id: Q09683
gene_symbol: mre11
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:284812
  label: Schizosaccharomyces pombe (strain 972 / ATCC 24843)
description: Mre11 (Rad32) is the DNA-binding nuclease subunit of the nuclear Mre11-Rad50-Nbs1 complex.
  It helps recognize and tether DNA double-strand breaks, coordinates DNA-end processing with Ctp1, and
  supports homologous recombination, selected nonhomologous end-joining reactions, telomere maintenance,
  and DNA damage signaling. Its conserved nuclease domain has endonucleolytic and 3′-to-5′ exonucleolytic
  activities. During meiosis it processes Rec12-linked DNA ends for repair and can initiate a separate
  palindrome-associated breakage pathway.
existing_annotations:
- term: &id021
    id: GO:0000014
    label: single-stranded DNA endonuclease activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  supporting_entities:
  - PANTHER:PTN000015644
  - UniProtKB:P49959
  review:
    summary: single-stranded DNA endonuclease activity is supported.
    action: ACCEPT
    reason: Mre11 is the conserved phosphodiesterase nuclease of MRN. Purified homolog biochemistry establishes
      DNA endonuclease and 3′-to-5′ exonuclease chemistry; fission yeast catalytic-domain structures and
      nuclease mutants independently establish a functional nuclease. This activity is distinct from the
      net 5′-strand resection produced by the repair pathway.
    supported_by:
    - &id001
      reference_id: PMID:9651580
      supporting_text: We have investigated the enzymatic activities of the purified proteins and found
        that Mre11 by itself has 3' to 5' exonuclease activity that is increased when Mre11 is in a complex
        with Rad50. Mre11 also exhibits endonuclease activity, as shown by the asymmetric opening of DNA
        hairpin loops.
    - &id002
      reference_id: PMID:22705791
      supporting_text: To understand the functional architecture of MRN, we determined the crystal structures
        of the Schizosaccharomyces pombe Mre11 dimeric catalytic domain alone and in complex with a fragment
        of Nbs1.
    - &id003
      reference_id: PMID:19139281
      supporting_text: This study demonstrates for the first time that Mre11 (Schizosaccharomyces pombe
        Rad32(Mre11)) nuclease activity is required for the removal of Rec12(Spo11).
    - &id004
      reference_id: PMID:9705271
      supporting_text: We show that the Rad50-Mre11-p95 complex possesses manganese-dependent single-stranded
        DNA endonuclease and 3' to 5' exonuclease activities.
- term:
    id: GO:0000014
    label: single-stranded DNA endonuclease activity
  evidence_type: ISO
  original_reference_id: PMID:9651580
  qualifier: enables
  supporting_entities:
  - UniProtKB:P49959
  review:
    summary: single-stranded DNA endonuclease activity is supported.
    action: ACCEPT
    reason: Mre11 is the conserved phosphodiesterase nuclease of MRN. Purified homolog biochemistry establishes
      DNA endonuclease and 3′-to-5′ exonuclease chemistry; fission yeast catalytic-domain structures and
      nuclease mutants independently establish a functional nuclease. This activity is distinct from the
      net 5′-strand resection produced by the repair pathway.
    supported_by:
    - *id001
    - *id002
    - *id003
    - *id004
- term:
    id: GO:0000403
    label: Y-form DNA binding
  evidence_type: ISO
  original_reference_id: PMID:18854158
  qualifier: enables
  supporting_entities:
  - UniProtKB:Q8U1N9
  review:
    summary: Y-form DNA binding is supported.
    action: ACCEPT
    reason: DNA-complex structures resolve how the conserved Mre11 dimer engages branched substrates and
      DNA ends. Fission yeast mutational analysis links this architecture to MRN assembly and break repair,
      supporting the curated orthology transfer rather than a claim of a target-only binding assay.
    supported_by:
    - &id011
      reference_id: PMID:18854158
      supporting_text: To define the roles of Mre11 in both DNA bridging and nucleolytic processing during
        initiation of DSB repair, we combined small-angle X-ray scattering (SAXS) and crystal structures
        of Pyrococcus furiosus Mre11 dimers bound to DNA with mutational analyses of fission yeast Mre11.
- term: &id026
    id: GO:0000723
    label: telomere maintenance
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  supporting_entities:
  - FB:FBgn0020270
  - PANTHER:PTN000015644
  - PomBase:SPAC13C5.07
  - SGD:S000004837
  - UniProtKB:P49959
  review:
    summary: telomere maintenance is supported.
    action: ACCEPT
    reason: Rad32 associates with fission yeast telomeres by chromatin immunoprecipitation and functions
      with Tel1 in telomere maintenance. Telomeric residence and maintenance are established functions
      of the complex.
    supported_by:
    - &id005
      reference_id: PMID:12196391
      supporting_text: Chromatin immunoprecipitation analyses found that Rad3, Rad1, Rad9, Hus1, Rad17,
        Rad32, and Ku70 associate with telomeres.
    - &id006
      reference_id: PMID:29851556
      supporting_text: These activities require Mre11-Rad50, which localizes to DSBs and bind Tel1 in
        the absence of Nbs1.
