CDC26_RAT
ID CDC26_RAT Reviewed; 85 AA.
AC Q6YDN7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Anaphase-promoting complex subunit CDC26;
DE AltName: Full=Cell division cycle protein 26 homolog;
DE AltName: Full=Protein BWK-2;
GN Name=Cdc26;
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 [MRNA].
RC STRAIN=Donryu;
RA Koami K., Yamakita S., Irino T., Osaka M.;
RT "Cloning of a novel leukemia-related gene.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. May
CC recruit the E2 ubiquitin-conjugating enzymes to the complex (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: V-shaped homodimer. Interacts with CDC16. The mammalian APC/C
CC is composed at least of 14 distinct subunits ANAPC1, ANAPC2,
CC CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10,
CC ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a
CC complex of at least 19 chains with a combined molecular mass of around
CC 1.2 MDa; APC/C interacts with FZR1 and FBXO5.
CC {ECO:0000250|UniProtKB:Q8NHZ8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDC26 family. {ECO:0000305}.
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DR EMBL; AY156922; AAO18338.1; -; mRNA.
DR EMBL; BC086343; AAH86343.1; -; mRNA.
DR RefSeq; NP_001013258.1; NM_001013240.2.
DR RefSeq; NP_001253983.1; NM_001267054.1.
DR RefSeq; NP_001253984.1; NM_001267055.1.
DR RefSeq; XP_006238304.1; XM_006238242.2.
DR RefSeq; XP_008762018.1; XM_008763796.2.
DR AlphaFoldDB; Q6YDN7; -.
DR SMR; Q6YDN7; -.
DR STRING; 10116.ENSRNOP00000049754; -.
DR iPTMnet; Q6YDN7; -.
DR PhosphoSitePlus; Q6YDN7; -.
DR PaxDb; Q6YDN7; -.
DR PRIDE; Q6YDN7; -.
DR GeneID; 366381; -.
DR KEGG; rno:366381; -.
DR CTD; 246184; -.
DR RGD; 1311342; Cdc26.
DR eggNOG; ENOG502S5GK; Eukaryota.
DR HOGENOM; CLU_190086_0_0_1; -.
DR InParanoid; Q6YDN7; -.
DR OMA; HKSREQM; -.
DR OrthoDB; 1612963at2759; -.
DR PhylomeDB; Q6YDN7; -.
DR TreeFam; TF101057; -.
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:Q6YDN7; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000029785; Expressed in thymus and 20 other tissues.
DR Genevisible; Q6YDN7; RN.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:InterPro.
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; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR InterPro; IPR018860; APC_suCDC26.
DR PANTHER; PTHR28579; PTHR28579; 1.
DR Pfam; PF10471; ANAPC_CDC26; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..85
FT /note="Anaphase-promoting complex subunit CDC26"
FT /id="PRO_0000271197"
FT REGION 26..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..38
FT /evidence="ECO:0000255"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 85 AA; 9802 MW; A6EAC06F9E1BC9EE CRC64;
MLRRKPTRLE LKLDDIEEFE NIRKDLEARK KQKEDVEGVG TSDGEGAAGL SSDPKSREQM
INDRIGYKPQ LKTNNRTSQF GNFEF
