APC11_CAEEL
ID APC11_CAEEL Reviewed; 135 AA.
AC Q20052;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Anaphase-promoting complex subunit 11 {ECO:0000312|WormBase:F35G12.9};
DE Short=APC11 {ECO:0000250|UniProtKB:Q9NYG5};
GN Name=apc-11 {ECO:0000312|WormBase:F35G12.9};
GN ORFNames=F35G12.9 {ECO:0000312|WormBase:F35G12.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11861581; DOI=10.1093/genetics/160.2.805;
RA Davis E.S., Wille L., Chestnut B.A., Sadler P.L., Shakes D.C., Golden A.;
RT "Multiple subunits of the Caenorhabditis elegans anaphase-promoting complex
RT are required for chromosome segregation during meiosis I.";
RL Genetics 160:805-813(2002).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UBC-2, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-100.
RX PubMed=15466891; DOI=10.1242/jcs.01417;
RA Frazier T., Shakes D., Hota U., Boyd L.;
RT "Caenorhabditis elegans UBC-2 functions with the anaphase-promoting complex
RT but also has other activities.";
RL J. Cell Sci. 117:5427-5435(2004).
CC -!- FUNCTION: Probable component of the anaphase promoting
CC complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase
CC that controls progression through mitosis and the G1 phase of the cell
CC cycle (PubMed:11861581). The APC/C complex acts by mediating
CC ubiquitination and subsequent degradation of target proteins
CC (PubMed:11861581). Developmental role in early embryogenesis and the
CC metaphase to anaphase transition in meiosis and mitosis
CC (PubMed:11861581). In vitro, recruits the ubiquitin-conjugating enzyme
CC ubc-2 to exert ubiquitin ligase activity (PubMed:15466891).
CC {ECO:0000269|PubMed:11861581, ECO:0000269|PubMed:15466891}.
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: The APC/C complex is probably composed of at least 12
CC subunits: apc-2, apc-10, apc-11, cdc-26, emb-1, emb-27, emb-30, mat-1,
CC mat-2, mat-3, such-1 and gfi-3 (Probable). Interacts with ubc-2
CC (PubMed:15466891). {ECO:0000269|PubMed:15466891, ECO:0000305}.
CC -!- INTERACTION:
CC Q20052; P34514: apc-2; NbExp=8; IntAct=EBI-314913, EBI-321211;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NYG5}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown is embryonic lethal with
CC the display of a meiotic metaphase-to-anaphase defective phenotype
CC marked by arrest at meiosis I at the one-cell stage of embryogenesis.
CC {ECO:0000269|PubMed:11861581, ECO:0000269|PubMed:15466891}.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
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DR EMBL; Z46242; CAA86328.1; -; Genomic_DNA.
DR PIR; T21802; T21802.
DR RefSeq; NP_497937.1; NM_065536.5.
DR AlphaFoldDB; Q20052; -.
DR SMR; Q20052; -.
DR ComplexPortal; CPX-3382; Anaphase Promoting Complex/Cyclosome.
DR DIP; DIP-24995N; -.
DR IntAct; Q20052; 10.
DR STRING; 6239.F35G12.9; -.
DR EPD; Q20052; -.
DR PaxDb; Q20052; -.
DR PeptideAtlas; Q20052; -.
DR EnsemblMetazoa; F35G12.9.1; F35G12.9.1; WBGene00000145.
DR GeneID; 175604; -.
DR KEGG; cel:CELE_F35G12.9; -.
DR UCSC; F35G12.9; c. elegans.
DR CTD; 175604; -.
DR WormBase; F35G12.9; CE00978; WBGene00000145; apc-11.
DR eggNOG; KOG1493; Eukaryota.
DR GeneTree; ENSGT00550000075186; -.
DR HOGENOM; CLU_115512_0_2_1; -.
DR InParanoid; Q20052; -.
DR OMA; ECPIAIG; -.
DR OrthoDB; 1587140at2759; -.
DR PhylomeDB; Q20052; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q20052; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000145; Expressed in embryo and 4 other tissues.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:1904666; P:regulation of ubiquitin protein ligase activity; IC:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:WormBase.
DR CDD; cd16456; RING-H2_APC11; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR024991; RING-H2_APC11.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12861; zf-ANAPC11; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Developmental protein; Meiosis; Metal-binding;
KW Mitosis; Nucleus; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..135
FT /note="Anaphase-promoting complex subunit 11"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435326"
FT ZN_FING 83..128
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 100
FT /note="C->L: Loss of ubiquitination activity."
FT /evidence="ECO:0000269|PubMed:15466891"
SQ SEQUENCE 135 AA; 15513 MW; 1CC8B4AF1AB671E7 CRC64;
MEQQIQMDEQ ENDESQGNDD QQNMSMSSSE LHTMQDDHPG ILLKTNTRMS ITVKKLHVCG
EWKWLQGGED TCGICRMEFE SACNMCKFPG DDCPLVLGIC RHAFHRHCID KWIAAPTNQP
RAQCPLCRQD WTIVE
