sgcA

id: Q551V8
gene_symbol: sgcA
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:44689
  label: Dictyostelium discoideum
description: sgcA (sGC) is one of the two guanylyl cyclases of Dictyostelium
  discoideum and provides the great majority of chemoattractant-stimulated cGMP
  synthesis during cAMP chemotaxis. It is an unusually large (2843 aa, ~315 kDa)
  cytosolic enzyme whose central pair of class III adenylyl/guanylyl-cyclase
  catalytic domains is flanked by two large (~1000 aa) N- and C-terminal regions.
  Despite the "soluble guanylyl cyclase" name it is homologous to mammalian
  soluble adenylyl cyclase (a class III cyclase) rather than to the metazoan
  NO-sensitive, heme-containing soluble guanylyl cyclase; its Mg2+/GTP-dependent
  activity is stimulated by GTPgammaS and inhibited by Ca2+, and there is no
  evidence for NO or heme regulation. In resting cells the protein is largely
  cytosolic, and during chemotaxis it translocates to the leading edge, where its
  N-terminal region binds actin filaments in extending pseudopodia and the enzyme
  becomes catalytically active upon membrane association. The rapidly diffusing
  cGMP it produces promotes assembly of myosin II filaments in the cortex and rear
  of the cell, suppressing lateral pseudopodia and thereby maintaining polarity
  and directional movement. The sGC protein also has a cGMP-independent activity in
  which anteriorly localized protein refines and stabilizes pseudopod formation at
  the leading edge. Loss of the gene reduces chemotactic sensitivity toward cAMP and
  impairs aggregation, and the protein additionally influences electrotaxis
  directionality and the timing of intracellular calcium responses.
existing_annotations:
- term:
    id: GO:0000287
    label: magnesium ion binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000104
  qualifier: enables
  review:
    summary: sgcA is a class III nucleotide cyclase, and these enzymes use a
      divalent metal (Mg2+ or Mn2+) for two-metal-ion catalysis. Physiological
      activity is Mg2+/GTP dependent, so magnesium binding by the catalytic
      domain is biologically real. This is a cofactor requirement supporting the
      guanylate cyclase activity rather than a standalone core function.
    action: KEEP_AS_NON_CORE
    reason: Magnesium binding is a genuine catalytic cofactor requirement of the
      cyclase domain (physiological substrate is Mg2+/GTP) but is ancillary to
      the core guanylate cyclase molecular function.
    supported_by:
    - reference_id: PMID:11500361
      supporting_text: prevailing Mg 2+ concentration
    - reference_id: PMID:11500361
      supporting_text: stimulated by GTPγS and inhibited by Ca 2+ ions
- term:
    id: GO:0006182
    label: cGMP biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000108
  qualifier: involved_in
  review:
    summary: sgcA is the predominant source of chemoattractant-stimulated cGMP in
      Dictyostelium; gene disruption reduces guanylyl cyclase activity more than
      10-fold. The cGMP biosynthetic process annotation is a direct and accurate
      consequence of the enzyme's guanylate cyclase activity.
    action: ACCEPT
    reason: cGMP biosynthesis is the core biological output of this guanylate
      cyclase and is directly supported by experimental gene-disruption data.
    supported_by:
    - reference_id: PMID:11500361
      supporting_text: '>10-fold reduction in guanylyl cyclase activity'
- term:
    id: GO:0009190
    label: cyclic nucleotide biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: This is a correct but more general parent of cGMP biosynthetic
      process. The specific product of sgcA is cGMP, so the more precise cGMP
      biosynthetic process term better captures the function.
    action: KEEP_AS_NON_CORE
    reason: Accurate but redundant with the more specific cGMP biosynthetic
      process annotation; retained as a non-core general term.
    supported_by:
    - reference_id: PMID:11500361
      supporting_text: '>10-fold reduction in guanylyl cyclase activity'
- term:
    id: GO:0035556
    label: intracellular signal transduction
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: cGMP produced by sgcA acts as an intracellular second messenger
      during chemotaxis, so participation in intracellular signal transduction is
      correct. It is a broad term that does not capture the specific chemotactic
      role.
    action: KEEP_AS_NON_CORE
    reason: Correct high-level process term; retained as non-core because more
      specific chemotaxis and cGMP-biosynthesis terms better describe the role.
