ID   CD123_RAT               Reviewed;         336 AA.
AC   Q62834;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Cell division cycle protein 123 homolog;
DE            Short=Protein D123;
GN   Name=Cdc123; Synonyms=D123;
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], AND VARIANT VAL-109.
RC   STRAIN=Fischer;
RX   PubMed=8601400; DOI=10.1006/excr.1996.0078;
RA   Okuda A., Kimura G.;
RT   "An amino acid change in novel protein D123 is responsible for temperature-
RT   sensitive G1-phase arrest in a mutant of rat fibroblast line 3Y1.";
RL   Exp. Cell Res. 223:242-249(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9683532; DOI=10.1006/excr.1998.4074;
RA   Onisto M., Zeilante P., Scannapieco P., Pellati D., Pozza M., Caenazzo C.,
RA   Negro A., Garbisa S.;
RT   "Expression study on D123 gene product: evidence for high positivity in
RT   testis.";
RL   Exp. Cell Res. 242:451-459(1998).
RN   [4]
RP   DEGRADATION OF VARIANT VAL-109.
RX   PubMed=10698258; DOI=10.1247/csf.24.443;
RA   Okuda A., Ohtsu M., Kimura G.;
RT   "Extensive degradation of mutant-type D123 protein is responsible for
RT   temperature-sensitive proliferation inhibition in 3Y1tsD123 cells.";
RL   Cell Struct. Funct. 24:443-449(1999).
RN   [5]
RP   DEGRADATION OF VARIANT VAL-109, AND PHOSPHORYLATION.
RX   PubMed=11699637; DOI=10.1247/csf.26.205;
RA   Okuda A., Ohtsu M., Kimura G.;
RT   "Reversion of temperature-sensitive mutation by inhibition of proteasome-
RT   mediated degradation of mutated D123 protein.";
RL   Cell Struct. Funct. 26:205-214(2001).
CC   -!- FUNCTION: Required for S phase entry of the cell cycle.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9683532}.
CC   -!- TISSUE SPECIFICITY: Frequently detected in granular vesicles, in the
CC       cytoplasm of some epithelial, stromal and sperm cells and in
CC       varicosities lining nervous fibers, while it appears to be absent in
CC       endothelial and smooth muscle cells (at protein level). Widely
CC       expressed. Expressed at high level in testis.
CC       {ECO:0000269|PubMed:9683532}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11699637}.
CC   -!- PTM: The Val-109 variant is degraded by the proteasome suggesting that
CC       it is polyubiquitinated.
CC   -!- SIMILARITY: Belongs to the CDC123 family. {ECO:0000305}.
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DR   EMBL; U34843; AAB60521.1; -; mRNA.
DR   EMBL; BC061527; AAH61527.1; -; mRNA.
DR   RefSeq; NP_446329.1; NM_053877.3.
DR   AlphaFoldDB; Q62834; -.
DR   SMR; Q62834; -.
DR   STRING; 10116.ENSRNOP00000024016; -.
DR   jPOST; Q62834; -.
DR   PRIDE; Q62834; -.
DR   Ensembl; ENSRNOT00000116923; ENSRNOP00000096017; ENSRNOG00000017770.
DR   GeneID; 116656; -.
DR   KEGG; rno:116656; -.
DR   CTD; 8872; -.
DR   RGD; 619766; Cdc123.
DR   eggNOG; KOG2983; Eukaryota.
DR   GeneTree; ENSGT00390000003057; -.
DR   HOGENOM; CLU_034402_0_0_1; -.
DR   InParanoid; Q62834; -.
DR   OMA; RDLNHFD; -.
DR   OrthoDB; 1539674at2759; -.
DR   PhylomeDB; Q62834; -.
DR   TreeFam; TF323348; -.
DR   PRO; PR:Q62834; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000017770; Expressed in cerebellum and 20 other tissues.
DR   Genevisible; Q62834; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   InterPro; IPR009772; CDC123.
DR   PANTHER; PTHR15323; PTHR15323; 1.
DR   Pfam; PF07065; D123; 1.
DR   PIRSF; PIRSF007807; Cdc123; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..336
FT                   /note="Cell division cycle protein 123 homolog"
FT                   /id="PRO_0000228665"
FT   REGION          48..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75794"
FT   VARIANT         109
FT                   /note="A -> V (in 3Y1tsD123 cell line; reversibly arrested
FT                   in G1 phase of cell cycle at the restrictive temperature of
FT                   39.8 degrees Celsius; due to extensive degradation by the
FT                   proteasome)"
FT                   /evidence="ECO:0000269|PubMed:10698258,
FT                   ECO:0000269|PubMed:11699637, ECO:0000269|PubMed:8601400"
SQ   SEQUENCE   336 AA;  38812 MW;  6E1D1379A2612934 CRC64;
     MKKEHVSHCQ FSAWYPLFRS LTIKSVILPL PQNVKDYLLD DGTLVVSGRE DPPTCSQPDS
     GDEAEETQWS DDESTATLTA PEFPEFNTQV QEAINSLGGS VFPKLNWSAP RDAYWIAMNS
     SLKCKSLSDI FLLFKSSDFI THDFTQPFIH CNDDSPDPCI EYELVLRKWC ELIPGAEFRC
     FVKENKLIGI SQRDYTQYYD HISKQKEEIC RCIQDFFKEH LQYKFLDEDF VFDIYRDSRG
     KVWLIDFNPF GEVTDSLLFT WEELTSENNL RGDVSEADAL EQDSPAFRCT NSEVTVQPSP
     YLSYGLPKDF VDLSTGEDAH KLIDFLKLKR NQQEDD