CDC27_CAEEL
ID CDC27_CAEEL Reviewed; 788 AA.
AC Q9N593; Q6AW18; Q8T4K4;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cell division cycle protein 27 homolog {ECO:0000250|UniProtKB:P30260};
DE AltName: Full=Anaphase-promoting complex subunit 3 {ECO:0000250|UniProtKB:P30260};
DE AltName: Full=Metaphase-to-anaphase transition defect protein 1 {ECO:0000312|WormBase:Y110A7A.17a};
GN Name=mat-1 {ECO:0000312|WormBase:Y110A7A.17a};
GN Synonyms=apc-3 {ECO:0000312|WormBase:Y110A7A.17a},
GN cdc-27 {ECO:0000312|WormBase:Y110A7A.17a},
GN pod-5 {ECO:0000312|WormBase:Y110A7A.17a};
GN ORFNames=Y110A7A.17 {ECO:0000312|WormBase:Y110A7A.17a};
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:AAL92523.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF ISOFORM A, FUNCTION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLU-467.
RX PubMed=12620985; DOI=10.1242/dev.00385;
RA Shakes D.C., Sadler P.L., Schumacher J.M., Abdolrasulnia M., Golden A.;
RT "Developmental defects observed in hypomorphic anaphase-promoting complex
RT mutants are linked to cell cycle abnormalities.";
RL Development 130:1605-1620(2003).
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, AND MUTAGENESIS OF ALA-45; LEU-105; LEU-140; GLY-529; GLU-531 AND
RP ALA-580.
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 [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
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).
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:12620985, PubMed:11134076). Required for
CC embryonic anterior-posterior axis formation (PubMed:11832245). Plays a
CC role in regulating the abundance of glr-1 receptors in postmitotic
CC neurons, which may in turn control animal locomotion (PubMed:15556870).
CC {ECO:0000250|UniProtKB:P30260, ECO:0000269|PubMed:11134076,
CC ECO:0000269|PubMed:11832245, ECO:0000269|PubMed:12620985,
CC ECO:0000269|PubMed:15556870}.
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: Nucleus {ECO:0000250|UniProtKB:P38042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y110A7A.17a};
CC IsoId=Q9N593-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y110A7A.17b};
CC IsoId=Q9N593-2; Sequence=VSP_058042, VSP_058043;
CC -!- TISSUE SPECIFICITY: Expressed in the ventral nerve cord.
CC {ECO:0000269|PubMed:15556870}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in defective
CC metaphase to anaphase transition (Mat phenotype) and embryos that
CC arrest at the one-cell stage. {ECO:0000269|PubMed:12620985}.
CC -!- SIMILARITY: Belongs to the APC3/CDC27 family.
CC {ECO:0000250|UniProtKB:P30260}.
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DR EMBL; FO080728; CCD66209.1; -; Genomic_DNA.
DR EMBL; AY081955; AAL92523.1; -; mRNA.
DR EMBL; FO080728; CCD66210.1; -; Genomic_DNA.
DR RefSeq; NP_001021714.1; NM_001026543.4. [Q9N593-1]
DR RefSeq; NP_001021715.1; NM_001026544.2.
DR AlphaFoldDB; Q9N593; -.
DR SMR; Q9N593; -.
DR ComplexPortal; CPX-3382; Anaphase Promoting Complex/Cyclosome.
DR DIP; DIP-25913N; -.
DR STRING; 6239.Y110A7A.17a; -.
DR EPD; Q9N593; -.
DR PaxDb; Q9N593; -.
DR PeptideAtlas; Q9N593; -.
DR EnsemblMetazoa; Y110A7A.17a.1; Y110A7A.17a.1; WBGene00003132. [Q9N593-1]
DR EnsemblMetazoa; Y110A7A.17b.1; Y110A7A.17b.1; WBGene00003132.
DR GeneID; 172145; -.
DR KEGG; cel:CELE_Y110A7A.17; -.
DR UCSC; Y110A7A.17a; c. elegans.
DR CTD; 172145; -.
