GenomeNet

Database: UniProt
Entry: G3V7U0_RAT
LinkDB: G3V7U0_RAT
Original site: G3V7U0_RAT 
ID   G3V7U0_RAT              Unreviewed;       194 AA.
AC   G3V7U0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Cysteine and glycine rich protein 3 {ECO:0000313|Ensembl:ENSRNOP00000019310.3};
GN   Name=Csrp3 {ECO:0000313|Ensembl:ENSRNOP00000019310.3,
GN   ECO:0000313|RGD:71092};
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 {ECO:0000313|Ensembl:ENSRNOP00000019310.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000019310.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000019310.3,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
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).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000019310.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000019310.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_006229299.1; XM_006229237.2.
DR   AlphaFoldDB; G3V7U0; -.
DR   Ensembl; ENSRNOT00000019311.6; ENSRNOP00000019310.3; ENSRNOG00000014327.6.
DR   RGD; 71092; Csrp3.
DR   GeneTree; ENSGT00940000159533; -.
DR   HOGENOM; CLU_054591_1_1_1; -.
DR   OMA; TCYGRRY; -.
DR   OrthoDB; 7294at2759; -.
DR   TreeFam; TF313758; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000014327; Expressed in heart and 14 other cell types or tissues.
DR   ExpressionAtlas; G3V7U0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0042805; F:actinin binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008307; F:structural constituent of muscle; IEA:Ensembl.
DR   GO; GO:0031433; F:telethonin binding; IEA:Ensembl.
DR   GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
DR   GO; GO:0035995; P:detection of muscle stretch; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0070528; P:protein kinase C signaling; IEA:Ensembl.
DR   GO; GO:0033365; P:protein localization to organelle; IEA:Ensembl.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
DR   GO; GO:0033292; P:T-tubule organization; IEA:Ensembl.
DR   CDD; cd09481; LIM1_CRP3; 1.
DR   CDD; cd09482; LIM2_CRP3; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24215:SF1; CYSTEINE AND GLYCINE-RICH PROTEIN 3; 1.
DR   PANTHER; PTHR24215; RHO-GTPASE-ACTIVATING PROTEIN LRG1; 1.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00132; LIM; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 4.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00023038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Zinc {ECO:0000256|ARBA:ARBA00023038}.
SQ   SEQUENCE   194 AA;  20862 MW;  2EE5FE1A91BA7EAB CRC64;
     MPNWGGGAKC GACDKTVYHA EEIQCNGRSF HKTCFHCMAC RKALDSTTVA AHESEIYCKV
     CYGRKYGPKG IGFGQGAGCL STDTGEHLGL QFQQSPKPAR AATTSNPSKF SAKFGESEKC
     PRCGKSVYAA EKVMGGGKPW HKTCFRCAIC GKSLESTNVT DKDGELYCKV CYAKNFGPTG
     IGFGGLTHQV EKKE
//
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