ID   CSRP2_BOVIN             Reviewed;         193 AA.
AC   Q32LE9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Cysteine and glycine-rich protein 2;
DE   AltName: Full=Cysteine-rich protein 2;
DE            Short=CRP2;
GN   Name=CSRP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; BC109617; AAI09618.1; -; mRNA.
DR   RefSeq; NP_001033272.1; NM_001038183.1.
DR   AlphaFoldDB; Q32LE9; -.
DR   SMR; Q32LE9; -.
DR   STRING; 9913.ENSBTAP00000017835; -.
DR   PaxDb; Q32LE9; -.
DR   PeptideAtlas; Q32LE9; -.
DR   PRIDE; Q32LE9; -.
DR   GeneID; 539381; -.
DR   KEGG; bta:539381; -.
DR   CTD; 1466; -.
DR   eggNOG; KOG1700; Eukaryota.
DR   HOGENOM; CLU_054591_1_0_1; -.
DR   InParanoid; Q32LE9; -.
DR   OrthoDB; 1214165at2759; -.
DR   TreeFam; TF313758; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   2: Evidence at transcript 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_0000247315"
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;  20954 MW;  2E4231D6427579E7 CRC64;
     MPVWGGGNKC GACGRTVYHA EEVQCDGRSF HRCCFLCMVC RKNLDSTTVA IHDEEIYCKS
     CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESVQPHRP TTNPNTSKFA QKYGGAEKCS
     RCGDSVYAAE KIIGAGKPWH KNCFRCAKCG KSLESTTLTE KEGEIYCKGC YAKNFGPKGF
     GYGQGAGALV HAQ