DR WormBase; Y110A7A.17a; CE23241; WBGene00003132; mat-1. [Q9N593-1]
DR WormBase; Y110A7A.17b; CE37056; WBGene00003132; mat-1. [Q9N593-2]
DR eggNOG; KOG1126; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_008850_3_0_1; -.
DR InParanoid; Q9N593; -.
DR OMA; YHETVNT; -.
DR OrthoDB; 280620at2759; -.
DR PhylomeDB; Q9N593; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9N593; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003132; Expressed in embryo and 4 other tissues.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0060471; P:cortical granule exocytosis; IMP:UniProtKB.
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: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; -; 4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Developmental protein;
KW Meiosis; Mitosis; Nucleus; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..788
FT /note="Cell division cycle protein 27 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435332"
FT REPEAT 561..594
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 596..628
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 629..662
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 664..696
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 731..764
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REGION 198..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 269..273
FT /note="PSRIN -> HEGYT (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058042"
FT VAR_SEQ 274..788
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058043"
FT MUTAGEN 45
FT /note="A->V: In ax144; mat phenotype."
FT /evidence="ECO:0000269|PubMed:11134076"
FT MUTAGEN 105
FT /note="L->F: In ax161; mat phenotype."
FT /evidence="ECO:0000269|PubMed:11134076"
FT MUTAGEN 140
FT /note="L->F: In ax227; mat phenotype."
FT /evidence="ECO:0000269|PubMed:11134076"
FT MUTAGEN 467
FT /note="E->K: In ye121; mat phenotype."
FT /evidence="ECO:0000269|PubMed:12620985"
FT MUTAGEN 529
FT /note="G->R: In ax520; mat phenotype."
FT /evidence="ECO:0000269|PubMed:11134076"
FT MUTAGEN 531
FT /note="E->G: In ax212; mat phenotype."
FT /evidence="ECO:0000269|PubMed:11134076"
FT MUTAGEN 580
FT /note="A->T: In ax72; mat phenotype."
FT /evidence="ECO:0000269|PubMed:11134076"
FT CONFLICT 780
FT /note="E -> K (in Ref. 1; AAL92523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 788 AA; 88511 MW; 7668E2E09F7A04BA CRC64;
MKESAASVAV RPQLREVFER FPADAHRTIE DEIHEMMKCY AFDDAIFLAE LHYETDKSNN
SESLLLYADC LYRANKKEEC YGLLSSVKLS GARLFYLLAR VSYDLNKIDD CRGALFEHDD
GVIRKDILEE PRVASHANLL HAQMLCDESY MDLALESCQK SLDENILLWS AIITYLRFGG
HDLAHTFEKH HRKSNGLYLD SPASSLKSET PSPNVPGPSS SSAASTAEPS RLESSVRRST
RGTIASANRE TRNTTSNITP RQSTPGSTPS RINPTAPRKS SRISEMTTRR TESSVTGSRS
SLFTEPERPH TRATHSSRNR ANAALNSDTE NSNASNTRTR SGIASVTRGS SSSQRTNPVR
TSIRIADAAA AANKTAKTLS QRRRNEKQPL VSRNSNLARS LSGSTNSVAS TASERPSEDE
VSQINPPLPS VASSLNNDEP MDIVDGVYDP EYKKLFDVYQ HIALIEESIS TYNWRSADAL
FAKLDRDIIL NTSMVRLQLG RACFEQSEYR ECRNILDDLH KRRKWKVDGT ELLSTSMWHL
QDTHALSALS QILTTESRER PQSWCAAGNC FSLQRQHTQA IECMERAIQL DKRFAYAYTL
LGHELIVQDE LDKAAGSFRS ALLLSPRDYR AWYGLGLVHL KKEQNLTALT NIQKAVNINP
TNRAMLCTLS QIEQQRGQID TALVLIDRAL TLNPLDVACR FNRSRLLFEA NRNEECLVEL
DKLKASSPDE AFIFHLLARV HRRMGNTHLA LLNYSWAAEL DPRGEQNITD SNVINREEYE
DDEYGSPV
