CDC16_CAEEL
ID CDC16_CAEEL Reviewed; 655 AA.
AC G5EG38;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cell division cycle protein 16 homolog {ECO:0000305};
DE AltName: Full=Abnormal embryogenesis protein 27 {ECO:0000312|WormBase:F10B5.6};
DE AltName: Full=Anaphase-promoting complex subunit 6 {ECO:0000305};
DE Short=APC6 {ECO:0000312|EMBL:AAG41979.1};
GN Name=emb-27 {ECO:0000312|WormBase:F10B5.6};
GN Synonyms=apc-6 {ECO:0000312|WormBase:F10B5.6},
GN pod-6 {ECO:0000312|WormBase:F10B5.6};
GN ORFNames=F10B5.6 {ECO:0000312|WormBase:F10B5.6};
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|EMBL:AAG41979.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF HIS-332.
RX PubMed=11134076; DOI=10.1083/jcb.151.7.1469;
RA Golden A., Sadler P.L., Wallenfang M.R., Schumacher J.M., Hamill D.R.,
RA Bates G., Bowerman B., Seydoux G., Shakes D.C.;
RT "Metaphase to anaphase (mat) transition-defective mutants in Caenorhabditis
RT elegans.";
RL J. Cell Biol. 151:1469-1482(2000).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=11832245; DOI=10.1016/s1534-5807(02)00114-4;
RA Rappleye C.A., Tagawa A., Lyczak R., Bowerman B., Aroian R.V.;
RT "The anaphase-promoting complex and separin are required for embryonic
RT anterior-posterior axis formation.";
RL Dev. Cell 2:195-206(2002).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15556870; DOI=10.1016/j.cub.2004.11.010;
RA Juo P., Kaplan J.M.;
RT "The anaphase-promoting complex regulates the abundance of GLR-1 glutamate
RT receptors in the ventral nerve cord of C. elegans.";
RL Curr. Biol. 14:2057-2062(2004).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24321454; DOI=10.1016/j.mcn.2013.12.001;
RA Kowalski J.R., Dube H., Touroutine D., Rush K.M., Goodwin P.R., Carozza M.,
RA Didier Z., Francis M.M., Juo P.;
RT "The anaphase-promoting complex (APC) ubiquitin ligase regulates GABA
RT transmission at the C. elegans neuromuscular junction.";
RL Mol. Cell. Neurosci. 58:62-75(2014).
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 (By similarity). The APC/C complex acts by mediating
CC ubiquitination and subsequent degradation of target proteins (By
CC similarity). Developmental role in early embryogenesis and the
CC metaphase to anaphase transition in oocyte and spermatocyte meiosis and
CC mitosis in germ cells (PubMed:11134076). Required for embryonic
CC anterior-posterior axis formation (PubMed:11832245). Plays a role in
CC regulating the abundance of glr-1 receptors in postmitotic neurons,
CC which may in turn control animal locomotion (PubMed:15556870). Involved
CC in regulating GABA neurotransmitter release at neuromuscular junctions
CC in GABA motor neurons (PubMed:24321454). {ECO:0000250|UniProtKB:Q13042,
CC ECO:0000269|PubMed:11134076, ECO:0000269|PubMed:11832245,
CC ECO:0000269|PubMed:15556870, ECO:0000269|PubMed:24321454}.
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:24321454}.
CC Synapse {ECO:0000269|PubMed:24321454}.
CC -!- TISSUE SPECIFICITY: Expressed in GABA motor neurons.
CC {ECO:0000269|PubMed:24321454}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results arrest at the
CC one-cell stage of embryogenesis. {ECO:0000269|PubMed:11134076}.
CC -!- SIMILARITY: Belongs to the APC6/CDC16 family. {ECO:0000305}.
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DR EMBL; AF314467; AAG41979.1; -; mRNA.
DR EMBL; Z48334; CAA88313.1; -; Genomic_DNA.
DR PIR; T20693; T20693.
DR RefSeq; NP_495712.1; NM_063311.7.
DR AlphaFoldDB; G5EG38; -.
DR SMR; G5EG38; -.
DR ComplexPortal; CPX-3382; Anaphase Promoting Complex/Cyclosome.
DR IntAct; G5EG38; 1.
DR STRING; 6239.F10B5.6; -.
DR EPD; G5EG38; -.
DR PaxDb; G5EG38; -.
DR PeptideAtlas; G5EG38; -.
DR PRIDE; G5EG38; -.
DR EnsemblMetazoa; F10B5.6.1; F10B5.6.1; WBGene00001281.
DR GeneID; 174314; -.
DR KEGG; cel:CELE_F10B5.6; -.
DR CTD; 174314; -.
DR WormBase; F10B5.6; CE01548; WBGene00001281; emb-27.
DR eggNOG; KOG1173; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_029222_0_0_1; -.
DR InParanoid; G5EG38; -.
DR OMA; EHEQAMN; -.
DR OrthoDB; 905026at2759; -.
DR PhylomeDB; G5EG38; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:G5EG38; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001281; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0030703; P:eggshell formation; IMP:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:UniProtKB.
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 Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell junction; Developmental protein; Meiosis;
KW Mitosis; Neurotransmitter transport; Reference proteome; Repeat; Synapse;
KW TPR repeat; Transport; Ubl conjugation pathway.
FT CHAIN 1..655
FT /note="Cell division cycle protein 16 homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435329"
FT REPEAT 44..77
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 203..236
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 342..375
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 376..409
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 495..528
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 530..562
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 332
FT /note="H->Y: In emb-27(g48); temperature sensitive mutant.
FT Embryos arrest at the one-cell stage of embryogenesis."
FT /evidence="ECO:0000269|PubMed:11134076"
SQ SEQUENCE 655 AA; 75153 MW; DB6E121AC7151209 CRC64;
MSAISPDTKS FAIPTLADEG SSSKPASSLD LPKHESIRFK PIKTLASRID GSEYYDEASM
EKVMEMLEIG RTDEAVAYAD TLYSNIIDDE QQDIVTIAEY VKILVVLRQW RRISHIIARG
NYHQIHIVFA YYAATALFQR KLYEDVAELS VGHLLPSNGQ IGPLPVRTLS QVTGRYVEEE
RMKYSFANMA ELDNSSKKLR MVPALMITIA ESFLKLMNRD AAMICINYAL SLDNTTLHVE
RLMAKYNLVE PAMWEKYRKV RNEQLKLHEG NHDPRILMER AQRAYEMGRF RETKKITDEL
FDLFGPHPEC IILRIHCLTM LKDSRSLLEL GHQLVSDDPH IPLPWYCVAM YYYSIGANSR
ARNFISKCTM MDSTFAEGWV AFGHILHYEV EHEQSMSCYY RASKLVDKSS EPFLYTSLQY
STHSQKLSKK FMGEAVARAP NDPLIRHEEA CVAYTAKSYA EADILFRTVL YMVTETDEII
PIEEVLKKKI DDFWHPMLNN IGHIARRQGR LNEAIMFYQK AIRMEPKFVD AIASTALCYA
VLGNIDKATE FFNKALAIDP FNETIRQCLS KMIQASKESY SVDQQTLPPA YNSETYFGAQ
EILPYCAIRK PRNDGFVVPS IVSSSQPFMS MLRDRLRRQD QLYAQEPDND AGNQV
