RGCC_RAT
ID RGCC_RAT Reviewed; 137 AA.
AC Q9Z2P4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Regulator of cell cycle RGCC;
DE AltName: Full=Response gene to complement 32 protein;
DE Short=RGC-32;
GN Name=Rgcc; Synonyms=Rgc32;
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], FUNCTION, INDUCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH CDK1, AND TISSUE SPECIFICITY.
RX PubMed=9756947; DOI=10.1074/jbc.273.41.26977;
RA Badea T.C., Niculescu F.I., Soane L., Shin M.L., Rus H.;
RT "Molecular cloning and characterization of RGC-32, a novel gene induced by
RT complement activation in oligodendrocytes.";
RL J. Biol. Chem. 273:26977-26981(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-97, AND
RP IDENTIFICATION BY 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: Modulates the activity of cell cycle-specific kinases.
CC Enhances CDK1 activity. May contribute to the regulation of the cell
CC cycle. Fibrogenic factor contributing to the pathogenesis of renal
CC fibrosis through fibroblast activation (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9756947}.
CC -!- SUBUNIT: Interacts with PLK1 (By similarity). Interacts with CDK1.
CC Interacts with SMAD3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9756947}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Note=Cytoplasmic in unstimulated cells.
CC Nuclear after activation by complement. Associated with the centrosome
CC during prometaphase and metaphase (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, heart, brain, lung, skin,
CC spleen and thymus. {ECO:0000269|PubMed:9756947}.
CC -!- INDUCTION: Up-regulated in oligodendrocytes in response to complement
CC activation. {ECO:0000269|PubMed:9756947}.
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; AF036548; AAC68839.1; -; mRNA.
DR RefSeq; NP_446460.1; NM_054008.1.
DR AlphaFoldDB; Q9Z2P4; -.
DR STRING; 10116.ENSRNOP00000060481; -.
DR iPTMnet; Q9Z2P4; -.
DR PhosphoSitePlus; Q9Z2P4; -.
DR PaxDb; Q9Z2P4; -.
DR Ensembl; ENSRNOT00000068216; ENSRNOP00000060481; ENSRNOG00000042960.
DR GeneID; 117183; -.
DR KEGG; rno:117183; -.
DR UCSC; RGD:619721; rat.
DR CTD; 28984; -.
DR RGD; 619721; Rgcc.
DR eggNOG; ENOG502S1UB; Eukaryota.
DR GeneTree; ENSGT00390000011709; -.
DR HOGENOM; CLU_154700_0_0_1; -.
DR InParanoid; Q9Z2P4; -.
DR OMA; RFFYGEH; -.
DR OrthoDB; 1604248at2759; -.
DR PhylomeDB; Q9Z2P4; -.
DR PRO; PR:Q9Z2P4; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000042960; Expressed in thymus and 18 other tissues.
DR Genevisible; Q9Z2P4; RN.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0006956; P:complement activation; ISO:RGD.
DR GO; GO:0072537; P:fibroblast activation; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; ISO:RGD.
DR GO; GO:0090272; P:negative regulation of fibroblast growth factor production; ISO:RGD.
DR GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; ISO:RGD.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:RGD.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:RGD.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; ISO:RGD.
DR GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; ISO:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; NAS:BHF-UCL.
DR InterPro; IPR029252; RGCC.
DR PANTHER; PTHR32193; PTHR32193; 1.
DR Pfam; PF15151; RGCC; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..137
FT /note="Regulator of cell cycle RGCC"
FT /id="PRO_0000274703"
FT REGION 57..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBX1"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4X1"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4X1"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4X1"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 111
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9H4X1"
SQ SEQUENCE 137 AA; 14766 MW; 0CBE742C5FDC544C CRC64;
MKPPSTQSSP AAVAAAAPAM DSAAAADLTD VLCEFDAVLA DFASPFHERH FHYEEHLERM
KRRSSASVSD SSGFSDSESA DSLYRDSFTF SDEKLNSPTD STPALLSSAV TPRKAKLGDT
KELEDFIADL DRTLASM
