the Inscuteable crescent remains apical"

# --- Germline ring canal ---
- term:
    id: GO:0045172
    label: germline ring canal
  evidence_type: IDA
  original_reference_id: PMID:9351468
  review:
    summary: >-
      IDA annotation for germline ring canal localization. jar localizes to the rim
      of ring
      canals where it mediates particle transport into the oocyte.
    action: ACCEPT
    reason: >-
      Directly observed. "Additional myosin-VI molecules located at the rim of the
      ring canals
      seem to be involved in particle transport into the oocyte" (PMID:9351468).
    supported_by:
    - reference_id: PMID:9351468
      supporting_text: "Additional myosin-VI molecules located at the rim of the ring
        canals seem to be involved in particle transport into the oocyte"

# --- Basal protein localization (IMP) ---
- term:
    id: GO:0045175
    label: basal protein localization
  evidence_type: IMP
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IMP annotation for basal protein localization. jar is required for basal targeting
      of Miranda in neuroblasts.
    action: ACCEPT
    reason: >-
      Core finding of the study. "Miranda localization requires the unconventional
      myosin VI
      Jaguar" and "Miranda and its associated proteins are translocated basally by
      this
      actin-based motor" (PMID:12586070).
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "Miranda directly binds to Jar, raising the possibility that
        Miranda and its associated proteins are translocated basally by this actin-based
        motor"
    - reference_id: file:DROME/jar/jar-deep-research-falcon.md
      supporting_text: "myosin VI/Jar is required for **basal localization** of the
        fate determinant adaptor **Miranda** and for correct spindle orientation"

# --- Basal protein localization (IGI) ---
- term:
    id: GO:0045175
    label: basal protein localization
  evidence_type: IGI
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IGI annotation for basal protein localization based on genetic interaction with
      lgl
      (lethal giant larvae).
    action: ACCEPT
    reason: >-
      Supported by the genetic framework of asymmetric division. jar and lgl pathway
      components interact in establishing basal determinant localization (PMID:12586070).
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "Miranda directly binds to Jar, raising the possibility that
        Miranda and its associated proteins are translocated basally by this actin-based
        motor"

# --- Basal part of cell ---
- term:
    id: GO:0045178
    label: basal part of cell
  evidence_type: IDA
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IDA annotation for basal part of cell localization. jar is found at the basal
      cortex
      of neuroblasts.
    action: ACCEPT
    reason: >-
      Directly observed. jar localizes basally in neuroblasts and recruits Miranda
      to
      the basal cortex (PMID:12586070).
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "Miranda localization requires the unconventional myosin VI
        Jaguar (Jar). In jar null mutant embryos, Miranda is delocalized"

# --- Neuroblast division ---
- term:
    id: GO:0055057
    label: neuroblast division
  evidence_type: IMP
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IMP annotation for neuroblast division. jar null mutants have misoriented spindles
      and delocalized Miranda during neuroblast division.
    action: ACCEPT
    reason: >-
      Directly supported. jar is required for proper asymmetric neuroblast division
      through
      its role in Miranda targeting and spindle orientation (PMID:12586070).
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "In jar null mutant embryos, Miranda is delocalized and the
        spindle is misoriented"

# --- Sperm individualization (IGI, PMID:12432073) ---
- term:
    id: GO:0007291
    label: sperm individualization
  evidence_type: IGI
  original_reference_id: PMID:12432073
  review:
    summary: >-
      IGI annotation for sperm individualization based on genetic interaction between
      jar
      and dynamin (shibire).
    action: ACCEPT
    reason: >-
      Supported by genetic interaction. "when dynamin and myosin VI function are both
      impaired,
      major defects in actin structures are observed" during spermatogenesis (PMID:12432073).
    supported_by:
    - reference_id: PMID:12432073
      supporting_text: "myosin VI and dynamin function in parallel pathways that regulate
        actin dynamics"

# --- Regulation of protein localization ---
- term:
    id: GO:0032880
    label: regulation of protein localization
  evidence_type: IMP
  original_reference_id: PMID:12432073
  review:
    summary: >-
      IMP annotation for regulation of protein localization. jar is required for proper
      localization of cortactin and Arp2/3 to actin structures during spermatogenesis.
    action: ACCEPT
    reason: >-
      Directly supported. "myosin VI colocalizes with and is required for the accumulation
      of
      the actin polymerization regulatory proteins, cortactin and arp2/3 complex"
      (PMID:12432073).
    supported_by:
    - reference_id: PMID:12432073
      supporting_text: "myosin VI colocalizes with and is required for the accumulation
        of the actin polymerization regulatory proteins, cortactin and arp2/3 complex"

