CDC27_RAT
ID CDC27_RAT Reviewed; 824 AA.
AC Q4V8A2;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cell division cycle protein 27 homolog;
GN Name=Cdc27;
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=Testis;
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: Homodimer. The mammalian APC/C is composed at least of 14
CC distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5,
CC CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13,
CC ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains
CC with a combined molecular mass of around 1.2 MDa; APC/C interacts with
CC FZR1 and FBXO5 (By similarity). Interacts with RB. Interacts with
CC FAM168B/MANI (By similarity). Interacts with MCPH1 (By similarity).
CC {ECO:0000250|UniProtKB:A2A6Q5, ECO:0000250|UniProtKB:P30260}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30260}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P30260}.
CC -!- PTM: Phosphorylated. Phosphorylation on Ser-427 and Thr-447 occurs
CC specifically during mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APC3/CDC27 family. {ECO:0000305}.
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DR EMBL; BC097475; AAH97475.1; -; mRNA.
DR RefSeq; NP_001019964.1; NM_001024793.1.
DR AlphaFoldDB; Q4V8A2; -.
DR SMR; Q4V8A2; -.
DR BioGRID; 262095; 6.
DR IntAct; Q4V8A2; 1.
DR MINT; Q4V8A2; -.
DR STRING; 10116.ENSRNOP00000007963; -.
DR iPTMnet; Q4V8A2; -.
DR PhosphoSitePlus; Q4V8A2; -.
DR jPOST; Q4V8A2; -.
DR PaxDb; Q4V8A2; -.
DR PRIDE; Q4V8A2; -.
DR GeneID; 360643; -.
DR KEGG; rno:360643; -.
DR UCSC; RGD:1304921; rat.
DR CTD; 996; -.
DR RGD; 1304921; Cdc27.
DR VEuPathDB; HostDB:ENSRNOG00000005904; -.
DR eggNOG; KOG1126; Eukaryota.
DR HOGENOM; CLU_008850_1_0_1; -.
DR InParanoid; Q4V8A2; -.
DR OMA; ADKRHYN; -.
DR OrthoDB; 280620at2759; -.
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:Q4V8A2; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000005904; Expressed in testis and 19 other tissues.
DR Genevisible; Q4V8A2; RN.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
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:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; ISO:RGD.
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 GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..824
FT /note="Cell division cycle protein 27 homolog"
FT /id="PRO_0000390474"
FT REPEAT 84..114
FT /note="TPR 1"
FT REPEAT 115..148
FT /note="TPR 2"
FT REPEAT 499..532
FT /note="TPR 3"
FT REPEAT 567..600
FT /note="TPR 4"
FT REPEAT 602..634
FT /note="TPR 5"
FT REPEAT 635..668
FT /note="TPR 6"
FT REPEAT 670..702
FT /note="TPR 7"
FT REPEAT 704..736
FT /note="TPR 8"
FT REPEAT 737..770
FT /note="TPR 9"
FT REGION 251..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
SQ SEQUENCE 824 AA; 91663 MW; 24B02A896A0463A3 CRC64;
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL
LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ KSHDDLVTEF GDSACFTLSL
LGHVYCKTDR LAKGSECYQK SLSLNPFLWS PFESLCEIGE KPDPDQTFKL TSLQNFSSCL
PNTCTALVSN HSLSHRQPET VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI
SPDNVPLGTG PSILSKQVQN KPKTGRSLLG GPTALSPLTP SFGILPLETP SPGDGSYLQN
YTNTPSVIDV PSTGAPTKKS VARMGHTGAK SVFSQSGNSR EATPVLVAQT QSSGPQTSTT
PQVLSPTITS PPNALPRRSS RLFTSDSSTT KENSKKLKMK FPPKIPNRKT KSKTNKGGIT
QPNINDSLEI TKLDSSIISE GKISTITPQI QAFNLQKAAA GLMSLLREMG KGYLALCSYN
CKEAINILSH LPSHHYSTGW VLCQIGRAYF ELSEYMQAER IFSEVRRIES FRVEGMEIYS
TTLWHLQKDV ALSVLSKDLT DMDKNSPEAW CAAGNCFSLQ REHDIAIKFF QRAIQVDPNY
AYAYTLLGHE FVLTEELDKA LACFRNAIRV NPRHYNAWYG LGMIYYKQEK FSLAEMHFQK
ALDINPQSSV LLCHIGVVQH ALKKSEKALD TLNKAIVIDP KNPLCKFHRA SVLFANEKYK
SALQELEELK QIVPKESLVY FLIGKVYKKL GQTHLALMNF SWAMDLDPKG ANNQIKEAID
KRYLPDDEEP ITQEEQIMGT DESQESSMTD ADDTQLHAAE SDEF