- term:
    id: GO:0000723
    label: telomere maintenance
  evidence_type: IGI
  original_reference_id: PMID:12861005
  qualifier: involved_in
  supporting_entities:
  - PomBase:SPAC16A10.07c
  review:
    summary: telomere maintenance is supported.
    action: ACCEPT
    reason: Rad32 associates with fission yeast telomeres by chromatin immunoprecipitation and functions
      with Tel1 in telomere maintenance. Telomeric residence and maintenance are established functions
      of the complex. The original PMID:12861005 annotation is retained at its stated evidential scope;
      accessible source text and the independent evidence cited here are considered together.
    supported_by:
    - *id005
    - *id006
- term: &id019
    id: GO:0000724
    label: double-strand break repair via homologous recombination
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  supporting_entities:
  - MGI:MGI:1100512
  - PANTHER:PTN000015644
  - PomBase:SPAC13C5.07
  - SGD:S000004837
  - UniProtKB:P49959
  review:
    summary: double-strand break repair via homologous recombination is supported.
    action: ACCEPT
    reason: Fission yeast rad32 mutants are defective in physical DSB repair and efficient homologous
      gene conversion. This is a central repair role of MRN, encompassing DNA-end coordination and nuclease-dependent
      removal of end-bound obstacles.
    supported_by:
    - &id007
      reference_id: PMID:7885834
      supporting_text: Pulsed field gel electrophoresis of DNA from irradiated cells indicates that the
        rad32 mutant, in comparison to wild type cells, has decreased ability to repair DNA double strand
        breaks. The mutant also undergoes decreased meiotic recombination and displays reduced stability
        of minichromosomes.
    - &id008
      reference_id: PMID:12628934
      supporting_text: We found that the homologous recombination (HR) genes rhp51(+), rad22A(+), rad32(+)
        and the nucleotide excision repair gene rad16(+) were required for efficient interchromosomal
        gene conversion.
    - &id009
      reference_id: PMID:21931565
      supporting_text: However, Mre11 nuclease and Ctp1 are required to disassociate the MRN complex and
        the Ku70-Ku80 nonhomologous end-joining (NHEJ) complex from DSBs, which is required for efficient
        RPA localization.
- term:
    id: GO:0000724
    label: double-strand break repair via homologous recombination
  evidence_type: IMP
  original_reference_id: PMID:12628934
  qualifier: involved_in
  review:
    summary: double-strand break repair via homologous recombination is supported.
    action: ACCEPT
    reason: Fission yeast rad32 mutants are defective in physical DSB repair and efficient homologous
      gene conversion. This is a central repair role of MRN, encompassing DNA-end coordination and nuclease-dependent
      removal of end-bound obstacles.
    supported_by:
    - *id007
    - *id008
    - *id009
- term: &id018
    id: GO:0000729
    label: DNA double-strand break processing
  evidence_type: IMP
  original_reference_id: PMID:19139281
  qualifier: involved_in
  review:
    summary: DNA double-strand break processing is supported.
    action: ACCEPT
    reason: Mre11/Rad32 and Ctp1 process damaged DNA ends, including removal of covalent Rec12 complexes
      in meiosis and displacement of Ku/MRN to expose DNA for RPA and homologous recombination. The requirement
      for Mre11 protein must be distinguished from the requirement for its nuclease chemistry in particular
      resection assays.
    supported_by:
    - *id003
    - &id010
      reference_id: PMID:19752195
      supporting_text: Rec12-oligonucleotide generation strictly requires Ctp1 (Sae2 nuclease homolog),
        the Rad32 (Mre11) nuclease domain, and Rad50 of the MRN complex.
    - *id009
- term:
    id: GO:0000729
    label: DNA double-strand break processing
  evidence_type: IMP
  original_reference_id: PMID:19752195
  qualifier: involved_in
  review:
    summary: DNA double-strand break processing is supported.
    action: ACCEPT
    reason: Mre11/Rad32 and Ctp1 process damaged DNA ends, including removal of covalent Rec12 complexes
      in meiosis and displacement of Ku/MRN to expose DNA for RPA and homologous recombination. The requirement
      for Mre11 protein must be distinguished from the requirement for its nuclease chemistry in particular
      resection assays.
    supported_by:
    - *id010
    - *id009
- term:
    id: GO:0000729
    label: DNA double-strand break processing
  evidence_type: IMP
  original_reference_id: PMID:19911044
  qualifier: involved_in
  review:
    summary: DNA double-strand break processing is supported.
    action: ACCEPT
    reason: Mre11/Rad32 and Ctp1 process damaged DNA ends, including removal of covalent Rec12 complexes
      in meiosis and displacement of Ku/MRN to expose DNA for RPA and homologous recombination. The requirement
      for Mre11 protein must be distinguished from the requirement for its nuclease chemistry in particular
      resection assays.
    supported_by:
    - reference_id: PMID:19911044
      supporting_text: Ctp1, Rad50, and the nuclease activity of Rad32, the fission yeast homolog of Mre11,
        are required for endonucleolytic Rec12 removal.