    supported_by:
    - reference_id: PMID:16790492
      supporting_text: cGMP plays an important role during chemotaxis
- term:
    id: GO:0019722
    label: calcium-mediated signaling
  evidence_type: IGI
  original_reference_id: PMID:40295210
  qualifier: acts_upstream_of_or_within
  review:
    summary: Genetic analysis shows that gca/sgc-null cells have an altered
      (slightly delayed) intracellular calcium response to external calcium, and
      the authors conclude that cGMP participates in calcium homeostasis. This is
      a modulatory, downstream role rather than a core function of the enzyme.
    action: KEEP_AS_NON_CORE
    reason: sgcA/cGMP modulates the timing of calcium responses but this is an
      accessory role, not the core guanylate-cyclase function.
    supported_by:
    - reference_id: PMID:40295210
      supporting_text: gca/sgc-null cells showed a slightly delayed response
    - reference_id: PMID:40295210
      supporting_text: G proteins, cGMP, and IplA are involved in calcium homeostasis
- term:
    id: GO:0031252
    label: cell leading edge
  evidence_type: IDA
  original_reference_id: PMID:19346484
  qualifier: located_in
  review:
    summary: In migrating cells the sGC protein localizes to the leading-edge
      pseudopod in an actin-dependent manner, consistent with direct-imaging data
      in this and other studies. This is a well-supported localization.
    action: ACCEPT
    reason: Direct experimental evidence places sGC at the leading-edge pseudopod
      during directed migration.
    supported_by:
    - reference_id: PMID:19346484
      supporting_text: components of the GCase- and PI3K-dependent signaling
        pathways localized at the leading edge of migrating cells during
        electrotaxis in an actin-dependent manner
- term:
    id: GO:0051602
    label: response to electrical stimulus
  evidence_type: IGI
  original_reference_id: PMID:19346484
  qualifier: acts_upstream_of_or_within
  review:
    summary: Genetic modulation of the guanylyl cyclases and the cGMP target
      GbpC reverses the preferred direction of migration in an electric field
      (electrotaxis), showing that sgcA acts within the response to an electrical
      stimulus. This is an accessory role rather than the enzyme's core function.
    action: KEEP_AS_NON_CORE
    reason: sgcA contributes to directional switching during electrotaxis, a
      specialized downstream behavior, not the core molecular function.
    supported_by:
    - reference_id: PMID:19346484
      supporting_text: the preferential direction of migration during
        electrotaxis in Dictyostelium cells can be reversed by genetically
        modulating both guanylyl cyclases
- term:
    id: GO:0031252
    label: cell leading edge
  evidence_type: IDA
  original_reference_id: PMID:29118357
  qualifier: located_in
  review:
    summary: The four chemotaxis-pathway proteins, including sGC, and their mRNAs
      are preferentially enriched at the cell front during migration. This
      supports leading-edge localization of sgcA.
    action: ACCEPT
    reason: Direct-imaging evidence places sGC among the chemotaxis proteins
      enriched at the leading edge/cell front.
    supported_by:
    - reference_id: PMID:29118357
      supporting_text: proteins of these four chemotaxis pathways and actin are
        preferentially enriched at the cell front
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IDA
  original_reference_id: PMID:15601898
  qualifier: located_in
  review:
    summary: In resting cells the major fraction of sGC-GFP is cytosolic, with a
      small cortical fraction. Cytosolic localization is directly observed and is
      the resting distribution of the enzyme.
    action: ACCEPT
    reason: Direct fluorescence imaging shows sGC is predominantly cytosolic in
      resting cells.
    supported_by:
    - reference_id: PMID:15601898
      supporting_text: major fraction of the sGC-GFP fusion protein localizes to
        the cytosol
- term:
    id: GO:1904269
    label: cell leading edge cell cortex
  evidence_type: IDA
  original_reference_id: PMID:15601898
  qualifier: located_in
  review:
    summary: In a cAMP gradient sGC-GFP relocates to the anterior (leading-edge)
      cell cortex, where the membrane-associated enzyme is catalytically active.