# --- Regulation of actin cytoskeleton organization ---
- term:
    id: GO:0032956
    label: regulation of actin cytoskeleton organization
  evidence_type: IMP
  original_reference_id: PMID:12432073
  review:
    summary: >-
      IMP annotation for regulation of actin cytoskeleton organization during spermatogenesis.
    action: ACCEPT
    reason: >-
      Directly supported. jar regulates actin dynamics at sites of membrane remodeling
      and
      is required for proper actin structure formation (PMID:12432073).
    supported_by:
    - reference_id: PMID:12432073
      supporting_text: "Regions of myosin VI accumulation are proposed as sites where
        actin assembly is coupled to membrane dynamics"

# --- Sperm individualization (IMP, PMID:16126191) ---
- term:
    id: GO:0007291
    label: sperm individualization
  evidence_type: IMP
  original_reference_id: PMID:16126191
  review:
    summary: >-
      IMP annotation for sperm individualization from a study primarily about myosin
      V.
      Both myosin V and myosin VI contribute to individualization.
    action: ACCEPT
    reason: >-
      Although PMID:16126191 is primarily about myosin V, the study also documents
      the
      involvement of myosin VI in spermatid individualization, consistent with the
      well-established
      role of jar in this process (PMID:10588662, PMID:16571671).
    supported_by:
    - reference_id: PMID:16126191
      supporting_text: "MyoV contributes to the formation of the actin-based investment
        cones"

# --- Myosin light chain binding ---
- term:
    id: GO:0032027
    label: myosin light chain binding
  evidence_type: IPI
  original_reference_id: PMID:16917818
  review:
    summary: >-
      IPI annotation for myosin light chain binding. jar was identified as a binding
      partner
      for the essential light chain by mass spectrometry and co-precipitation.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "We identify four myosins (myosin II, myosin V, myosin
      VI and
      myosin VIIA)...as binding partners for the essential light chain" (PMID:16917818).
    supported_by:
    - reference_id: PMID:16917818
      supporting_text: "We identify four myosins (myosin II, myosin V, myosin VI and
        myosin VIIA)...as binding partners for the essential light chain (but not
        the regulatory light chain) through mass spectrometry and co-precipitation"

# --- Border follicle cell migration ---
- term:
    id: GO:0007298
    label: border follicle cell migration
  evidence_type: IMP
  original_reference_id: PMID:12134162
  review:
    summary: >-
      IMP annotation for border cell migration. jar depletion from border cells severely
      inhibits their migration.
    action: ACCEPT
    reason: >-
      Core finding. "depletion of MyoVI specifically from border cells severely inhibited
      their
      migration" (PMID:12134162). jar stabilizes E-cadherin and Armadillo required
      for migration.
    supported_by:
    - reference_id: PMID:12134162
      supporting_text: "depletion of MyoVI specifically from border cells severely
        inhibited their migration...MyoVI is required for border cell migration where
        it stabilizes E-cadherin and Arm"

# --- Dorsal closure (IMP, PMID:15454264) ---
- term:
    id: GO:0007391
    label: dorsal closure
  evidence_type: IMP
  original_reference_id: PMID:15454264
  review:
    summary: >-
      IMP annotation for dorsal closure. jar localizes to the leading edge of the
      migrating
      epithelial sheet and is required for proper dorsal closure.
    action: ACCEPT
    reason: >-
      Directly demonstrated. "Dorsal closure, where there is a ring of Myosin VI at
      the edge
      of the migrating epithelial sheet, is often abnormal" in jar mutants (PMID:15454264).
    supported_by:
    - reference_id: PMID:15454264
      supporting_text: "Dorsal closure, where there is a ring of Myosin VI at the
        edge of the migrating epithelial sheet, is often abnormal"