    - *id010
    - *id009
- term:
    id: GO:0000729
    label: DNA double-strand break processing
  evidence_type: IMP
  original_reference_id: PMID:21931565
  qualifier: involved_in
  review:
    summary: DNA double-strand break processing is supported.
    action: ACCEPT
    reason: Mre11/Rad32 and Ctp1 process damaged DNA ends, including removal of covalent Rec12 complexes
      in meiosis and displacement of Ku/MRN to expose DNA for RPA and homologous recombination. The requirement
      for Mre11 protein must be distinguished from the requirement for its nuclease chemistry in particular
      resection assays.
    supported_by:
    - *id010
    - *id009
- term:
    id: GO:0000729
    label: DNA double-strand break processing
  evidence_type: IMP
  original_reference_id: PMID:23080121
  qualifier: involved_in
  review:
    summary: DNA double-strand break processing is supported.
    action: ACCEPT
    reason: Mre11/Rad32 and Ctp1 process damaged DNA ends, including removal of covalent Rec12 complexes
      in meiosis and displacement of Ku/MRN to expose DNA for RPA and homologous recombination. The requirement
      for Mre11 protein must be distinguished from the requirement for its nuclease chemistry in particular
      resection assays.
    supported_by:
    - &id012
      reference_id: PMID:23080121
      supporting_text: The equivalent W248R allele in fission yeast allows Mre11 to form an MRN complex
        that efficiently binds double-strand breaks, activates Tel1/ATM and maintains telomeres; yet,
        it causes hypersensitivity to ionizing radiation and collapsed replication forks, increased Rad52
        foci, defective Chk1 signaling and meiotic failure.
    - *id010
    - *id009
- term:
    id: GO:0000781
    label: chromosome, telomeric region
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  supporting_entities:
  - UniProtKB-SubCell:SL-0276
  review:
    summary: chromosome, telomeric region is supported.
    action: ACCEPT
    reason: Rad32 associates with fission yeast telomeres by chromatin immunoprecipitation and functions
      with Tel1 in telomere maintenance. Telomeric residence and maintenance are established functions
      of the complex.
    supported_by:
    - *id005
    - *id006
- term:
    id: GO:0004518
    label: nuclease activity
  evidence_type: IDA
  original_reference_id: PMID:22705791
  qualifier: enables
  review:
    summary: nuclease activity is supported.
    action: ACCEPT
    reason: Mre11 is the conserved phosphodiesterase nuclease of MRN. Purified homolog biochemistry establishes
      DNA endonuclease and 3′-to-5′ exonuclease chemistry; fission yeast catalytic-domain structures and
      nuclease mutants independently establish a functional nuclease. This activity is distinct from the
      net 5′-strand resection produced by the repair pathway.
    supported_by:
    - *id001
    - *id002
    - *id003
- term:
    id: GO:0004519
    label: endonuclease activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  supporting_entities:
  - InterPro:IPR007281
  review:
    summary: endonuclease activity is supported.
    action: ACCEPT
    reason: Mre11 is the conserved phosphodiesterase nuclease of MRN. Purified homolog biochemistry establishes
      DNA endonuclease and 3′-to-5′ exonuclease chemistry; fission yeast catalytic-domain structures and
      nuclease mutants independently establish a functional nuclease. This activity is distinct from the
      net 5′-strand resection produced by the repair pathway.
    supported_by:
    - *id001
    - *id002
    - *id003
- term:
    id: GO:0004520
    label: DNA endonuclease activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  supporting_entities:
  - InterPro:IPR003701
  review:
    summary: DNA endonuclease activity is supported.
    action: ACCEPT
    reason: Mre11 is the conserved phosphodiesterase nuclease of MRN. Purified homolog biochemistry establishes
      DNA endonuclease and 3′-to-5′ exonuclease chemistry; fission yeast catalytic-domain structures and
      nuclease mutants independently establish a functional nuclease. This activity is distinct from the
      net 5′-strand resection produced by the repair pathway.
    supported_by:
    - *id001
    - *id002
    - *id003
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:12944481
  qualifier: enables
  supporting_entities:
  - PomBase:SPBC6B1.09c
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary. The original PMID:12944481 annotation is retained at its stated evidential scope; accessible
      source text and the independent evidence cited here are considered together.
    supported_by:
    - *id002
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:12944481
  qualifier: enables
  supporting_entities:
  - UniProtKB:O43070
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary. The original PMID:12944481 annotation is retained at its stated evidential scope; accessible
      source text and the independent evidence cited here are considered together.
    supported_by:
    - *id002
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:12944482
  qualifier: enables
  supporting_entities:
  - UniProtKB:O43070
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary.
    supported_by:
    - &id013
      reference_id: PMID:12944482
      supporting_text: Fission yeast Nbs1, Rad32 (the homolog of Mre11), and Rad50 are involved in DNA
        damage repair, telomere regulation, and the S-phase DNA damage checkpoint. However, they are not
        required for G(2) DNA damage checkpoint.