      This anterior cortical localization is directly observed.
    action: ACCEPT
    reason: Direct imaging shows chemoattractant-induced enrichment of sGC at the
      anterior cell cortex.
    supported_by:
    - reference_id: PMID:15601898
      supporting_text: sGC-GFP localizes to the anterior cell cortex
- term:
    id: GO:0004383
    label: guanylate cyclase activity
  evidence_type: IMP
  original_reference_id: PMID:11500361
  qualifier: enables
  review:
    summary: Gene disruption of sgcA abolishes most guanylyl cyclase activity
      (>10-fold reduction) without affecting adenylyl cyclase activity,
      demonstrating that this protein is a guanylate cyclase. This is the core
      molecular function.
    action: ACCEPT
    reason: Mutant-phenotype evidence directly establishes guanylate cyclase
      activity as the core molecular function of sgcA.
    supported_by:
    - reference_id: PMID:11500361
      supporting_text: '>10-fold reduction in guanylyl cyclase activity'
- term:
    id: GO:0050920
    label: regulation of chemotaxis
  evidence_type: IGI
  original_reference_id: PMID:22081140
  qualifier: acts_upstream_of_or_within
  review:
    summary: sGC is one of several accessory signalling enzymes that are not
      required for basal Ras-driven chemotaxis but provide a memory of direction
      and improved orientation, amplifying sensitivity in shallow gradients. This
      is a regulatory contribution to chemotaxis.
    action: KEEP_AS_NON_CORE
    reason: Accurate but general regulation-of-chemotaxis role; the specific
      chemotaxis-to-cAMP annotation better captures the biology.
    supported_by:
    - reference_id: PMID:22081140
      supporting_text: they provide a memory of direction and improved
        orientation of the cell
- term:
    id: GO:0043327
    label: chemotaxis to cAMP
  evidence_type: IGI
  original_reference_id: PMID:18299345
  qualifier: acts_upstream_of_or_within
  review:
    summary: Genetic screens identify sGC as a key mediator of cAMP chemotaxis.
      The protein localizes to the leading edge and interacts with actin
      filaments, while its cGMP product induces myosin filaments in the rear.
      This directly captures the physiological process sgcA acts within.
    action: ACCEPT
    reason: sgcA is a central mediator of chemotaxis to cAMP, providing both
      leading-edge protein and rear cGMP signals.
    supported_by:
    - reference_id: PMID:18299345
      supporting_text: this activity is mediated by a soluble guanylyl cyclase
    - reference_id: PMID:18299345
      supporting_text: cyclic guanosine monophosphate product induces myosin
        filaments in the rear of the cell
- term:
    id: GO:0006935
    label: chemotaxis
  evidence_type: IGI
  original_reference_id: PMID:18073238
  qualifier: acts_upstream_of_or_within
  review:
    summary: sGC/cGMP contributes to chemotaxis by maintaining a quiescent rear
      and efficient pseudopod retraction, which increases directional movement
      and stable cell streaming. This is a correct but general parent of the more
      specific chemotaxis-to-cAMP annotation.
    action: KEEP_AS_NON_CORE
    reason: Correct but broad; the specific chemotaxis-to-cAMP term is the more
      informative core process annotation.
    supported_by:
    - reference_id: PMID:18073238
      supporting_text: quiescent rear of the cell increases the efficiency of
        directional movement
- term:
    id: GO:0120320
    label: lateral pseudopodium retraction
  evidence_type: IGI
  original_reference_id: PMID:18073238
  qualifier: acts_upstream_of_or_within
  review:
    summary: cGMP produced by sGC promotes cortical myosin in the rear, enabling
      efficient retraction of lateral/rear pseudopodia during the rising flank of
      the cAMP wave. sgcA acts within this process.
    action: KEEP_AS_NON_CORE
    reason: A specific downstream consequence of cGMP/myosin signalling; accurate
      but not the core molecular function.
    supported_by:
    - reference_id: PMID:18073238
      supporting_text: efficiently retract pseudopodia in the rear of the cell
        during the rising flank of the cAMP wave
- term:
    id: GO:0004383
    label: guanylate cyclase activity
  evidence_type: IDA
  original_reference_id: PMID:16790492
  qualifier: enables
  review:
    summary: The sGC protein is the predominant guanylyl cyclase producing cGMP
      during chemotaxis; a point mutation in the catalytic site (sGCDeltacat)
      abolishes activity, confirming direct guanylate cyclase function. Core
      molecular function.