# --- Establishment of mitotic spindle localization ---
- term:
    id: GO:0040001
    label: establishment of mitotic spindle localization
  evidence_type: IMP
  original_reference_id: PMID:12586070
  review:
    summary: >-
      IMP annotation for establishment of mitotic spindle localization. jar null mutants
      have misoriented spindles in neuroblasts.
    action: ACCEPT
    reason: >-
      Directly supported. "In jar null mutant embryos, Miranda is delocalized and
      the spindle
      is misoriented" (PMID:12586070). jar contributes to spindle orientation independently
      of the Inscuteable apical complex.
    supported_by:
    - reference_id: PMID:12586070
      supporting_text: "In jar null mutant embryos, Miranda is delocalized and the
        spindle is misoriented, but the Inscuteable crescent remains apical"

# --- Cell-cell junction maintenance ---
- term:
    id: GO:0045217
    label: cell-cell junction maintenance
  evidence_type: TAS
  original_reference_id: PMID:12620217
  review:
    summary: >-
      TAS annotation for cell-cell junction maintenance based on a review article
      about
      neuroblast asymmetric division and Jaguar's role.
    action: KEEP_AS_NON_CORE
    reason: >-
      PMID:12620217 is a commentary/review by Tuxworth and Chia, not a primary research
      article. The junction maintenance function is better supported by PMID:15454264
      and
      PMID:12134162 which show jar is required for cell adhesion and E-cadherin stability.
    supported_by:
    - reference_id: PMID:15454264
      supporting_text: "Myosin VI is crucial for correct cell morphology and maintenance
        of adhesive cellular contacts within epithelial cell layers"

# --- Actin filament-based movement (NAS, PMID:1429838) ---
- term:
    id: GO:0030048
    label: actin filament-based movement
  evidence_type: NAS
  original_reference_id: PMID:1429838
  review:
    summary: >-
      NAS annotation for actin filament-based movement. Based on the original cloning
      paper
      which identified jar as a new unconventional myosin.
    action: ACCEPT
    reason: >-
      Reasonable inference from the original characterization as an unconventional
      myosin
      with a head domain similar to other myosins and ATP-binding, actin-binding motifs
      (PMID:1429838). Later confirmed by direct observation (PMID:8202156).
    supported_by:
    - reference_id: PMID:1429838
      supporting_text: "it represents a new class of unconventional myosin heavy chains...contains
        ATP-binding, actin-binding and calmodulin/myosin light chain-binding motifs"

# --- Actin binding (NAS, PMID:1429838) ---
- term:
    id: GO:0003779
    label: actin binding
  evidence_type: NAS
  original_reference_id: PMID:1429838
  review:
    summary: >-
      NAS annotation for actin binding. Based on original identification as an ATP-sensitive
      actin-binding protein.
    action: ACCEPT
    reason: >-
      jar was originally identified as "a 140-kD ATP-sensitive actin-binding protein"
      (PMID:1429838). The actin-binding domain was identified in the head region.
    supported_by:
    - reference_id: PMID:1429838
      supporting_text: "the molecular analysis of a 140-kD ATP-sensitive actin-binding
        protein"

# --- Actin binding (IDA, PMID:9472041) ---
- term:
    id: GO:0003779
    label: actin binding
  evidence_type: IDA
  original_reference_id: PMID:9472041
  review:
    summary: >-
      IDA annotation for actin binding based on biochemical characterization.
    action: ACCEPT
    reason: >-
      jar is an actin-based motor. Actin binding is a fundamental property confirmed
      by
      multiple approaches (PMID:9472041, PMID:1429838).
    supported_by:
    - reference_id: PMID:9472041
      supporting_text: "a class VI unconventional myosin, the Drosophila 95F unconventional
        myosin, transports particles along actin filaments"

# --- Protein binding (IPI, PMID:9472041) ---
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:9472041
  review:
    summary: >-
      IPI annotation for protein binding based on co-immunoprecipitation with D-CLIP-190.
    action: MODIFY
    reason: >-
      Per curation guidelines, 'protein binding' is uninformative. The specific interaction
      is with D-CLIP-190 (CLIP-170 homolog), a microtubule-binding protein. A more
      specific
      term describing microtubule-associated protein binding would be preferred.
    proposed_replacement_terms:
    - id: GO:0008017
      label: microtubule binding
    supported_by:
    - reference_id: PMID:9472041
      supporting_text: "a 195-kD protein that coimmunoprecipitates with a class VI
        myosin, Drosophila 95F unconventional myosin"