    - *id002
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:18854158
  qualifier: enables
  supporting_entities:
  - UniProtKB:O43070
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary.
    supported_by:
    - *id011
    - *id002
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21441914
  qualifier: enables
  supporting_entities:
  - UniProtKB:O43070
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary. The original PMID:21441914 annotation is retained at its stated evidential scope; accessible
      source text and the independent evidence cited here are considered together.
    supported_by:
    - *id002
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22705791
  qualifier: enables
  supporting_entities:
  - PomBase:SPAC13C5.07
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary.
    supported_by:
    - *id002
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22705791
  qualifier: enables
  supporting_entities:
  - PomBase:SPBC6B1.09c
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary.
    supported_by:
    - *id002
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22705791
  qualifier: enables
  supporting_entities:
  - UniProtKB:O43070
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary.
    supported_by:
    - *id002
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23080121
  qualifier: enables
  supporting_entities:
  - PomBase:SPBC6B1.09c
  review:
    summary: protein binding is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic
      protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function
      summary.
    supported_by:
    - *id012
    - *id002
- term: &id028
    id: GO:0005634
    label: nucleus
  evidence_type: EXP
  original_reference_id: PMID:12944482
  qualifier: located_in
  review:
    summary: nucleus is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id013
    - *id012
    - *id006
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  supporting_entities:
  - InterPro:IPR007281
  - UniProtKB-SubCell:SL-0191
  review:
    summary: nucleus is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id012
    - *id006
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: NAS
  original_reference_id: PMID:22705791
  qualifier: located_in
  review:
    summary: nucleus is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id002
    - *id012
    - *id006
- term:
    id: GO:0005694
    label: chromosome
  evidence_type: EXP
  original_reference_id: PMID:23080121
  qualifier: located_in
  review:
    summary: chromosome is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id012
    - *id006
- term:
    id: GO:0005694
    label: chromosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  supporting_entities:
  - UniProtKB-SubCell:SL-0468
  review:
    summary: chromosome is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id012
    - *id006
- term: &id024
    id: GO:0006302
    label: double-strand break repair
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  supporting_entities:
  - InterPro:IPR003701
  - InterPro:IPR007281
  review:
    summary: double-strand break repair is supported.
    action: ACCEPT
    reason: Fission yeast rad32 mutants are defective in physical DSB repair and efficient homologous
      gene conversion. This is a central repair role of MRN, encompassing DNA-end coordination and nuclease-dependent
      removal of end-bound obstacles.
    supported_by:
    - *id007
    - *id008
    - *id009
- term:
    id: GO:0006302
    label: double-strand break repair
  evidence_type: IMP
  original_reference_id: PMID:7885834
  qualifier: involved_in
  review:
    summary: double-strand break repair is supported.
    action: ACCEPT
    reason: Fission yeast rad32 mutants are defective in physical DSB repair and efficient homologous
      gene conversion. This is a central repair role of MRN, encompassing DNA-end coordination and nuclease-dependent
      removal of end-bound obstacles.
    supported_by:
    - *id007
    - *id008
    - *id009
- term:
    id: GO:0006302
    label: double-strand break repair
  evidence_type: NAS
  original_reference_id: PMID:22705791
  qualifier: involved_in
  review:
    summary: double-strand break repair is supported.
    action: ACCEPT
    reason: Fission yeast rad32 mutants are defective in physical DSB repair and efficient homologous
      gene conversion. This is a central repair role of MRN, encompassing DNA-end coordination and nuclease-dependent
      removal of end-bound obstacles.
    supported_by:
    - *id002
    - *id007
    - *id008
    - *id009
- term:
    id: GO:0006303
    label: double-strand break repair via nonhomologous end joining
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  supporting_entities:
  - PANTHER:PTN000015644
  - PomBase:SPAC13C5.07
  - SGD:S000004837
  - UniProtKB:P49959
  review:
    summary: double-strand break repair via nonhomologous end joining is supported.
    action: ACCEPT
    reason: Fission yeast experiments support an MRN contribution to nonhomologous end joining, especially
      tethering dysfunctional telomeres or nonligatable hairpin-ended substrates. This does not imply
      its nuclease activity is required for every NHEJ reaction.
    supported_by:
    - &id014
      reference_id: PMID:23188080
      supporting_text: Thus, MRN acts to tether unlinked DNA ends, allowing for efficient NHEJ.
    - &id015
      reference_id: PMID:28292918
      supporting_text: S. pombe NHEJ was reduced >1000-fold in cells lacking each MRN subunit, and loss
        of MRN-associated Ctp1 caused a 30-fold reduction.
- term:
    id: GO:0006303
    label: double-strand break repair via nonhomologous end joining
  evidence_type: IGI
  original_reference_id: PMID:23188080
  qualifier: involved_in
  supporting_entities:
  - PomBase:SPAC16A10.07c
  review:
    summary: double-strand break repair via nonhomologous end joining is supported.
    action: ACCEPT
    reason: Fission yeast experiments support an MRN contribution to nonhomologous end joining, especially
      tethering dysfunctional telomeres or nonligatable hairpin-ended substrates. This does not imply
      its nuclease activity is required for every NHEJ reaction.
    supported_by:
    - *id014
    - *id015
- term:
    id: GO:0006303
    label: double-strand break repair via nonhomologous end joining
  evidence_type: IMP
  original_reference_id: PMID:10373582
  qualifier: involved_in
  review:
    summary: double-strand break repair via nonhomologous end joining is supported.
    action: ACCEPT
    reason: Fission yeast experiments support an MRN contribution to nonhomologous end joining, especially
      tethering dysfunctional telomeres or nonligatable hairpin-ended substrates. This does not imply
      its nuclease activity is required for every NHEJ reaction. The original PMID:10373582 annotation
      is retained at its stated evidential scope; accessible source text and the independent evidence
      cited here are considered together.
