CSRP1_COTJA
ID CSRP1_COTJA Reviewed; 192 AA.
AC P67967; P32965;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 76.
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 Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic fibroblast;
RX PubMed=7499425; DOI=10.1074/jbc.270.48.28946;
RA Weiskirchen R., Pino J.D., Macalma T., Bister K., Beckerle M.C.;
RT "The cysteine-rich protein family of highly related LIM domain proteins.";
RL J. Biol. Chem. 270:28946-28954(1995).
CC -!- FUNCTION: Heat stable protein, that interacts with zyxin/ZYX. May be a
CC component of a signal transduction pathway that mediates adhesion-
CC stimulated changes in gene expression. {ECO:0000250|UniProtKB:P67966}.
CC -!- SUBUNIT: Interacts with ZYX. {ECO:0000250|UniProtKB:P67966}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21291}. Cytoplasm
CC {ECO:0000250|UniProtKB:P67966}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P67966}. Note=Associates with the actin
CC cytoskeleton. {ECO:0000250|UniProtKB:P67966}.
CC -!- DOMAIN: Glycine-rich repeats mediate the association with the actin
CC cytoskeleton. {ECO:0000305}.
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DR EMBL; Z28333; CAA82187.1; -; mRNA.
DR PIR; S38879; S38879.
DR RefSeq; XP_015740342.1; XM_015884856.1.
DR RefSeq; XP_015740344.1; XM_015884858.1.
DR AlphaFoldDB; P67967; -.
DR SMR; P67967; -.
DR Ensembl; ENSCJPT00005013423; ENSCJPP00005008922; ENSCJPG00005007905.
DR GeneID; 107324658; -.
DR KEGG; cjo:107324658; -.
DR CTD; 1465; -.
DR GeneTree; ENSGT00940000156777; -.
DR OrthoDB; 1214165at2759; -.
DR Proteomes; UP000694412; Chromosome 26.
DR GO; GO:0031252; C:cell leading edge; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; ISS:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..192
FT /note="Cysteine and glycine-rich protein 1"
FT /id="PRO_0000075720"
FT DOMAIN 10..61
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 118..169
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"
SQ SEQUENCE 192 AA; 20385 MW; 43D3D301938BBCE3 CRC64;
MPNWGGGKKC GVCQKAVYFA EEVQCEGSSF HKSCFLCMVC KKNLDSTTVA VHGDEIYCKS
CYGKKYGPKG YGYGMGAGTL STDKGESLGI KYEEGQSHRP TNPNASRMAQ KVGGSDGCPR
CGQAVYAAEK VIGAGKSWHK SCFRCAKCGK SLESTTLADK DGEIYCKGCY AKNFGPKGFG
FGQGAGALIH SQ