# --- Microtubule associated complex ---
- term:
    id: GO:0005875
    label: microtubule associated complex
  evidence_type: IDA
  original_reference_id: PMID:9472041
  review:
    summary: >-
      IDA annotation for microtubule associated complex. jar co-immunoprecipitates
      with
      D-CLIP-190 and both cosediment with microtubules.
    action: ACCEPT
    reason: >-
      Directly demonstrated. jar physically associates with D-CLIP-190, which cosediments
      with microtubules (PMID:9472041). The complex links actin and microtubule systems.
    supported_by:
    - reference_id: PMID:9472041
      supporting_text: "Cloning and sequencing of the gene encoding the 195-kD protein
        reveals that it is the first homologue identified of cytoplasmic linker protein
        (CLIP)-170"

# --- Dorsal closure (IEP, PMID:1429838) ---
- term:
    id: GO:0007391
    label: dorsal closure
  evidence_type: IEP
  original_reference_id: PMID:1429838
  review:
    summary: >-
      IEP annotation for dorsal closure based on expression pattern. jar is expressed
      at
      high levels during mid-embryogenesis when dorsal closure occurs.
    action: ACCEPT
    reason: >-
      Although IEP evidence alone is weak, the direct role of jar in dorsal closure
      was
      confirmed by IMP evidence (PMID:15454264) and lethal mutant analysis showing
      defective
      dorsal closure (PMID:15454264). The IEP annotation is consistent with the confirmed
      role.
    supported_by:
    - reference_id: PMID:1429838
      supporting_text: "transcripts and protein are present throughout the life cycle,
        with peak expression occurring during mid-embryogenesis and adulthood"

# --- Microtubule binding ---
- term:
    id: GO:0008017
    label: microtubule binding
  evidence_type: IDA
  original_reference_id: PMID:9472041
  review:
    summary: >-
      IDA annotation for microtubule binding. jar associates with microtubule-associated
      complexes through its interaction with D-CLIP-190.
    action: ACCEPT
    reason: >-
      Supported by co-immunoprecipitation with D-CLIP-190 which cosediments with microtubules,
      and colocalization on particulate structures that resemble vesicles (PMID:9472041).
      Note
      this is indirect microtubule association via D-CLIP-190 rather than direct microtubule
      binding by jar itself.
    supported_by:
    - reference_id: PMID:9472041
      supporting_text: "these two proteins may functionally link the actin and microtubule
        cytoskeletons"

# --- Unconventional myosin complex (NAS) ---
- term:
    id: GO:0016461
    label: unconventional myosin complex
  evidence_type: NAS
  original_reference_id: PMID:1429838
  review:
    summary: >-
      NAS annotation for unconventional myosin complex from the original cloning paper.
    action: ACCEPT
    reason: >-
      jar was identified as a new class of unconventional myosin heavy chains (PMID:1429838),
      later confirmed as class VI.
    supported_by:
    - reference_id: PMID:1429838
      supporting_text: "it represents a new class of unconventional myosin heavy chains"

# --- Unconventional myosin complex (IDA) ---
- term:
    id: GO:0016461
    label: unconventional myosin complex
  evidence_type: IDA
  original_reference_id: PMID:9472041
  review:
    summary: >-
      IDA annotation for unconventional myosin complex. jar forms a complex with D-CLIP-190
      and light chains.
    action: ACCEPT
    reason: >-
      Directly demonstrated by immunoprecipitation. jar is a class VI unconventional
      myosin
      that forms multi-protein complexes (PMID:9472041).
    supported_by:
    - reference_id: PMID:9472041
      supporting_text: "a 195-kD protein that coimmunoprecipitates with a class VI
        myosin, Drosophila 95F unconventional myosin"

# --- Endocytic vesicle (IDA, PMID:9472041) ---
- term:
    id: GO:0030139
    label: endocytic vesicle
  evidence_type: IDA
  original_reference_id: PMID:9472041
  review:
    summary: >-
      IDA annotation for endocytic vesicle localization. jar colocalizes with D-CLIP-190
      on vesicle-like structures in neurons.
    action: ACCEPT
    reason: >-
      Directly observed. "In the axonal processes of neurons, they are colocalized
      in the same
      particulate structures, which resemble vesicles" (PMID:9472041). D-CLIP-190
      is a homolog
      of CLIP-170 which links endocytic vesicles to microtubules.
    supported_by:
    - reference_id: PMID:9472041
      supporting_text: "In the axonal processes of neurons, they are colocalized in
        the same particulate structures, which resemble vesicles"