    supported_by:
    - *id014
    - *id015
- term:
    id: GO:0006303
    label: double-strand break repair via nonhomologous end joining
  evidence_type: IMP
  original_reference_id: PMID:23188080
  qualifier: involved_in
  review:
    summary: double-strand break repair via nonhomologous end joining is supported.
    action: ACCEPT
    reason: Fission yeast experiments support an MRN contribution to nonhomologous end joining, especially
      tethering dysfunctional telomeres or nonligatable hairpin-ended substrates. This does not imply
      its nuclease activity is required for every NHEJ reaction.
    supported_by:
    - *id014
    - *id015
- term:
    id: GO:0006303
    label: double-strand break repair via nonhomologous end joining
  evidence_type: IMP
  original_reference_id: PMID:28292918
  qualifier: involved_in
  review:
    summary: double-strand break repair via nonhomologous end joining is supported.
    action: ACCEPT
    reason: Fission yeast experiments support an MRN contribution to nonhomologous end joining, especially
      tethering dysfunctional telomeres or nonligatable hairpin-ended substrates. This does not imply
      its nuclease activity is required for every NHEJ reaction.
    supported_by:
    - *id014
    - *id015
- term:
    id: GO:0007095
    label: mitotic G2 DNA damage checkpoint signaling
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  supporting_entities:
  - FB:FBgn0020270
  - MGI:MGI:1100512
  - PANTHER:PTN000015644
  review:
    summary: mitotic G2 DNA damage checkpoint signaling is not fully resolved.
    action: UNDECIDED
    reason: The conserved checkpoint inference needs phase-specific resolution in fission yeast. PMID:12944482
      reports that Rad32/Rad50/Nbs1 are required for the S-phase checkpoint but not the G2 checkpoint,
      whereas PMID:23080121 reports defective Chk1 signaling for a separation-of-function Mre11 allele.
      These assay contexts do not yet justify an unqualified G2-checkpoint assignment or a blanket rejection.
    supported_by:
    - *id013
    - *id012
- term:
    id: GO:0007131
    label: reciprocal meiotic recombination
  evidence_type: IMP
  original_reference_id: PMID:7885834
  qualifier: involved_in
  review:
    summary: reciprocal meiotic recombination is supported.
    action: ACCEPT
    reason: Rad32 is required for efficient meiotic recombination and repair of meiotic DNA breaks. Removal
      of Rec12-linked DNA ends is a mechanistically supported contribution; the protein does not catalyze
      strand exchange itself.
    supported_by:
    - *id007
    - &id016
      reference_id: PMID:15238514
      supporting_text: Meiotic DNA breakage in Schizosaccharomyces pombe did not require Rad50 or Rad32,
        although the homologs Rad50 and Mre11 are required in Saccharomyces cerevisiae; these proteins
        are required for meiotic DNA break repair in both yeasts.
    - *id003
- term:
    id: GO:0008296
    label: 3'-5'-DNA exonuclease activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  supporting_entities:
  - InterPro:IPR003701
  review:
    summary: 3'-5'-DNA exonuclease activity is supported.
    action: ACCEPT
    reason: Mre11 is the conserved phosphodiesterase nuclease of MRN. Purified homolog biochemistry establishes
      DNA endonuclease and 3′-to-5′ exonuclease chemistry; fission yeast catalytic-domain structures and
      nuclease mutants independently establish a functional nuclease. This activity is distinct from the
      net 5′-strand resection produced by the repair pathway.
    supported_by:
    - *id001
    - *id002
    - *id003
- term: &id025
    id: GO:0008311
    label: double-stranded DNA 3'-5' DNA exonuclease activity
  evidence_type: ISO
  original_reference_id: PMID:9651580
  qualifier: enables
  supporting_entities:
  - UniProtKB:P49959
  review:
    summary: double-stranded DNA 3'-5' DNA exonuclease activity is supported.
    action: ACCEPT
    reason: Mre11 is the conserved phosphodiesterase nuclease of MRN. Purified homolog biochemistry establishes
      DNA endonuclease and 3′-to-5′ exonuclease chemistry; fission yeast catalytic-domain structures and
      nuclease mutants independently establish a functional nuclease. This activity is distinct from the
      net 5′-strand resection produced by the repair pathway.
    supported_by:
    - *id001
    - *id002
    - *id003
- term:
    id: GO:0016787
    label: hydrolase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  supporting_entities:
  - InterPro:IPR004843
  review:
    summary: hydrolase activity is supported.
    action: ACCEPT
    reason: Mre11 is the conserved phosphodiesterase nuclease of MRN. Purified homolog biochemistry establishes
      DNA endonuclease and 3′-to-5′ exonuclease chemistry; fission yeast catalytic-domain structures and
      nuclease mutants independently establish a functional nuclease. This activity is distinct from the
      net 5′-strand resection produced by the repair pathway.
    supported_by:
    - *id001
    - *id002
    - *id003
- term:
    id: GO:0030145
    label: manganese ion binding
  evidence_type: IDA
  original_reference_id: PMID:22705791
  qualifier: enables
  review:
    summary: manganese ion binding is supported.
    action: ACCEPT
    reason: The Mre11 catalytic phosphodiesterase domain binds divalent metal ions, with manganese represented
      in the target-specific structural and biochemical work. Metal binding is a cofactor property of
      the nuclease rather than a separate physiological pathway.
