CDC20_PIG
ID CDC20_PIG Reviewed; 499 AA.
AC Q5H7C0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cell division cycle protein 20 homolog;
DE AltName: Full=p55CDC;
GN Name=CDC20;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yamamuro T., Naito K., Tojo H.;
RT "Porcine homolog of CDC20 (cell division cycle 20), p55CDC.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for full ubiquitin ligase activity of the anaphase
CC promoting complex/cyclosome (APC/C) and may confer substrate
CC specificity upon the complex. Is regulated by MAD2L1: in metaphase the
CC MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the
CC CDC20-APC/C binary complex is active in degrading substrates. The
CC CDC20-APC/C complex positively regulates the formation of synaptic
CC vesicle clustering at active zone to the presynaptic membrane in
CC postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces
CC presynaptic differentiation (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of a complex with CDC20, CDC27, SPATC1 and TUBG1 (By
CC similarity). Interacts with NEUROD2 (By similarity). Interacts with
CC dimeric MAD2L1 in its closed conformation form (By similarity).
CC Interacts with BUB1B (By similarity). The phosphorylated form interacts
CC with APC/C (By similarity). Interacts with NINL (By similarity). May
CC interact with MAD2L2 (By similarity). Interacts with CDK5RAP2 (By
CC similarity). Interacts with SIRT2 (By similarity). Interacts with
CC isoform 1 of NEK2 (By similarity). Interacts with HSF1 (via
CC phosphorylated form); this interaction occurs in mitosis in a MAD2L1-
CC dependent manner and prevents PLK1-stimulated degradation of HSF1 by
CC blocking the recruitment of the SCF(BTRC) ubiquitin ligase complex (By
CC similarity). Interacts (via the N-terminal substrate-binding domain)
CC with FBXO5 (By similarity). Interacts with CCNF (By similarity).
CC {ECO:0000250|UniProtKB:Q12834, ECO:0000250|UniProtKB:Q9JJ66}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis, probably by maturation promoting
CC factor (MPF). Phosphorylated by BUB1 at Ser-41; Ser-72; Ser-92; Ser-
CC 153; Thr-157 and Ser-161. Phosphorylated by NEK2 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Dephosphorylated by CTDP1. {ECO:0000250}.
CC -!- PTM: Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation
CC enhances the interaction of CDC20 with CDC27, leading to activation of
CC anaphase promoting complex/cyclosome (APC/C) (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated and degraded by the proteasome during spindle
CC assembly checkpoint. Deubiquitinated by USP44, leading to stabilize the
CC MAD2L1-CDC20-APC/C ternary complex, thereby preventing premature
CC activation of the APC/C. Ubiquitinated at Lys-490 during prometaphase.
CC Ubiquitination at Lys-485 and Lys-490 has no effect on its ability to
CC bind the APC/C complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
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DR EMBL; AB192873; BAD89276.1; -; mRNA.
DR RefSeq; NP_001116566.1; NM_001123094.1.
DR AlphaFoldDB; Q5H7C0; -.
DR SMR; Q5H7C0; -.
DR STRING; 9823.ENSSSCP00000004268; -.
DR PaxDb; Q5H7C0; -.
DR PRIDE; Q5H7C0; -.
DR Ensembl; ENSSSCT00000004368; ENSSSCP00000004268; ENSSSCG00000003949.
DR Ensembl; ENSSSCT00015099449; ENSSSCP00015041112; ENSSSCG00015073942.
DR Ensembl; ENSSSCT00040091155; ENSSSCP00040040157; ENSSSCG00040066718.
DR Ensembl; ENSSSCT00045065251; ENSSSCP00045046162; ENSSSCG00045037768.
DR Ensembl; ENSSSCT00050054962; ENSSSCP00050023246; ENSSSCG00050040608.
DR Ensembl; ENSSSCT00055006222; ENSSSCP00055004886; ENSSSCG00055003208.
DR GeneID; 397379; -.
DR KEGG; ssc:397379; -.
DR CTD; 991; -.
DR VGNC; VGNC:86444; CDC20.
DR eggNOG; KOG0305; Eukaryota.
DR GeneTree; ENSGT00950000183104; -.
DR HOGENOM; CLU_014831_6_1_1; -.
DR InParanoid; Q5H7C0; -.
DR OMA; NGHEDRV; -.
DR OrthoDB; 1220675at2759; -.
DR TreeFam; TF101065; -.
DR Reactome; R-SSC-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
DR Reactome; R-SSC-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-SSC-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-SSC-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-SSC-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-SSC-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-SSC-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-SSC-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-SSC-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-SSC-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-SSC-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-SSC-176417; Phosphorylation of Emi1.
DR Reactome; R-SSC-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-SSC-2467813; Separation of Sister Chromatids.
DR Reactome; R-SSC-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SSC-5663220; RHO GTPases Activate Formins.
DR Reactome; R-SSC-5689880; Ub-specific processing proteases.
DR Reactome; R-SSC-68877; Mitotic Prometaphase.
DR Reactome; R-SSC-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-SSC-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000003949; Expressed in forelimb bud and 32 other tissues.
DR ExpressionAtlas; Q5H7C0; baseline and differential.
DR Genevisible; Q5H7C0; SS.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IBA:GO_Central.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:AgBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:1904146; P:positive regulation of meiotic cell cycle process involved in oocyte maturation; IMP:AgBase.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR033010; Cdc20/Fizzy.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19918; PTHR19918; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Mitosis; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..499
FT /note="Cell division cycle protein 20 homolog"
FT /id="PRO_0000278194"
FT REPEAT 182..221
FT /note="WD 1"
FT REPEAT 224..263
FT /note="WD 2"
FT REPEAT 266..303
FT /note="WD 3"
FT REPEAT 307..346
FT /note="WD 4"
FT REPEAT 353..395
FT /note="WD 5"
FT REPEAT 397..438
FT /note="WD 6"
FT REPEAT 441..480
FT /note="WD 7"
FT REGION 20..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12834"
SQ SEQUENCE 499 AA; 54784 MW; F07E9C7BC742799F CRC64;
MAQFVFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH SAGRTPGRTP
GKSNSKMQTT PSKPGGDRYI PHRSASQMEV ASFLLSKENQ PDNSQTPTKK EHQKAWALNL
NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV LYSQKATPGS SRKTCRYIPS LPDRILDAPE
IRNDYYLNLV DWSSGNVLAV ALDNSVYLWS ASSGDILQLL QMEQPGDYVS SVAWIKEGNY
LAVGTSSAEV QLWDVQQQKR LRNMTSHSAR VGSLCWNSYI LSSGSRSGHI HHHDVRVAEH
HVATLSGHSQ EVCGLRWAPD GRHLASGGND NLVNVWPSAP GEGGWVPLQT FTQHQGAVKA
VAWCPWQSNV LATGGGTSDR HIRIWNVCSG ACLSAVDAHS QVCSILWSPH YKELISGHGF
AQNQLVIWKY PTMAKVAELK GHTARVLSLT MSPDGATVAS AAADETLRLW RCFELDPARR
REREKASAAK SSLIHQGIR