references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with 
    GO terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular 
    Location vocabulary mapping
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning 
    models
  findings: []
- id: PMID:1429838
  title: An unconventional myosin heavy chain gene from Drosophila melanogaster.
  findings:
  - statement: >-
      jar was identified as a new class of unconventional myosin with a head domain
      29-33%
      identical to other myosins, containing ATP-binding, actin-binding, and calmodulin-binding
      motifs.
    supporting_text: "it represents a new class of unconventional myosin heavy chains...contains
      ATP-binding, actin-binding and calmodulin/myosin light chain-binding motifs"
- id: PMID:7790355
  title: The 95F unconventional myosin is required for proper organization of 
    the Drosophila syncytial blastoderm.
  findings:
  - statement: >-
      jar is required for normal actin-based transient membrane furrow formation,
      nuclear
      positioning, and actin cap organization in the syncytial blastoderm.
    supporting_text: "We propose that 95F myosin function is required to generate
      normal actin-based transient membrane furrows"
- id: PMID:8202156
  title: Transport of cytoplasmic particles catalysed by an unconventional 
    myosin in living Drosophila embryos.
  findings:
  - statement: >-
      jar catalyzes actin-based, ATP-dependent transport of cytoplasmic particles
      in living
      embryos. This was the first direct observation of unconventional myosin-catalyzed
      transport
      in living cells.
    supporting_text: "this transport is actin-based, ATP-dependent and catalysed by
      one such unconventional myosin, the 95F myosin"
- id: PMID:9351468
  title: Drosophila unconventional myosin VI is involved in intra- and 
    intercellular transport during oogenesis.
  findings:
  - statement: >-
      jar mediates microfilament-dependent transport of particles including mitochondria
      from
      nurse cells through ring canals into the oocyte.
    supporting_text: "this unconventional myosin of class VI is involved in the transport
      processes"
- id: PMID:9472041
  title: A class VI unconventional myosin is associated with a homologue of a 
    microtubule-binding protein, cytoplasmic linker protein-170, in neurons and 
    at the posterior pole of Drosophila embryos.
  findings:
  - statement: >-
      jar co-immunoprecipitates with D-CLIP-190 (CLIP-170 homolog), a microtubule-binding
      protein. They colocalize in neurons and at the posterior pole, suggesting a
      role in
      actin-microtubule coordination.
    supporting_text: "these two proteins may functionally link the actin and microtubule
      cytoskeletons"
- id: PMID:10523504
  title: A targeted gene silencing technique shows that Drosophila myosin VI is 
    required for egg chamber and imaginal disc morphogenesis.
  findings:
  - statement: >-
      jar is required for follicle cell migration, egg chamber morphogenesis, and
      imaginal
      disc morphogenesis. Loss causes aberrant follicle cell shapes and lethality.
    supporting_text: "the Drosophila myosin VI is required for follicle cell epithelial
      morphogenesis"
- id: PMID:10588662
  title: Class VI unconventional myosin is required for spermatogenesis in 
    Drosophila.
  findings:
  - statement: >-
      jar is a component of the individualization complex (IC) and is essential for
      spermatid
      individualization. Partial loss-of-function causes male sterility rescued by
      transgene expression.
    supporting_text: "95F myosin is a component of the IC whose function is essential
      for individualization"
- id: PMID:12134162
  title: Myosin VI is required for E-cadherin-mediated border cell migration.
  findings:
  - statement: >-
      jar is required for border cell migration via stabilization of E-cadherin and
      Armadillo.
      jar and Armadillo co-immunoprecipitate.
    supporting_text: "MyoVI is required for border cell migration where it stabilizes
      E-cadherin and Arm"
- id: PMID:12432073
  title: A role for myosin VI in actin dynamics at sites of membrane remodeling 
    during Drosophila spermatogenesis.
  findings:
  - statement: >-
      jar colocalizes with and is required for accumulation of cortactin and Arp2/3
      at actin
      structures during spermatogenesis. jar and dynamin act in parallel to regulate
      actin dynamics.
    supporting_text: "myosin VI and dynamin function in parallel pathways that regulate
      actin dynamics"
- id: PMID:12586070
  title: The Drosophila myosin VI Jaguar is required for basal protein targeting
    and correct spindle orientation in mitotic neuroblasts.
  findings:
  - statement: >-
      jar is required for basal targeting of Miranda and correct spindle orientation
      in
      neuroblasts. Miranda directly binds jar.
    supporting_text: "Miranda localization requires the unconventional myosin VI Jaguar
      (Jar)"
- id: PMID:12620217
  title: 'Asymmetric cell division: Miranda chauffeured by Jaguar?'
  findings:
  - statement: >-
      Review/commentary discussing how myosin VI (Jaguar) transports Miranda basally
      in neuroblasts for asymmetric cell division.
    supporting_text: "a myosin VI (Jaguar) has been shown to be necessary for basal
      targeting of cell fate determinants in neuroblasts"
- id: PMID:15454264
  title: Myosin VI plays a role in cell-cell adhesion during epithelial 
    morphogenesis.
  findings:
  - statement: >-
      jar is required for dorsal closure and maintenance of cell-cell adhesion in
      epithelia.
      Mutants show cell detachment and irregular epithelial sheets.
    supporting_text: "Myosin VI is crucial for correct cell morphology and maintenance
      of adhesive cellular contacts within epithelial cell layers"
- id: PMID:16126191
  title: Drosophila myosin V is required for larval development and spermatid 
    individualization.
  findings:
  - statement: >-
      Study primarily about myosin V (MyoV). Both myosin V and myosin VI contribute
      to
      spermatid individualization, but with distinct roles.
    supporting_text: "MyoV contributes to the formation of the actin-based investment
      cones and acts to coordinate and/or anchor these structures"
- id: PMID:16571671
  title: Myosin VI stabilizes an actin network during Drosophila spermatid 
    individualization.
  findings:
  - statement: >-
      jar stabilizes a branched actin network in actin cones during spermatid individualization.
      FRAP shows jar tethers rather than transports at cone fronts.
    supporting_text: "myosin VI stabilizes a branched actin network in actin structures
      (cones) that mediate the separation of the syncytial spermatids"
- id: PMID:16790438
  title: Androcam is a tissue-specific light chain for myosin VI in the 
    Drosophila testis.
  findings:
  - statement: >-
      Androcam (Acam) is a testis-specific light chain for jar. They colocalize at
      actin
      cone leading edges and co-immunoprecipitate. Androcam replaces calmodulin in
      the testis.
    supporting_text: "Acam and not CaM acts as a myosin VI light chain in the Drosophila
      testis"
- id: PMID:16917818
  title: Native nonmuscle myosin II stability and light chain binding in 