    action: ACCEPT
    reason: Direct experimental evidence, including a catalytically dead point
      mutant, establishes guanylate cyclase activity as the core function.
    supported_by:
    - reference_id: PMID:16790492
      supporting_text: cGMP plays an important role during chemotaxis and is
        produced predominantly by a soluble guanylyl cyclase
- term:
    id: GO:0006935
    label: chemotaxis
  evidence_type: IMP
  original_reference_id: PMID:16790492
  qualifier: acts_upstream_of_or_within
  review:
    summary: gc-null cells have a reduced chemotaxis index (0.43 vs 0.64 for
      cells expressing wild-type sGC), demonstrating that sgcA is required for
      full chemotactic efficiency. Correct but general process term.
    action: KEEP_AS_NON_CORE
    reason: Mutant-phenotype support for a general chemotaxis role; the specific
      chemotaxis-to-cAMP term better captures the core process.
    supported_by:
    - reference_id: PMID:16790492
      supporting_text: chemotaxis index of gc -null cells of 0.43
- term:
    id: GO:0015629
    label: actin cytoskeleton
  evidence_type: IDA
  original_reference_id: PMID:16790492
  qualifier: colocalizes_with
  review:
    summary: The sGC protein associates with actin filaments in pseudopodia via
      its N-terminal region; this actin association targets the enzyme to the
      leading edge and underlies its cGMP-independent role in refining pseudopod
      formation. A directly observed and functionally important localization.
    action: ACCEPT
    reason: Direct evidence that sGC colocalizes with/associates with the actin
      cytoskeleton in pseudopodia, a key aspect of its leading-edge behavior.
    supported_by:
    - reference_id: PMID:16790492
      supporting_text: sGC protein associates with actin filaments in pseudopodia
- term:
    id: GO:0031033
    label: myosin filament organization
  evidence_type: IGI
  original_reference_id: PMID:16790492
  qualifier: acts_upstream_of_or_within
  review:
    summary: cGMP from sGC drives incorporation of myosin into the cell cortex;
      cGMP-null cells incorporate almost no myosin in the posterior cortex during
      chemotaxis. sgcA acts upstream of cortical myosin filament organization.
    action: KEEP_AS_NON_CORE
    reason: Genuine downstream effect of cGMP signalling on cortical myosin, but
      an accessory process rather than the core molecular function.
    supported_by:
    - reference_id: PMID:16790492
      supporting_text: incorporate almost no myosin in the posterior cell cortex
        during chemotaxis
- term:
    id: GO:0031252
    label: cell leading edge
  evidence_type: IDA
  original_reference_id: PMID:16790492
  qualifier: located_in
  review:
    summary: The sGC protein is enriched in extending pseudopodia at the leading
      edge during chemotaxis. This is directly observed and is a core aspect of
      the enzyme's spatial behavior.
    action: ACCEPT
    reason: Direct imaging shows sGC enrichment at the leading edge during
      chemotaxis.
    supported_by:
    - reference_id: PMID:16790492
      supporting_text: The sGC protein is enriched in extending pseudopodia at
        the leading edge of the cell during chemotaxis
- term:
    id: GO:0031037
    label: myosin II filament disassembly
  evidence_type: TAS
  original_reference_id: PMID:14710184
  qualifier: acts_upstream_of_or_within
  review:
    summary: This review describes the cGMP cascade as regulating myosin filament
      formation in the posterior of the cell to inhibit lateral pseudopodia.
      Because the cascade primarily promotes cortical myosin II assembly, the
      disassembly direction is debatable; the annotation nonetheless correctly
      places sgcA within myosin II filament turnover, a downstream process.
    action: KEEP_AS_NON_CORE
    reason: TAS from a secondary review; sgcA/cGMP acts within cortical myosin II
      filament dynamics (the cascade chiefly promotes filament formation), an
      accessory role rather than the core function.
    supported_by:
    - reference_id: PMID:14710184
      supporting_text: regulates myosin filament formation in the posterior of
        the cell
- term:
    id: GO:0120320
    label: lateral pseudopodium retraction
  evidence_type: TAS
  original_reference_id: PMID:14710184
  qualifier: acts_upstream_of_or_within
  review:
    summary: The cGMP-signalling cascade regulates posterior myosin filament
      formation and thereby inhibits the formation of lateral pseudopodia that
      would misdirect the cell. sgcA acts within this process.
