ID CDC23_BOVIN Reviewed; 597 AA.
AC A1A4R8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE RecName: Full=Cell division cycle protein 23 homolog;
DE AltName: Full=Anaphase-promoting complex subunit 8;
DE Short=APC8;
DE AltName: Full=Cyclosome subunit 8;
GN Name=CDC23; Synonyms=ANAPC8;
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=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) 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: 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. Interacts with FBXO43; the interaction is direct.
CC {ECO:0000250|UniProtKB:Q9UJX2}.
CC -!- PTM: Phosphorylated. Phosphorylation on Thr-562 occurs specifically
CC during mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APC8/CDC23 family. {ECO:0000305}.
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DR EMBL; BC126843; AAI26844.1; -; mRNA.
DR RefSeq; NP_001073735.1; NM_001080266.1.
DR AlphaFoldDB; A1A4R8; -.
DR SMR; A1A4R8; -.
DR STRING; 9913.ENSBTAP00000011540; -.
DR PaxDb; 9913-ENSBTAP00000011540; -.
DR Ensembl; ENSBTAT00000011540.5; ENSBTAP00000011540.4; ENSBTAG00000008759.5.
DR GeneID; 512651; -.
DR KEGG; bta:512651; -.
DR CTD; 8697; -.
DR VEuPathDB; HostDB:ENSBTAG00000008759; -.
DR VGNC; VGNC:50038; CDC23.
DR eggNOG; KOG1155; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_018320_3_0_1; -.
DR InParanoid; A1A4R8; -.
DR OMA; PQYLSAW; -.
DR OrthoDB; 3131281at2759; -.
DR TreeFam; TF101055; -.
DR Reactome; R-BTA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-BTA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-BTA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-BTA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-BTA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-BTA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-BTA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-BTA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-BTA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-BTA-176412; Phosphorylation of the APC/C.
DR Reactome; R-BTA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-BTA-2467813; Separation of Sister Chromatids.
DR Reactome; R-BTA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-BTA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-BTA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000008759; Expressed in tongue muscle and 106 other cell types or tissues.
DR ExpressionAtlas; A1A4R8; baseline and differential.
DR GO; GO:0005680; C:anaphase-promoting complex; 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:0007080; P:mitotic metaphase chromosome alignment; IEA:Ensembl.
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; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR007192; APC8.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12558; CELL DIVISION CYCLE 16,23,27; 1.
DR PANTHER; PTHR12558:SF10; CELL DIVISION CYCLE PROTEIN 23 HOMOLOG; 1.
DR Pfam; PF04049; ANAPC8; 1.
DR Pfam; PF13414; TPR_11; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Isopeptide bond; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT CHAIN 2..597
FT /note="Cell division cycle protein 23 homolog"
FT /id="PRO_0000379876"
FT REPEAT 27..63
FT /note="TPR 1"
FT REPEAT 73..112
FT /note="TPR 2"
FT REPEAT 114..144
FT /note="TPR 3"
FT REPEAT 169..200
FT /note="TPR 4"
FT REPEAT 229..259
FT /note="TPR 5"
FT REPEAT 263..293
FT /note="TPR 6"
FT REPEAT 297..327
FT /note="TPR 7"
FT REPEAT 331..361
FT /note="TPR 8"
FT REPEAT 366..395
FT /note="TPR 9"
FT REPEAT 400..432
FT /note="TPR 10"
FT REPEAT 433..466
FT /note="TPR 11"
FT REPEAT 468..500
FT /note="TPR 12"
FT REPEAT 504..540
FT /note="TPR 13"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 273
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 467
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 565
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 582
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX2"
SQ SEQUENCE 597 AA; 68780 MW; 230EAF23D101564D CRC64;
MAASSSIVSV APTASSVPVL PSSCDFSNLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF
SLPALPLSEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD RAAHFLHGCN SKKAYFLYMY
SRYLSGEKKK DDETVDSLGP LEKGQVKNEA LRELRVELSK KHQARELDGF GLYLYGVVLR
KLDLVKEAID VFVEATHVLP LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE
LQLIEEALQK YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM
DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA ALYFQRALKL
NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR AWYGLGQTYE ILKMPFYCLY
YYRRAHQLRP NDSRMLVALG ECYEKLNQLV EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL
TESEQAAQCY IKYIQDIYSC GEIVEHLEES TAFRYLAQYY FKCKLWDEAS ACAQKCCAFN
DTREEGKALL RQILQLRNQG ETPSTEIPAP FFLPASLSAN NTPTRRVSPL NLSSVTP
//