    Drosophila melanogaster.
  findings:
  - statement: >-
      jar (myosin VI) was identified as a binding partner for the essential light
      chain
      by mass spectrometry and co-precipitation.
    supporting_text: "We identify four myosins (myosin II, myosin V, myosin VI and
      myosin VIIA)...as binding partners for the essential light chain"
- id: PMID:19204120
  title: Protein phosphatase 4 mediates localization of the Miranda complex 
    during Drosophila neuroblast asymmetric divisions.
  findings:
  - statement: >-
      PP4 phosphatase pathway mediates Miranda complex localization during neuroblast
      asymmetric divisions. PP4 acts in parallel to or downstream from lgl.
    supporting_text: "Protein Phosphatase 4 (PP4) regulatory subunit PP4R3/Falafel
      (Flfl) as a key mediator specific for the localization of Miranda (Mira)"
- id: PMID:20592219
  title: Evidence that myosin activity opposes microtubule-based axonal 
    transport of mitochondria.
  findings:
  - statement: >-
      jar (myosin VI) opposes microtubule-based retrograde mitochondrial transport
      in neurons.
      Depletion increases retrograde transport velocity and duty cycle.
    supporting_text: "Myosin VI depletion increased the same movement parameters but
      was selective for retrograde movement"
- id: PMID:21368190
  title: Proteomics approach to study the functions of Drosophila myosin VI 
    through identification of multiple cargo-binding proteins.
  findings:
  - statement: >-
      Multiple cargo-binding partners identified for jar including Cornetto. jar and
      Cornetto
      are both required for Hedgehog secretion.
    supporting_text: "the microtubule-associated protein Cornetto bound myosin VI,
      and we demonstrated a role for both in secretion of the lipidated morphogen
      Hedgehog"
- id: PMID:21853045
  title: Myosin VI regulates actin structure specialization through conserved 
    cargo-binding domain sites.
  findings:
  - statement: >-
      Both motor and cargo-binding domains of jar are required for actin cone localization
      and function. Conserved partner-binding sites in the tail are critical.
    supporting_text: "The head (motor) and globular tail (cargo-binding) domains were
      both needed for localization at the cone front and dense meshwork formation"
- id: file:DROME/jar/jar-deep-research-bioreason-sft.md
  title: BioReason deep research for jar
  findings:
  - statement: >-
      BioReason SFT model describes jar as an actin-based, minus-end-directed motor
      using an
      ATP-hydrolyzing head and calmodulin-regulated lever arm. The domain architecture
      analysis
      correctly identifies the motor, lever arm, and cargo-binding domains and their
      functional
      implications.
- id: PMID:25694447
  title: Drosophila CLIP-190 and mammalian CLIP-170 display reduced microtubule
    plus end association in the nervous system.
  findings:
  - statement: >-
      CLIP-190 forms F-actin-dependent patches in growth cones mediated by binding
      to
      jar (myosin VI). CLIP proteins are not essential for axon extension.
    supporting_text: "CLIP-190 and CLIP-170 form F-actin-dependent patches in growth
      cones, mediated by binding of the coiled-coil domain to myosin-VI"
- id: PMID:21745401
  title: Myosin VI contributes to synaptic transmission and development at the
    Drosophila neuromuscular junction.
  findings:
  - statement: >-
      At the larval neuromuscular junction, loss-of-function jar alleles reduce NMJ
      length and synaptic bouton number, alter synaptic vesicle localization, and
      perturb basal synaptic transmission and short-term plasticity. Myosin VI is
      proposed to anchor/tether synaptic vesicles at the bouton periphery. This NMJ
      synaptic function is not currently captured in GOA annotations for jar.
    reference_section_type: ABSTRACT
    supporting_text: "anchor to tether vesicles to the bouton periphery and, thereby,
      participating in"
- id: PMID:25062032
  title: Localization and mobility of synaptic vesicles in Myosin VI mutants of
    Drosophila.
  findings:
  - statement: >-
      FM-dye loading and FRAP of GFP-labeled synaptic vesicles show that in jar
      mutant boutons, newly endocytosed vesicles distribute throughout the bouton
      rather than peripherally and move more freely, supporting a role for myosin VI
      in tethering synaptic vesicles to their proper sub-cellular location.
    reference_section_type: ABSTRACT
    supporting_text: "function of Myosin VI in the nerve terminal is tethering synaptic
      vesicles to"
- id: PMID:18493084
  title: Genetic characterization of the Drosophila jaguar322 mutant reveals that
    complete myosin VI loss of function is not lethal.
  findings:
  - statement: >-
      Complete loss of myosin VI is not lethal in Drosophila; the previously reported
      lethality of the jar322 null allele is most likely due to deletion of a
      neighboring gene. Null animals are recovered at a lower than expected Mendelian
      frequency, indicating that jar contributes to robust development without being
      strictly essential for viability. This supports treating the broad pleiotropic
      developmental phenotypes as non-core consequences of jar loss.
    reference_section_type: ABSTRACT
    supporting_text: "myosin VI is not lethal in flies and that the previously reported
      lethality of"
- id: PMID:24204696
  title: Kermit interacts with Galphao, Vang, and motor proteins in Drosophila
    planar cell polarity.
  findings:
  - statement: >-
      In planar cell polarity, the activity of Kermit relies on motor proteins
      including the actin-based myosin VI, which is proposed to help deliver the PCP
      component Vang to dedicated cellular compartments downstream of Galphao
      signaling. This places jar/myosin VI in the PCP trafficking network.
    reference_section_type: ABSTRACT
    supporting_text: "actin-based myosin VI. Our results place Kermit as a potential
      transducer of Go,"
- id: file:DROME/jar/jar-deep-research-falcon.md
  title: Falcon deep research report for jar (Drosophila myosin VI / jaguar)
  findings:
  - statement: >-
      Falcon (Edison Scientific) synthesized report confirming jar/Q01989 encodes
      Drosophila myosin VI (jaguar; Mhc95F), an unconventional actin-based motor that
      moves toward the minus/pointed end of actin filaments and functions in a
      context-dependent manner as either a transporter or a tether/anchor. The report
      consolidates primary evidence for actin-cone stabilization during spermatid
      individualization (minutes-long actin binding by FRAP), basal Miranda targeting
      and spindle orientation in neuroblasts, synaptic vesicle tethering at the NMJ,
      and PCP trafficking. Class VI-specific inserts reverse directionality and slow
      ADP release to favor long actin association.
    reference_section_type: OTHER
    supporting_text: |-
      jar encodes a mechanochemical ATPase that converts **ATP hydrolysis** into movement and/or tension on **F-actin**, with context-dependent roles either as (i) a **motor/transporter** or (ii) a **tether/anchor** that binds actin strongly for extended periods and stabilizes actin-linked structures or vesicle positioning.