    action: KEEP_AS_NON_CORE
    reason: Accurate downstream role in suppressing lateral pseudopodia via cGMP;
      accessory to the core guanylate cyclase function.
    supported_by:
    - reference_id: PMID:14710184
      supporting_text: inhibiting the formation of lateral pseudopodia
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000104
  title: Electronic Gene Ontology annotations created by transferring manual GO annotations
    between related proteins based on shared sequence features
  findings: []
- id: GO_REF:0000108
  title: Automatic assignment of GO terms using logical inference, based on on inter-ontology
    links
  findings: []
- id: PMID:11500361
  title: The Dictyostelium homologue of mammalian soluble adenylyl cyclase encodes
    a guanylyl cyclase.
  findings:
  - statement: sgcA (sGC) is a class III cyclase homologous to mammalian soluble
      adenylyl cyclase, and its disruption reduces guanylyl cyclase activity more
      than 10-fold without affecting adenylyl cyclase activity.
    supporting_text: '>10-fold reduction in guanylyl cyclase activity'
  - statement: Physiological Mg2+-dependent sGC activity is stimulated by GTPgammaS
      and inhibited by Ca2+, indicating regulation distinct from the NO/heme
      metazoan soluble guanylyl cyclase.
    supporting_text: stimulated by GTPγS and inhibited by Ca 2+ ions
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Primary paper identifying and disrupting sgcA; establishes it as
      the predominant guanylyl cyclase and a class III (sAC-homologous) enzyme, not
      a NO-sensitive heme cyclase.
- id: PMID:14710184
  title: 'Chemotaxis: signalling modules join hands at front and tail.'
  findings:
  - statement: The cGMP-signalling cascade regulates myosin filament formation in
      the posterior of the cell, inhibiting lateral pseudopodia that could
      misdirect the cell.
    supporting_text: regulates myosin filament formation in the posterior of the cell
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Review that frames the front/back modular model; supports the
      cGMP-myosin-pseudopod suppression role but is a secondary source.
- id: PMID:15601898
  title: Activation of soluble guanylyl cyclase at the leading edge during Dictyostelium
    chemotaxis.
  findings:
  - statement: In resting cells sGC-GFP is mainly cytosolic, and in a cAMP gradient
      it relocates to the anterior cell cortex where the membrane-associated enzyme
      becomes active.
    supporting_text: major fraction of the sGC-GFP fusion protein localizes to the cytosol
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Establishes cytosolic resting distribution and chemoattractant-induced
      anterior cortical activation; cached record is abstract-only (full_text_available
      false) but the abstract states these localizations directly.
- id: PMID:16790492
  title: Guanylyl cyclase protein and cGMP product independently control front and
    back of chemotaxing Dictyostelium cells.
  findings:
  - statement: The sGC protein is enriched at the leading edge and associates with
      actin filaments in pseudopodia, while its cGMP product drives cortical myosin
      in the rear; the two functions are separable.
    supporting_text: The sGC protein is enriched in extending pseudopodia at the
      leading edge of the cell during chemotaxis
  - statement: sGC associates with actin filaments in pseudopodia.
    supporting_text: sGC protein associates with actin filaments in pseudopodia
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Uncouples catalytic activity (sGCDeltacat) from leading-edge
      localization (sGCDeltaN); the strongest evidence for the dual, cGMP-dependent
      and cGMP-independent, roles of sgcA.
- id: PMID:18073238
  title: The role of cGMP and the rear of the cell in Dictyostelium chemotaxis and
    cell streaming.
  findings:
  - statement: A quiescent, cGMP-dependent rear with efficient pseudopod retraction
      increases directional movement and stable cell streaming.
    supporting_text: quiescent rear of the cell increases the efficiency of directional
      movement
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Abstract-only cache; supports the rear/cGMP role in chemotaxis and
      pseudopod retraction.
- id: PMID:18299345
  title: Four key signaling pathways mediating chemotaxis in Dictyostelium discoideum.
  findings:
  - statement: A soluble guanylyl cyclase mediates chemotaxis by localizing to the
      leading edge (protein) and inducing rear myosin filaments (cGMP product).
    supporting_text: cyclic guanosine monophosphate product induces myosin filaments
      in the rear of the cell
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Genetic identification of sGC as one of four key chemotaxis
      pathways; supports chemotaxis-to-cAMP core process.