    supported_by:
    - *id002
    - *id004
- term:
    id: GO:0030145
    label: manganese ion binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  supporting_entities:
  - InterPro:IPR007281
  review:
    summary: manganese ion binding is supported.
    action: ACCEPT
    reason: The Mre11 catalytic phosphodiesterase domain binds divalent metal ions, with manganese represented
      in the target-specific structural and biochemical work. Metal binding is a cofactor property of
      the nuclease rather than a separate physiological pathway.
    supported_by:
    - *id002
    - *id004
- term: &id022
    id: GO:0030870
    label: Mre11 complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  supporting_entities:
  - FB:FBgn0020270
  - MGI:MGI:1100512
  - PANTHER:PTN000015644
  - PomBase:SPAC13C5.07
  - SGD:S000004837
  - UniProtKB:P49959
  - UniProtKB:Q9W6K1
  review:
    summary: Mre11 complex is supported.
    action: ACCEPT
    reason: Fission yeast structural analysis directly resolves Mre11 dimer association with Nbs1; genetics
      and biochemical analysis establish Mre11 as the catalytic core of MRN.
    supported_by:
    - *id002
    - *id013
- term:
    id: GO:0030870
    label: Mre11 complex
  evidence_type: IDA
  original_reference_id: PMID:22705791
  qualifier: part_of
  review:
    summary: Mre11 complex is supported.
    action: ACCEPT
    reason: Fission yeast structural analysis directly resolves Mre11 dimer association with Nbs1; genetics
      and biochemical analysis establish Mre11 as the catalytic core of MRN.
    supported_by:
    - *id002
    - *id013
- term:
    id: GO:0030870
    label: Mre11 complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: part_of
  supporting_entities:
  - ARBA:ARBA00088211
  - InterPro:IPR003701
  review:
    summary: Mre11 complex is supported.
    action: ACCEPT
    reason: Fission yeast structural analysis directly resolves Mre11 dimer association with Nbs1; genetics
      and biochemical analysis establish Mre11 as the catalytic core of MRN.
    supported_by:
    - *id002
    - *id013
- term:
    id: GO:0030870
    label: Mre11 complex
  evidence_type: NAS
  original_reference_id: PMID:22705791
  qualifier: part_of
  review:
    summary: Mre11 complex is supported.
    action: ACCEPT
    reason: Fission yeast structural analysis directly resolves Mre11 dimer association with Nbs1; genetics
      and biochemical analysis establish Mre11 as the catalytic core of MRN.
    supported_by:
    - *id002
    - *id013
- term: &id027
    id: GO:0031573
    label: mitotic intra-S DNA damage checkpoint signaling
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  supporting_entities:
  - MGI:MGI:1100512
  - PANTHER:PTN000015646
  - PomBase:SPAC13C5.07
  review:
    summary: mitotic intra-S DNA damage checkpoint signaling is supported.
    action: ACCEPT
    reason: The original fission yeast study explicitly establishes the Rad32-MRN requirement for the
      S-phase DNA damage checkpoint. This phase-specific signaling role is experimentally grounded.
    supported_by:
    - *id013
- term:
    id: GO:0031573
    label: mitotic intra-S DNA damage checkpoint signaling
  evidence_type: IMP
  original_reference_id: PMID:12944482
  qualifier: involved_in
  review:
    summary: mitotic intra-S DNA damage checkpoint signaling is supported.
    action: ACCEPT
    reason: The original fission yeast study explicitly establishes the Rad32-MRN requirement for the
      S-phase DNA damage checkpoint. This phase-specific signaling role is experimentally grounded.
    supported_by:
    - *id013
- term: &id023
    id: GO:0035861
    label: site of double-strand break
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  supporting_entities:
  - PANTHER:PTN000015644
  - PomBase:SPAC13C5.07
  - UniProtKB:P49959
  review:
    summary: site of double-strand break is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id012
    - *id006
- term:
    id: GO:0035861
    label: site of double-strand break
  evidence_type: IDA
  original_reference_id: PMID:17936710
  qualifier: is_active_in
  review:
    summary: site of double-strand break is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location. The original PMID:17936710
      annotation is retained at its stated evidential scope; accessible source text and the independent
      evidence cited here are considered together.
    supported_by:
    - *id012
    - *id006
- term:
    id: GO:0035861
    label: site of double-strand break
  evidence_type: IDA
  original_reference_id: PMID:19804755
  qualifier: is_active_in
  review:
    summary: site of double-strand break is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location. The original PMID:19804755
      annotation is retained at its stated evidential scope; accessible source text and the independent
      evidence cited here are considered together.
    supported_by:
    - *id012
    - *id006
- term:
    id: GO:0035861
    label: site of double-strand break
  evidence_type: IDA
  original_reference_id: PMID:21931565
  qualifier: is_active_in
  review:
    summary: site of double-strand break is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id009
    - *id012
    - *id006
- term:
    id: GO:0035861
    label: site of double-strand break
  evidence_type: IDA
  original_reference_id: PMID:23080121
  qualifier: is_active_in
  review:
    summary: site of double-strand break is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id012
    - *id006
- term:
    id: GO:0035861
    label: site of double-strand break
  evidence_type: IDA
  original_reference_id: PMID:29851556
  qualifier: is_active_in
  review:
    summary: site of double-strand break is supported.
    action: ACCEPT
    reason: The Mre11 complex binds chromosomal DNA breaks and functions in nuclear DNA repair. Target-specific
      recruitment and separation-of-function mutants support this cellular location.
    supported_by:
    - *id012
    - *id006
- term:
    id: GO:0042138
    label: meiotic DNA double-strand break formation
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  supporting_entities:
  - PANTHER:PTN000015644
  - PomBase:SPAC13C5.07
  - SGD:S000004837
  review:
    summary: meiotic DNA double-strand break formation is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Fission yeast MRN can generate meiotic breaks at a palindrome through a Rec12-independent
      pathway during premeiotic replication. The experimental assertion is sound in this specialized context.