core_functions:
- description: >-
    Actin-based minus-end-directed motor activity. jar is a class VI unconventional
    myosin
    that catalyzes ATP-dependent transport of cytoplasmic particles along actin filaments
    toward the pointed (minus) end. This motor activity underlies its diverse cellular
    functions
    including particle transport in embryos and nurse cell-to-oocyte transport.
  molecular_function:
    id: GO:0000146
    label: microfilament motor activity
  directly_involved_in:
  - id: GO:0030048
    label: actin filament-based movement
  locations:
  - id: GO:0005737
    label: cytoplasm
  in_complex:
    id: GO:0031476
    label: myosin VI complex
  supported_by:
  - reference_id: PMID:8202156
    supporting_text: "this transport is actin-based, ATP-dependent and catalysed by
      one such unconventional myosin, the 95F myosin"

- description: >-
    Actin structure stabilization during spermatid individualization. jar stabilizes
    the
    branched actin network in investment cones that mediate membrane remodeling during
    spermatid separation. It acts by tethering/cross-linking actin filaments rather
    than
    transporting cargo, with slow turnover at cone fronts.
  molecular_function:
    id: GO:0051015
    label: actin filament binding
  directly_involved_in:
  - id: GO:0007291
    label: sperm individualization
  - id: GO:0032970
    label: regulation of actin filament-based process
  locations:
  - id: GO:0070865
    label: investment cone
  - id: GO:0070864
    label: sperm individualization complex
  supported_by:
  - reference_id: PMID:16571671
    supporting_text: "myosin VI stabilizes a branched actin network in actin structures
      (cones) that mediate the separation of the syncytial spermatids"
  - reference_id: PMID:16571671
    supporting_text: "myosin VI remains bound to F-actin for minutes, suggesting its
      role is tethering, rather than transporting cargo"

