ID A0A1S3EJN4_DIPOR Unreviewed; 810 AA.
AC A0A1S3EJN4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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|RefSeq:XP_012864571.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012864571.1};
RN [1] {ECO:0000313|RefSeq:XP_012864571.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012864571.1};
RG RefSeq;
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 RefSeq; XP_012864571.1; XM_013009117.1.
DR AlphaFoldDB; A0A1S3EJN4; -.
DR GeneID; 105980312; -.
DR CTD; 29945; -.
DR OrthoDB; 1211942at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:UniProtKB-UniRule.
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:UP000081671};
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 231..429
FT /note="Anaphase-promoting complex subunit 4 long"
FT /evidence="ECO:0000259|Pfam:PF12896"
FT REGION 756..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR037303-2"
FT CROSSLNK 800
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR037303-2"
SQ SEQUENCE 810 AA; 92094 MW; 41A1CA161ED7169C CRC64;
MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA SFHRVWSFPP
NENTGKEVTS LAWRPDGKLL AFALADTKKI ILCDVEKPES LHSFSVEAPV SCMHWMEVTV
ESSVLTSFYN AEDESNLLLP KLPTLPKNST SKIFSEENSD EIIKLLGDVR LNILVLGGSS
GYIELYAYGM FKIARVTGIA GTCLALCLSS DLKSLSVVAE VSTGGASEVS YFQLETNLLY
SFLPEVTRMA RKFTHISALL QYINLSLTCM CEAWEEILMQ MDSRLTKFVQ EKNTTTSVQD
EFMHLLLWGK ASAELQTLLM NQQTVKGLKK LGQSIESSYS SIQKLVISHL QSGSESLLYH
LSELKGMASW KQKYKPLGLD ATGIEDAITA VGSFILKANE LLQVIDSSMK NFKAFFRWLY
VAMLRMTEDH VLPELNKVCT EMTQKDITFV AEFLTEHFNE APDLYNRKGK YFNVEKVGQY
LKDEDDDLVS PPNTEGNQWY DFLQNSSHLK ESPLLFPYYP RKSLHFVKRR METIIDQCLQ
MPADVIGKSM NQAICIPLYR DARSEDSARR LLKFPFLWNN KSSNLQYLLF TILEDSLYKM
CILRRHTDIS QSVSNGLIAV KFGSFTYATT EKVRRSNYSC LDAQFYDDET VTVILKDTMG
REGRDRLLVQ LPLSFVYNSE DAAEYQFTGT YATRLDEQSS VIPTRTLHFE KHWRLLESMK
AQYVAGNGFR KVSCVLSSNL RHVRVFEMDI DDEWELDESS DEEEEASGKP VKIKEEVLSE
SETEAHHASA DAPAPEIVVK VEKLDPELDS
//
