CRIP2_MOUSE
ID CRIP2_MOUSE Reviewed; 208 AA.
AC Q9DCT8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cysteine-rich protein 2;
DE Short=CRP-2;
DE AltName: Full=Heart LIM protein;
GN Name=Crip2; Synonyms=Crp2, Hlp;
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 [GENOMIC DNA / MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv; TISSUE=Heart;
RX PubMed=12128222; DOI=10.1016/s0925-4773(02)00139-9;
RA Yu T.S., Moctezuma-Anaya M., Kubo A., Keller G., Robertson S.;
RT "The heart LIM protein gene (Hlp), expressed in the developing and adult
RT heart, defines a new tissue-specific LIM-only protein family.";
RL Mech. Dev. 116:187-192(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=12370427; DOI=10.1073/pnas.212392399;
RA Zhou J., Ashouian N., Delepine M., Matsuda F., Chevillard C., Riblet R.,
RA Schildkraut C.L., Birshtein B.K.;
RT "The origin of a developmentally regulated Igh replicon is located near the
RT border of regulatory domains for Igh replication and expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13693-13698(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 INTERACTION WITH TGFB1I1.
RX PubMed=15713747; DOI=10.1242/jcs.01683;
RA Kim-Kaneyama J.-R., Suzuki W., Ichikawa K., Ohki T., Kohno Y., Sata M.,
RA Nose K., Shibanuma M.;
RT "Uni-axial stretching regulates intracellular localization of Hic-5
RT expressed in smooth-muscle cells in vivo.";
RL J. Cell Sci. 118:937-949(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-138 AND LYS-144, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 -!- SUBUNIT: Interacts with TGFB1I1. {ECO:0000269|PubMed:15713747}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, its expression is primarily
CC restricted to the developing heart. In situ hybridization showed
CC expression at 7.75 dpc in the paired heart-forming primordia prior to
CC linear heart-tube formation. At 8.5 dpc, strong expression is detected
CC in the heart, with equal expression in both heart chambers. Expression
CC is detected in both myocardium and endocardium, and in vascular
CC endothelium. Later in fetal development low levels of expression is
CC detected outside the heart, including dorsal root ganglia and the
CC spinal cord. In the adult, it is expressed at highest levels in the
CC heart, and at lower levels in the brain, skeletal muscle and aorta.
CC {ECO:0000269|PubMed:12128222}.
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DR EMBL; AF469648; AAM89218.1; -; mRNA.
DR EMBL; AF470625; AAM89219.1; -; Genomic_DNA.
DR EMBL; AF450245; AAM97586.1; -; Genomic_DNA.
DR EMBL; AK002484; BAB22136.1; -; mRNA.
DR EMBL; BC002093; AAH02093.1; -; mRNA.
DR EMBL; BC002096; AAH02096.1; -; mRNA.
DR CCDS; CCDS26204.1; -.
DR RefSeq; NP_001334372.1; NM_001347443.1.
DR RefSeq; NP_077185.1; NM_024223.2.
DR AlphaFoldDB; Q9DCT8; -.
DR BioGRID; 212808; 4.
DR IntAct; Q9DCT8; 2.
DR STRING; 10090.ENSMUSP00000081943; -.
DR iPTMnet; Q9DCT8; -.
DR PhosphoSitePlus; Q9DCT8; -.
DR SwissPalm; Q9DCT8; -.
DR CPTAC; non-CPTAC-3422; -.
DR EPD; Q9DCT8; -.
DR jPOST; Q9DCT8; -.
DR MaxQB; Q9DCT8; -.
DR PaxDb; Q9DCT8; -.
DR PRIDE; Q9DCT8; -.
DR ProteomicsDB; 284014; -.
DR TopDownProteomics; Q9DCT8; -.
DR Antibodypedia; 15064; 223 antibodies from 28 providers.
DR DNASU; 68337; -.
DR Ensembl; ENSMUST00000084882; ENSMUSP00000081943; ENSMUSG00000006356.
DR GeneID; 68337; -.
DR KEGG; mmu:68337; -.
DR UCSC; uc007pfy.2; mouse.
DR CTD; 1397; -.
DR MGI; MGI:1915587; Crip2.
DR VEuPathDB; HostDB:ENSMUSG00000006356; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158683; -.
DR HOGENOM; CLU_054591_2_0_1; -.
DR InParanoid; Q9DCT8; -.
DR OMA; YEKPCAE; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; Q9DCT8; -.
DR TreeFam; TF313758; -.
DR BioGRID-ORCS; 68337; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Crip2; mouse.
DR PRO; PR:Q9DCT8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9DCT8; protein.
DR Bgee; ENSMUSG00000006356; Expressed in ankle joint and 271 other tissues.
DR ExpressionAtlas; Q9DCT8; baseline and differential.
DR Genevisible; Q9DCT8; MM.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030097; P:hemopoiesis; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
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; LIM domain; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..208
FT /note="Cysteine-rich protein 2"
FT /id="PRO_0000075711"
FT DOMAIN 5..57
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 126..178
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52943"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 208 AA; 22727 MW; 9A3AEF8A8FBA1D19 CRC64;
MASKCPKCDK TVYFAEKVSS LGKDWHKFCL KCERCNKTLT PGGHAEHDGK PFCHKPCYAT
LFGPKGVNIG GAGSYIYEKP QTEAPQVTGP IEVPVVRTEE RKTSGPPKGP SKASSVTTFT
GEPNMCPRCN KRVYFAEKVT SLGKDWHRPC LRCERCSKTL TPGGHAEHDG QPYCHKPCYG
ILFGPKGVNT GAVGSYIYDK DPEGTVQP