- description: >-
    Basal protein targeting and spindle orientation in neuroblasts. jar binds Miranda
    directly and transports it basally during asymmetric neuroblast division. This
    is
    required for proper spindle orientation and asymmetric cell fate determination.
  molecular_function:
    id: GO:0000146
    label: microfilament motor activity
  directly_involved_in:
  - id: GO:0045175
    label: basal protein localization
  - id: GO:0045167
    label: asymmetric protein localization involved in cell fate determination
  - id: GO:0055057
    label: neuroblast division
  locations:
  - id: GO:0045178
    label: basal part of cell
  - id: GO:0005938
    label: cell cortex
  supported_by:
  - reference_id: PMID:12586070
    supporting_text: "Miranda directly binds to Jar, raising the possibility that
      Miranda and its associated proteins are translocated basally by this actin-based
      motor"

- description: >-
    Border cell migration via E-cadherin stabilization. jar is required for E-cadherin-mediated
    border cell migration during oogenesis by stabilizing E-cadherin and Armadillo
    at
    the membrane.
  molecular_function:
    id: GO:0000146
    label: microfilament motor activity
  directly_involved_in:
  - id: GO:0007298
    label: border follicle cell migration
  locations:
  - id: GO:0005886
    label: plasma membrane
  supported_by:
  - reference_id: PMID:12134162
    supporting_text: "MyoVI is required for border cell migration where it stabilizes
      E-cadherin and Arm"

- description: >-
    Actin-microtubule coordination via D-CLIP-190 interaction. jar associates with
    D-CLIP-190 (CLIP-170 homolog) to coordinate actin- and microtubule-based transport,
    linking endocytic vesicles to both cytoskeletal systems in neurons and at the
    posterior pole of embryos.
  molecular_function:
    id: GO:0008017
    label: microtubule binding
  directly_involved_in:
  - id: GO:0006897
    label: endocytosis
  locations:
  - id: GO:0030139
    label: endocytic vesicle
  supported_by:
  - reference_id: PMID:9472041
    supporting_text: "these two proteins may functionally link the actin and microtubule
      cytoskeletons"
  in_complex:
    id: GO:0005875
    label: microtubule associated complex