CSRP2_RAT
ID CSRP2_RAT Reviewed; 193 AA.
AC Q62908;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Cysteine and glycine-rich protein 2;
DE AltName: Full=Cysteine-rich protein 2;
DE Short=CRP2;
DE AltName: Full=Smooth muscle cell LIM protein;
DE Short=SmLIM;
GN Name=Csrp2; Synonyms=Smlim;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Aorta, and Smooth muscle;
RX PubMed=8626582; DOI=10.1074/jbc.271.17.10194;
RA Jain M., Fujita K.P., Hsieh C.-M., Endege W.O., Sibinga N.E.S., Yet S.-F.,
RA Kashiki S., Lee W.-S., Perrella M.A., Haber E., Lee M.-E.;
RT "Molecular cloning and characterization of SmLIM, a developmentally
RT regulated LIM protein preferentially expressed in aortic smooth muscle
RT cells.";
RL J. Biol. Chem. 271:10194-10199(1996).
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.
CC -!- SUBUNIT: Interacts with KAT14. The LIM domain 1 is necessary and
CC sufficient for this interaction (By similarity). Interacts with GLRX3
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q62908; Q3TKT4: Smarca4; Xeno; NbExp=3; IntAct=EBI-918425, EBI-1210244;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Highly expressed in the aorta; weakly found in the
CC kidney, thymus, and intestine. Barely detectable in brain, testis,
CC esophagus, lung, liver, aortic adventitia, vena cava, or uterus; not
CC present in heart and skeletal muscle.
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DR EMBL; U44948; AAC52554.1; -; mRNA.
DR RefSeq; NP_803174.2; NM_177425.3.
DR AlphaFoldDB; Q62908; -.
DR SMR; Q62908; -.
DR DIP; DIP-36882N; -.
DR IntAct; Q62908; 2.
DR STRING; 10116.ENSRNOP00000061356; -.
DR iPTMnet; Q62908; -.
DR PhosphoSitePlus; Q62908; -.
DR PaxDb; Q62908; -.
DR PRIDE; Q62908; -.
DR GeneID; 29317; -.
DR KEGG; rno:29317; -.
DR UCSC; RGD:61950; rat.
DR CTD; 1466; -.
DR RGD; 61950; Csrp2.
DR eggNOG; KOG1700; Eukaryota.
DR InParanoid; Q62908; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; Q62908; -.
DR PRO; PR:Q62908; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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:0045445; P:myoblast differentiation; IEP:RGD.
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_0000075723"
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:0000250|UniProtKB:P97314"
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:0000250|UniProtKB:P97314"
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"
SQ SEQUENCE 193 AA; 20940 MW; D412299E95190DC3 CRC64;
MPVWGGGNKC GACGRTVYHA EEVQCDGRTF HRCCFLCMVC RKNLDSTTVA IHDEEIYCKS
CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESAQPHRP TTNPNTSKFA QKYGGAEKCS
RCGDSVYAAE KIIGAGKPWH KNCFRCAKCG KSLESTTLTE KEGEIYCKGC YAKNFGPKGF
GYGQGAGALV HAQ
