RGCC_MOUSE
ID RGCC_MOUSE Reviewed; 137 AA.
AC Q9DBX1; Q9D0U0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11687586; DOI=10.1074/jbc.m109354200;
RA Badea T., Niculescu F., Soane L., Fosbrink M., Sorana H., Rus V.,
RA Shin M.L., Rus H.;
RT "RGC-32 increases p34CDC2 kinase activity and entry of aortic smooth muscle
RT cells into S-phase.";
RL J. Biol. Chem. 277:502-508(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-97 AND THR-111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH SMAD3.
RX PubMed=21990365; DOI=10.1074/jbc.m111.259184;
RA Li Z., Xie W.B., Escano C.S., Asico L.D., Xie Q., Jose P.A., Chen S.Y.;
RT "Response gene to complement 32 is essential for fibroblast activation in
RT renal fibrosis.";
RL J. Biol. Chem. 286:41323-41330(2011).
CC -!- FUNCTION: Modulates the activity of cell cycle-specific kinases.
CC Enhances CDK1 activity. May contribute to the regulation of the cell
CC cycle. May inhibit growth of glioma cells by promoting arrest of
CC mitotic progression at the G2/M transition. Fibrogenic factor
CC contributing to the pathogenesis of renal fibrosis through fibroblast
CC activation. {ECO:0000269|PubMed:21990365}.
CC -!- SUBUNIT: Interacts with CDK1 and PLK1 (By similarity). Interacts with
CC SMAD3. {ECO:0000250, ECO:0000269|PubMed:21990365}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Note=Cytoplasmic in unstimulated cells. Nuclear after
CC activation by complement. Associated with the centrosome during
CC prometaphase and metaphase (By similarity). {ECO:0000250}.
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; AF276981; AAK69442.1; -; mRNA.
DR EMBL; AK004451; BAB23310.1; -; mRNA.
DR EMBL; AK004705; BAB23490.1; -; mRNA.
DR EMBL; CT010403; CAJ18609.1; -; mRNA.
DR EMBL; BC049580; AAH49580.1; -; mRNA.
DR EMBL; BC050935; AAH50935.1; -; mRNA.
DR CCDS; CCDS49552.1; -.
DR RefSeq; NP_079703.2; NM_025427.2.
DR AlphaFoldDB; Q9DBX1; -.
DR STRING; 10090.ENSMUSP00000022595; -.
DR iPTMnet; Q9DBX1; -.
DR PhosphoSitePlus; Q9DBX1; -.
DR EPD; Q9DBX1; -.
DR jPOST; Q9DBX1; -.
DR MaxQB; Q9DBX1; -.
DR PaxDb; Q9DBX1; -.
DR PeptideAtlas; Q9DBX1; -.
DR PRIDE; Q9DBX1; -.
DR ProteomicsDB; 255319; -.
DR Antibodypedia; 23431; 98 antibodies from 16 providers.
DR DNASU; 66214; -.
DR Ensembl; ENSMUST00000022595; ENSMUSP00000022595; ENSMUSG00000022018.
DR GeneID; 66214; -.
DR KEGG; mmu:66214; -.
DR UCSC; uc007ust.1; mouse.
DR CTD; 28984; -.
DR MGI; MGI:1913464; Rgcc.
DR VEuPathDB; HostDB:ENSMUSG00000022018; -.
DR eggNOG; ENOG502S1UB; Eukaryota.
DR GeneTree; ENSGT00390000011709; -.
DR HOGENOM; CLU_154700_0_0_1; -.
DR InParanoid; Q9DBX1; -.
DR OMA; RFFYGEH; -.
DR OrthoDB; 1604248at2759; -.
DR PhylomeDB; Q9DBX1; -.
DR TreeFam; TF336312; -.
DR BioGRID-ORCS; 66214; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Rgcc; mouse.
DR PRO; PR:Q9DBX1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9DBX1; protein.
DR Bgee; ENSMUSG00000022018; Expressed in epididymal fat pad and 271 other tissues.
DR Genevisible; Q9DBX1; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0006956; P:complement activation; ISO:MGI.
DR GO; GO:0072537; P:fibroblast activation; IMP:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; ISO:MGI.
DR GO; GO:0090272; P:negative regulation of fibroblast growth factor production; ISO:MGI.
DR GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; ISO:MGI.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; ISO:MGI.
DR GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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_0000274702"
FT REGION 57..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000250|UniProtKB:Q9Z2P4"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 68
FT /note="V -> I (in Ref. 2; BAB23310)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="D -> N (in Ref. 2; BAB23310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 14717 MW; 01646F247F8B284A CRC64;
MKPPSAQSSP AAVAAAAPAM DSAAAADLTD VLCEFDAVLA DFASPFHERH FHYEEHLERM
KRRSSASVSD SSGFSDSESA DSVYRDSFTF SDEKLNSPTN SSPALLPSAV TPRKAKLGDT
KELEDFIADL DRTLASM
