ID   CSRP1_RAT               Reviewed;         193 AA.
AC   P47875;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Cysteine and glycine-rich protein 1;
DE   AltName: Full=Cysteine-rich protein 1;
DE            Short=CRP;
DE            Short=CRP1;
GN   Name=Csrp1; Synonyms=Csrp;
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=Olfactory bulb;
RX   PubMed=7816640; DOI=10.1093/nar/22.24.5477;
RA   McLaughlin C.R., Tao Q., Abood M.E.;
RT   "Isolation and developmental expression of a rat cDNA encoding a cysteine-
RT   rich zinc finger protein.";
RL   Nucleic Acids Res. 22:5477-5483(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-192, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
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).
CC   -!- FUNCTION: Could play a role in neuronal development.
CC   -!- SUBUNIT: Interacts with ASCC1; ASCC2 AND TRIP4.
CC       {ECO:0000250|UniProtKB:P21291}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21291}.
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DR   EMBL; U09567; AAC52157.1; -; mRNA.
DR   EMBL; BC062407; AAH62407.1; -; mRNA.
DR   PIR; S53580; S53580.
DR   RefSeq; NP_058844.1; NM_017148.2.
DR   AlphaFoldDB; P47875; -.
DR   SMR; P47875; -.
DR   IntAct; P47875; 2.
DR   STRING; 10116.ENSRNOP00000011991; -.
DR   iPTMnet; P47875; -.
DR   PhosphoSitePlus; P47875; -.
DR   jPOST; P47875; -.
DR   PaxDb; P47875; -.
DR   PRIDE; P47875; -.
DR   GeneID; 29276; -.
DR   KEGG; rno:29276; -.
DR   UCSC; RGD:62053; rat.
DR   CTD; 1465; -.
DR   RGD; 62053; Csrp1.
DR   VEuPathDB; HostDB:ENSRNOG00000008937; -.
DR   eggNOG; KOG1700; Eukaryota.
DR   HOGENOM; CLU_054591_1_0_1; -.
DR   InParanoid; P47875; -.
DR   OMA; VQCEGHS; -.
DR   OrthoDB; 1214165at2759; -.
DR   PhylomeDB; P47875; -.
DR   TreeFam; TF313758; -.
DR   PRO; PR:P47875; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000008937; Expressed in lung and 20 other tissues.
DR   Genevisible; P47875; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO: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:0007399; P:nervous system development; NAS: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; Isopeptide bond; LIM domain; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc.
FT   CHAIN           1..193
FT                   /note="Cysteine and glycine-rich protein 1"
FT                   /id="PRO_0000075718"
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         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         84
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97315"
FT   MOD_RES         112
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P21291"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P21291"
FT   MOD_RES         137
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97315"
FT   MOD_RES         161
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97315"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        91
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P21291"
SQ   SEQUENCE   193 AA;  20613 MW;  02421D8C6616F194 CRC64;
     MPNWGGGKKC GVCQKTVYFA EEVQCEGNSF HKSCFLCMVC KKNLDSTTVA VHGEEIYCKS
     CYGKKYGPKG YGYGQGAGTL SMDKGESLGI KHEEAPGHRP TTNPNASKFA QKIGGSERCP
     RCSQAVYAAE KVIGAGKSWH KSCFRCAKCG KGLESTTLAD KDGEIYCKGC YAKNFGPKGF
     GFGQGAGALV HSE