APC5_RAT
ID APC5_RAT Reviewed; 727 AA.
AC A1L1K3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Anaphase-promoting complex subunit 5;
DE Short=APC5;
DE AltName: Full=Cyclosome subunit 5;
GN Name=Anapc5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. The
CC APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation of
CC 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC ANAPC16 that assemble into a complex of at least 19 chains with a
CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC and FBXO5. {ECO:0000250|UniProtKB:Q9UJX4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJX4}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UJX4}.
CC -!- SIMILARITY: Belongs to the APC5 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC129106; AAI29107.1; -; mRNA.
DR RefSeq; NP_001073616.1; NM_001080147.1.
DR AlphaFoldDB; A1L1K3; -.
DR SMR; A1L1K3; -.
DR BioGRID; 252650; 1.
DR STRING; 10116.ENSRNOP00000001794; -.
DR iPTMnet; A1L1K3; -.
DR PhosphoSitePlus; A1L1K3; -.
DR jPOST; A1L1K3; -.
DR PaxDb; A1L1K3; -.
DR PeptideAtlas; A1L1K3; -.
DR PRIDE; A1L1K3; -.
DR GeneID; 288671; -.
DR KEGG; rno:288671; -.
DR UCSC; RGD:1306125; rat.
DR CTD; 51433; -.
DR RGD; 1306125; Anapc5.
DR eggNOG; KOG4322; Eukaryota.
DR HOGENOM; CLU_020635_0_0_1; -.
DR InParanoid; A1L1K3; -.
DR PhylomeDB; A1L1K3; -.
DR Reactome; R-RNO-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-RNO-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-RNO-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-RNO-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-RNO-176412; Phosphorylation of the APC/C.
DR Reactome; R-RNO-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:A1L1K3; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; A1L1K3; RN.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR037679; Apc5.
DR InterPro; IPR026000; Apc5_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12830; PTHR12830; 1.
DR Pfam; PF12862; ANAPC5; 2.
DR SUPFAM; SSF48452; SSF48452; 2.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..727
FT /note="Anaphase-promoting complex subunit 5"
FT /id="PRO_0000307377"
FT REPEAT 194..234
FT /note="TPR 1"
FT REPEAT 235..285
FT /note="TPR 2"
FT REPEAT 286..322
FT /note="TPR 3"
FT REPEAT 323..359
FT /note="TPR 4"
FT REPEAT 360..390
FT /note="TPR 5"
FT REPEAT 391..438
FT /note="TPR 6"
FT REPEAT 439..472
FT /note="TPR 7"
FT REPEAT 473..512
FT /note="TPR 8"
FT REPEAT 513..552
FT /note="TPR 9"
FT REPEAT 553..592
FT /note="TPR 10"
FT REPEAT 593..632
FT /note="TPR 11"
FT REPEAT 633..668
FT /note="TPR 12"
FT REPEAT 669..708
FT /note="TPR 13"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX4"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX4"
SQ SEQUENCE 727 AA; 81739 MW; A5017E5A91BC9958 CRC64;
MMTNGVVHAN LFGIKDWVTP YKIAVLVLLN EMGRTGEGAV SLVERRKLNQ LLLPLLQGPD
ITLSKLYKLI EESCPQLANS VQIRIKLMAE GELKDLEQFF DDLSDSFSGT EPEVHKTSVV
GLFLRHMILA YSKLSFSQVF KLYTALQQYF QNGEKKTVED ADMDREDGER QMEKEELDVS
VREEEVSCSG PLSQKQAEFF LSQQAALLKN DETKALTPAS LQKELNNLLK FNPDFAEAHY
LSYLNNLRVQ DVFSSTHSLL HYFDRLILTG AEGKSNGEEG YGRSLRYAAL NLAALHCRFG
HYQQAELALQ EAIRIAQESN DHVCLQHCLS WLYVLGQKRA DSYVLLEHSV KKAVHFGLPR
AFAGKTANKL MDALKDSDLL HWKHSLSELI DISIAQKTAI WRLYGRSTMA LQQAQMLLSM
NSLESLSAGV QQNNTESFAV ALCHLAELHA EQGCFAAAGE VLKHLKERFP PNSQHAQLWM
LCDQKIQFDR AMNDGKFHLA DSLVTGITAL NGIEGVYRKA VVLQAQNQMT EAHKLLQKLL
TYCQKLKNTE MVISVLLSVA ELYWRSSSPT IAMPVLLEAL ALSKEYRLQY LASETVLNLA
YAQLILGIPE QALTLLHMAI EPILADGAIL DKGRAMFLVS KCQVASAASY DPVKKAEALE
AAIQNLTEAK NYFAKVDCRE RIRDVSYFQA RLYHALGKTQ ERNHCAMVFR QLHQELPSHG
VPLINHL
