CDC27_BOVIN
ID CDC27_BOVIN Reviewed; 825 AA.
AC A7Z061;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cell division cycle protein 27 homolog;
GN Name=CDC27;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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; BC153259; AAI53260.1; -; mRNA.
DR RefSeq; NP_001098898.1; NM_001105428.1.
DR AlphaFoldDB; A7Z061; -.
DR SMR; A7Z061; -.
DR STRING; 9913.ENSBTAP00000003533; -.
DR PaxDb; A7Z061; -.
DR PRIDE; A7Z061; -.
DR Ensembl; ENSBTAT00000003533; ENSBTAP00000003533; ENSBTAG00000002726.
DR GeneID; 540660; -.
DR KEGG; bta:540660; -.
DR CTD; 996; -.
DR VEuPathDB; HostDB:ENSBTAG00000002726; -.
DR VGNC; VGNC:50040; CDC27.
DR eggNOG; KOG1126; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_008850_1_0_1; -.
DR InParanoid; A7Z061; -.
DR OrthoDB; 280620at2759; -.
DR TreeFam; TF101058; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000002726; Expressed in oocyte and 107 other tissues.
DR ExpressionAtlas; A7Z061; baseline.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
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; IBA:GO_Central.
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..825
FT /note="Cell division cycle protein 27 homolog"
FT /id="PRO_0000390472"
FT REPEAT 6..35
FT /note="TPR 1"
FT REPEAT 38..65
FT /note="TPR 2"
FT REPEAT 67..99
FT /note="TPR 3"
FT REPEAT 115..145
FT /note="TPR 4"
FT REPEAT 465..495
FT /note="TPR 5"
FT REPEAT 499..528
FT /note="TPR 6"
FT REPEAT 533..563
FT /note="TPR 7"
FT REPEAT 567..598
FT /note="TPR 8"
FT REPEAT 601..631
FT /note="TPR 9"
FT REPEAT 635..667
FT /note="TPR 10"
FT REPEAT 670..702
FT /note="TPR 11"
FT REPEAT 704..734
FT /note="TPR 12"
FT REPEAT 737..768
FT /note="TPR 13"
FT REGION 305..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..815
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 244
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 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
SQ SEQUENCE 825 AA; 91870 MW; 4B2410577714FF9C CRC64;
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL
LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ KSHDDIVTEF GDSACFTLSL
LGHVYCKTDR LAKGSECYQK SLSLNPFLWS PFESLCEIGE KPDPDQTFKL TSLQNFSSCL
PNSCTTLVSN HSLSHRQPET VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI
SPDTVPLGTG TSILSKQVQN KPKTGRSLLG GPAALSPLTP SFGILPLETP SPGDGSYLQN
YTNTSSVIDV PPTGAPSKKS VARIGQTGTK SVFSQSGNSR EVTPILVAQT QSSGPQTSTT
PQVLSPTITS PPNALPRRSS RLFTSDSSTT KENSKKLKMK FPPKIPNRKT KSKTNKGGIT
QPNINDSLEI TKLDSSIISE GKISTITPQI QAFNLQKAAA EGLMSLLREM GKGYLALCSY
NCKEAINILS HLPSHHYNTG WVLCQIGRAY FELSEYMQAE RIFSEVRRIE NYRVEGMEIY
STTLWHLQKD VALSVLSKDL TDMDKNSPEA WCAAGNCFSL QREHDIAIKF FQRAIQVDPN
YAYAYTLLGH EFVLTEELDK ALACFRNAIR VNPRHYNAWY GLGMIYYKQE KFSLAEMHFQ
KALDINPQSS VLLCHIGVVQ HALKKSEKAL DTLNKAIVID PKNPLCKFHR ASVLFANEKY
KSALQELEEL KQIVPKESLV YFLIGKVYKK LGQTHLALMN FSWAMDLDPK GANNQIKEAI
DKRYLPDDEE PITQEEQIMG TDESQESSMT DADDTQLHAA ESDEF