- id: PMID:19346484
  title: Switching direction in electric-signal-induced cell migration by cyclic guanosine
    monophosphate and phosphatidylinositol signaling.
  findings:
  - statement: sGC and its cGMP product control directional switching in
      electrotaxis, with sGC localizing to the leading-edge pseudopod in an
      actin-dependent manner.
    supporting_text: components of the GCase- and PI3K-dependent signaling pathways
      localized at the leading edge of migrating cells during electrotaxis in an
      actin-dependent manner
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Supports both leading-edge localization and an accessory role in
      electrotaxis directional switching.
- id: PMID:22081140
  title: 'Dictyostelium chemotaxis: essential Ras activation and accessory signalling
    pathways for amplification.'
  findings:
  - statement: sGC is an accessory signalling enzyme that is dispensable for basal
      Ras-driven chemotaxis but provides a memory of direction and improved
      orientation, amplifying sensitivity in shallow gradients.
    supporting_text: they provide a memory of direction and improved orientation of
      the cell
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Places sGC among accessory amplification pathways rather than the
      essential Ras module; supports regulation-of-chemotaxis annotation.
- id: PMID:29118357
  title: Pumilio-dependent localization of mRNAs at the cell front coordinates multiple
    pathways required for chemotaxis.
  findings:
  - statement: The four chemotaxis-pathway proteins (including sGC) and their mRNAs
      are preferentially enriched at the cell front during dynamic migration.
    supporting_text: proteins of these four chemotaxis pathways and actin are
      preferentially enriched at the cell front
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Supports leading-edge/cell-front enrichment of sGC among the
      coordinated chemotaxis pathways.
- id: PMID:40295210
  title: Intracellular Calcium Responses to External Calcium Stimuli in Dictyostelium.
  findings:
  - statement: gca/sgc-null cells show an altered (slightly delayed) intracellular
      calcium response to external calcium, and cGMP is implicated in calcium
      homeostasis.
    supporting_text: gca/sgc-null cells showed a slightly delayed response
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Supports a modulatory role of cGMP/sgcA in the timing of calcium
      responses; peripheral to the core function.
core_functions:
- description: sgcA is the principal soluble (class III, sAC-homologous) guanylyl
    cyclase of Dictyostelium, synthesizing the chemoattractant-induced cGMP burst
    from Mg2+/GTP. The enzyme is largely cytosolic at rest and becomes active upon
    membrane/leading-edge association; the diffusible cGMP promotes cortical myosin
    II assembly that suppresses lateral pseudopodia and maintains polarity during
    cAMP chemotaxis.
  molecular_function:
    id: GO:0004383
    label: guanylate cyclase activity
  directly_involved_in:
  - id: GO:0043327
    label: chemotaxis to cAMP
  locations:
  - id: GO:0005829
    label: cytosol
  - id: GO:0031252
    label: cell leading edge
  - id: GO:1904269
    label: cell leading edge cell cortex
  supported_by:
  - reference_id: PMID:11500361
    supporting_text: '>10-fold reduction in guanylyl cyclase activity'
  - reference_id: PMID:16790492
    supporting_text: cGMP plays an important role during chemotaxis and is produced
      predominantly by a soluble guanylyl cyclase
  - reference_id: PMID:15601898
    supporting_text: sGC-GFP localizes to the anterior cell cortex
- description: Independently of its catalytic product, the sGC protein acts as an
    actin-associated, leading-edge scaffold; its N-terminal region binds actin
    filaments in extending pseudopodia, localizing the protein to the cell front
    where it refines and stabilizes pseudopod formation.
  molecular_function:
    id: GO:0004383
    label: guanylate cyclase activity
  locations:
  - id: GO:0015629
    label: actin cytoskeleton
  - id: GO:0031252
    label: cell leading edge
  supported_by:
  - reference_id: PMID:16790492
    supporting_text: sGC protein associates with actin filaments in pseudopodia
  - reference_id: PMID:16790492
    supporting_text: The sGC protein is enriched in extending pseudopodia at the
      leading edge of the cell during chemotaxis