ID A0A0D9RVR4_CHLSB Unreviewed; 808 AA.
AC A0A0D9RVR4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Anaphase-promoting complex subunit 4 {ECO:0000256|ARBA:ARBA00016067, ECO:0000256|PIRNR:PIRNR037303};
DE AltName: Full=Cyclosome subunit 4 {ECO:0000256|PIRNR:PIRNR037303};
GN Name=ANAPC4 {ECO:0000313|Ensembl:ENSCSAP00000012703.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000012703.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000012703.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000012703.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle.
CC {ECO:0000256|PIRNR:PIRNR037303}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|PIRNR:PIRNR037303}.
CC -!- SIMILARITY: Belongs to the APC4 family.
CC {ECO:0000256|PIRNR:PIRNR037303}.
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DR EMBL; AQIB01114499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008015915.1; XM_008017724.1.
DR AlphaFoldDB; A0A0D9RVR4; -.
DR STRING; 60711.ENSCSAP00000012703; -.
DR Ensembl; ENSCSAT00000014739.1; ENSCSAP00000012703.1; ENSCSAG00000016642.1.
DR GeneID; 103246266; -.
DR CTD; 29945; -.
DR eggNOG; KOG4640; Eukaryota.
DR GeneTree; ENSGT00390000004612; -.
DR OMA; HCKLFVP; -.
DR OrthoDB; 1211942at2759; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 103246266; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 27.
DR Bgee; ENSCSAG00000016642; Expressed in pituitary gland and 7 other cell types or tissues.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR024789; APC4.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
DR InterPro; IPR024790; APC4_long_dom.
DR InterPro; IPR017169; APC4_metazoa.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13260; ANAPHASE PROMOTING COMPLEX SUBUNIT 4 APC4; 1.
DR PANTHER; PTHR13260:SF0; ANAPHASE-PROMOTING COMPLEX SUBUNIT 4; 1.
DR Pfam; PF12896; ANAPC4; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR PIRSF; PIRSF037303; APC4; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PIRNR:PIRNR037303};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|PIRNR:PIRNR037303};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|PIRNR:PIRNR037303};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR037303}.
FT DOMAIN 27..117
FT /note="Anaphase-promoting complex subunit 4-like WD40"
FT /evidence="ECO:0000259|Pfam:PF12894"
FT DOMAIN 233..431
FT /note="Anaphase-promoting complex subunit 4 long"
FT /evidence="ECO:0000259|Pfam:PF12896"
FT REGION 753..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 772
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR037303-2"
FT CROSSLNK 798
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR037303-2"
SQ SEQUENCE 808 AA; 92109 MW; 8FF9AEFE5DABF0EC CRC64;
MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA SFHRVWSFPP
NENTGKEVTC LAWRPDGKLL AFALADTKKI VLCDVEKPES LHSFSVEAPV SCMHWMEVTV
ESSVLTSFYN AEDESNLLLP KLPTLPKNYS NTSKIFSEEN SDEIIKLLGD VRLNILVLGG
SSGFIELYAY GMFKIARVTG IAGTCLALCL SSDLKSLSVV TEVSTSGASE VSYFQLETNL
LYSFLPEVTR MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKNTTTSV
QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS HLQSGSESLL
YHLSELKGMA SWKQKYEPLG LDAAGIEDAI TAVGSFILKA NELLQVIDSS MKNFKAFFRW
LYVAMLRMTE DHVLPELNKM TQKDITFVAE FLTEHFNEAP DLYNRKGKYF NVERVGQYLK
DEDDDLVSPP NTEGNQWYDF LQNSSHLKES PLLFPYYPRK SLHFVKRRME NIIDQCLQKP
ADVIGKSMNQ AICIPLYRDT RSEDSTRRLF KFPFLWNNKT SNLHYLLFTI LEDSLYKMCI
LRRHTDISQS VSNGLIAIKF GSFTYATTEK VRRSIYSCLD AQFYDDETVT VVLKDTVGRE
GRDRLLVQLP LSLVYNSEDS AEYQFTGTYS TRLDEQCSAI PTRTMHFEKH WRLLESMKAQ
YVAGNGFRKV SCVLSSNLRH VRVFEMDIDD EWELDESSDE EEEAGNKPVK IKEEVLSESE
TENQQAGAAA FAPEIVIKVE KLDPELDS
//