      Ordinary Rec12-dependent meiotic break formation does not require Rad32, so this should not imply
      a universal upstream requirement for programmed meiotic DSB formation.
    supported_by:
    - &id017
      reference_id: PMID:15654094
      supporting_text: We show that MRN-dependent DSBs are formed at or near the M-pal in vivo, and in
        contrast to the Rec12-dependent breaks, they appear early, during premeiotic replication.
    - *id016
- term:
    id: GO:0042138
    label: meiotic DNA double-strand break formation
  evidence_type: IMP
  original_reference_id: PMID:15654094
  qualifier: involved_in
  review:
    summary: meiotic DNA double-strand break formation is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Fission yeast MRN can generate meiotic breaks at a palindrome through a Rec12-independent
      pathway during premeiotic replication. The experimental assertion is sound in this specialized context.
      Ordinary Rec12-dependent meiotic break formation does not require Rad32, so this should not imply
      a universal upstream requirement for programmed meiotic DSB formation.
    supported_by:
    - *id017
    - *id016
- term:
    id: GO:0042138
    label: meiotic DNA double-strand break formation
  evidence_type: NAS
  original_reference_id: PMID:22705791
  qualifier: involved_in
  review:
    summary: meiotic DNA double-strand break formation is retained as an ancillary annotation.
    action: KEEP_AS_NON_CORE
    reason: Fission yeast MRN can generate meiotic breaks at a palindrome through a Rec12-independent
      pathway during premeiotic replication. The experimental assertion is sound in this specialized context.
      Ordinary Rec12-dependent meiotic break formation does not require Rad32, so this should not imply
      a universal upstream requirement for programmed meiotic DSB formation.
    supported_by:
    - *id002
    - *id017
    - *id016
- term:
    id: GO:0045027
    label: DNA end binding
  evidence_type: ISO
  original_reference_id: PMID:18854158
  qualifier: enables
  supporting_entities:
  - UniProtKB:Q8U1N9
  review:
    summary: DNA end binding is supported.
    action: ACCEPT
    reason: DNA-complex structures resolve how the conserved Mre11 dimer engages branched substrates and
      DNA ends. Fission yeast mutational analysis links this architecture to MRN assembly and break repair,
      supporting the curated orthology transfer rather than a claim of a target-only binding assay.
    supported_by:
    - *id011
- term:
    id: GO:0097552
    label: mitochondrial double-strand break repair via homologous recombination
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  supporting_entities:
  - PANTHER:PTN000015644
  - SGD:S000004837
  review:
    summary: mitochondrial double-strand break repair via homologous recombination is not fully resolved.
    action: UNDECIDED
    reason: A mitochondrial homologous-recombination repair role is a distinct compartment-specific assertion.
      The reviewed fission yeast literature establishes nuclear MRN repair but does not resolve mitochondrial
      targeting or mitochondrial repair by Rad32. The ancestral placement underlying this IBA requires
      additional investigation; nuclear function alone neither validates nor refutes it.
    supported_by:
    - *id007
- term:
    id: GO:0140445
    label: chromosome, telomeric repeat region
  evidence_type: IDA
  original_reference_id: PMID:12196391
  qualifier: is_active_in
  review:
    summary: chromosome, telomeric repeat region is supported.
    action: ACCEPT
    reason: Rad32 associates with fission yeast telomeres by chromatin immunoprecipitation and functions
      with Tel1 in telomere maintenance. Telomeric residence and maintenance are established functions
      of the complex.
    supported_by:
    - *id005
    - *id006
- term:
    id: GO:0140445
    label: chromosome, telomeric repeat region
  evidence_type: IDA
  original_reference_id: PMID:12861005
  qualifier: is_active_in
  review:
    summary: chromosome, telomeric repeat region is supported.
    action: ACCEPT
    reason: Rad32 associates with fission yeast telomeres by chromatin immunoprecipitation and functions
      with Tel1 in telomere maintenance. Telomeric residence and maintenance are established functions
      of the complex. The original PMID:12861005 annotation is retained at its stated evidential scope;
      accessible source text and the independent evidence cited here are considered together.
    supported_by:
    - *id005
    - *id006
- term: &id020
    id: GO:1990918
    label: double-strand break repair involved in meiotic recombination
  evidence_type: IMP
  original_reference_id: PMID:15238514
  qualifier: involved_in
  review:
    summary: double-strand break repair involved in meiotic recombination is supported.
    action: ACCEPT
    reason: Rad32 is required for efficient meiotic recombination and repair of meiotic DNA breaks. Removal
      of Rec12-linked DNA ends is a mechanistically supported contribution; the protein does not catalyze
      strand exchange itself.
