CSRP2_MOUSE
ID CSRP2_MOUSE Reviewed; 193 AA.
AC P97314; Q9CZG5;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cysteine and glycine-rich protein 2;
DE AltName: Full=Cysteine-rich protein 2;
DE Short=CRP2;
DE AltName: Full=Double LIM protein 1;
DE Short=DLP-1;
GN Name=Csrp2; Synonyms=Dlp1;
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].
RC STRAIN=C3H/HeJ;
RA Hashimoto N., Ogashiwa M.;
RT "Differential expression of three double LIM proteins during the skeletal
RT muscle terminal differentiation.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic stem cell;
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].
RC TISSUE=Liver;
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 [4]
RP INTERACTION WITH GLRX3.
RX PubMed=18258855; DOI=10.1161/circresaha.107.165985;
RA Jeong D., Kim J.M., Cha H., Oh J.G., Park J., Yun S.H., Ju E.S., Jeon E.S.,
RA Hajjar R.J., Park W.J.;
RT "PICOT attenuates cardiac hypertrophy by disrupting calcineurin-NFAT
RT signaling.";
RL Circ. Res. 102:711-719(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Drastically down-regulated in response to PDGF-BB or cell
CC injury, that promote smooth muscle cell proliferation and
CC dedifferentiation. Seems to play a role in the development of the
CC embryonic vascular system (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KAT14. The LIM domain 1 is necessary and
CC sufficient for this interaction (By similarity). Interacts with GLRX3.
CC {ECO:0000250, ECO:0000269|PubMed:18258855}.
CC -!- SUBCELLULAR LOCATION: Nucleus {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; D88792; BAA13722.1; -; mRNA.
DR EMBL; AK010626; BAB27072.1; -; mRNA.
DR EMBL; AK012647; BAB28379.1; -; mRNA.
DR EMBL; BC012663; AAH12663.1; -; mRNA.
DR CCDS; CCDS24165.1; -.
DR RefSeq; NP_031818.3; NM_007792.4.
DR AlphaFoldDB; P97314; -.
DR SMR; P97314; -.
DR BioGRID; 198953; 1.
DR STRING; 10090.ENSMUSP00000020403; -.
DR iPTMnet; P97314; -.
DR PhosphoSitePlus; P97314; -.
DR EPD; P97314; -.
DR jPOST; P97314; -.
DR MaxQB; P97314; -.
DR PaxDb; P97314; -.
DR PeptideAtlas; P97314; -.
DR PRIDE; P97314; -.
DR ProteomicsDB; 284053; -.
DR Antibodypedia; 29699; 244 antibodies from 34 providers.
DR DNASU; 13008; -.
DR Ensembl; ENSMUST00000020403; ENSMUSP00000020403; ENSMUSG00000020186.
DR GeneID; 13008; -.
DR KEGG; mmu:13008; -.
DR UCSC; uc007gzs.2; mouse.
DR CTD; 1466; -.
DR MGI; MGI:1202907; Csrp2.
DR VEuPathDB; HostDB:ENSMUSG00000020186; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000154980; -.
DR HOGENOM; CLU_054591_1_0_1; -.
DR InParanoid; P97314; -.
DR OMA; GSDKCAR; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; P97314; -.
DR TreeFam; TF313758; -.
DR BioGRID-ORCS; 13008; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Csrp2; mouse.
DR PRO; PR:P97314; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P97314; protein.
DR Bgee; ENSMUSG00000020186; Expressed in ascending aorta and 244 other tissues.
DR ExpressionAtlas; P97314; baseline and differential.
DR Genevisible; P97314; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0042805; F:actinin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0060537; P:muscle tissue development; IBA:GO_Central.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00132; LIM; 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Developmental protein; Differentiation; Isopeptide bond;
KW LIM domain; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation; Zinc.
FT CHAIN 1..193
FT /note="Cysteine and glycine-rich protein 2"
FT /id="PRO_0000075722"
FT DOMAIN 10..61
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 119..170
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOTIF 64..69
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21291"
FT MOD_RES 137
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97315"
FT MOD_RES 137
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 161
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97315"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16527"
FT CONFLICT 30
FT /note="F -> Y (in Ref. 1; BAB28379)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 20926 MW; BF792F284C9597E9 CRC64;
MPVWGGGNKC GACGRTVYHA EEVQCDGRSF HRCCFLCMVC RKNLDSTTVA IHDEEIYCKS
CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESAQPHRP TTNPNTSKFA QKYGGAEKCS
RCGDSVYAAE KIIGAGKPWH KNCFRCAKCG KSLESTTLTE KEGEIYCKGC YAKNFGPKGF
GYGQGAGALV HAQ