    supported_by:
    - *id007
    - *id016
    - *id003
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,
    accompanied by conservative changes to GO terms applied by UniProt
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:10373582
  title: The role of Schizosaccharomyces pombe Rad32, the Mre11 homologue, and other DNA damage response
    proteins in non-homologous end joining and telomere length maintenance.
  findings: []
  full_text_unavailable: true
- id: PMID:12196391
  title: Telomere binding of checkpoint sensor and DNA repair proteins contributes to maintenance of functional
    fission yeast telomeres.
  findings: []
  full_text_unavailable: true
- id: PMID:12628934
  title: Pathway utilization in response to a site-specific DNA double-strand break in fission yeast.
  findings: []
  full_text_unavailable: false
- id: PMID:12861005
  title: Competition between the Rad50 complex and the Ku heterodimer reveals a role for Exo1 in processing
    double-strand breaks but not telomeres.
  findings: []
  full_text_unavailable: true
- id: PMID:12944481
  title: Molecular characterization of the Schizosaccharomyces pombe nbs1+ gene involved in DNA repair
    and telomere maintenance.
  findings: []
  full_text_unavailable: true
- id: PMID:12944482
  title: The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint.
  findings: []
  full_text_unavailable: true
- id: PMID:15238514
  title: Conserved and nonconserved proteins for meiotic DNA breakage and repair in yeasts.
  findings: []
  full_text_unavailable: true
- id: PMID:15654094
  title: A novel recombination pathway initiated by the Mre11/Rad50/Nbs1 complex eliminates palindromes
    during meiosis in Schizosaccharomyces pombe.
  findings: []
  full_text_unavailable: true
- id: PMID:17936710
  title: Ctp1 is a cell-cycle-regulated protein that functions with Mre11 complex to control double-strand
    break repair by homologous recombination.
  findings: []
  full_text_unavailable: true
- id: PMID:18854158
  title: Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair.
  findings: []
  full_text_unavailable: false
- id: PMID:19139281
  title: Ctp1CtIP and Rad32Mre11 nuclease activity are required for Rec12Spo11 removal, but Rec12Spo11
    removal is dispensable for other MRN-dependent meiotic functions.
  findings: []
  full_text_unavailable: true
- id: PMID:19752195
  title: Meiotic DNA double-strand break repair requires two nucleases, MRN and Ctp1, to produce a single
    size class of Rec12 (Spo11)-oligonucleotide complexes.
  findings: []
  full_text_unavailable: true
- id: PMID:19804755
  title: Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and
    repair.
  findings: []
  full_text_unavailable: false
- id: PMID:19911044
  title: Ctp1 and the MRN-complex are required for endonucleolytic Rec12 removal with release of a single
    class of oligonucleotides in fission yeast.
  findings: []
  full_text_unavailable: false
- id: PMID:21441914
  title: ABC ATPase signature helices in Rad50 link nucleotide state to Mre11 interface for DNA repair.
  findings: []
  full_text_unavailable: false
- id: PMID:21931565
  title: Release of Ku and MRN from DNA ends by Mre11 nuclease activity and Ctp1 is required for homologous
    recombination repair of double-strand breaks.
  findings: []
  full_text_unavailable: false
- id: PMID:22705791
  title: Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations
    and DNA damage signaling.
  findings: []
  full_text_unavailable: false
- id: PMID:23080121
  title: Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair.
  findings: []
  full_text_unavailable: false
- id: PMID:23188080
  title: The fission yeast MRN complex tethers dysfunctional telomeres for NHEJ repair.
  findings: []
  full_text_unavailable: true
- id: PMID:28292918
  title: Nonhomologous End-Joining with Minimal Sequence Loss Is Promoted by the Mre11-Rad50-Nbs1-Ctp1
    Complex in Schizosaccharomyces pombe.
  findings: []
  full_text_unavailable: true
- id: PMID:29851556
  title: Mre11-Rad50-dependent activity of ATM/Tel1 at DNA breaks and telomeres in the absence of Nbs1.
  findings: []
  full_text_unavailable: false
- id: PMID:7885834
  title: 'Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene: a gene required for
    repair of double strand breaks and recombination.'
  findings: []
  full_text_unavailable: true
- id: PMID:9651580
  title: The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks.
  findings: []
  full_text_unavailable: true
- id: PMID:9705271
  title: Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11,
    and p95.
  full_text_unavailable: true
core_functions:
- description: DNA-end nuclease and coordinating subunit of MRN supporting double-strand break processing
    and repair.
  supported_by:
  - *id002
  - *id003
  - *id008
  - *id004
  directly_involved_in:
  - *id018
  - *id019
  - *id020
  molecular_function: *id021
  in_complex: *id022
  locations:
  - *id023
- description: Conserved double-stranded DNA 3′-to-5′ exonuclease chemistry of the Mre11 nuclease domain.
  supported_by:
  - *id001
  - *id002
  directly_involved_in:
  - *id024
  molecular_function: *id025
  in_complex: *id022
- description: MRN supports telomere maintenance and S-phase checkpoint signaling through DNA-end recognition
    and complex organization.
  supported_by:
  - *id005
  - *id013
  directly_involved_in:
  - *id026
  - *id027
  in_complex: *id022
  locations:
  - *id028