ID   CSRP2_COTJA             Reviewed;         194 AA.
AC   Q05158;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Cysteine and glycine-rich protein 2;
DE   AltName: Full=Cysteine-rich protein 2;
DE            Short=CRP2;
GN   Name=CSRP2;
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=8361751;
RA   Weiskirchen R., Bister K.;
RT   "Suppression in transformed avian fibroblasts of a gene (crp) encoding a
RT   cysteine-rich protein containing LIM domains.";
RL   Oncogene 8:2317-2324(1993).
RN   [2]
RP   STRUCTURE BY NMR OF 8-67.
RX   PubMed=9585524; DOI=10.1021/bi973055v;
RA   Kontaxis G., Konrat R., Kraeutler B., Weiskirchen R., Bister K.;
RT   "Structure and intramodular dynamics of the amino-terminal LIM domain from
RT   quail cysteine- and glycine-rich protein CRP2.";
RL   Biochemistry 37:7127-7134(1998).
RN   [3]
RP   STRUCTURE BY NMR OF 117-175.
RX   PubMed=9115265; DOI=10.1074/jbc.272.18.12001;
RA   Konrat R., Weiskirchen R., Krautler B., Bister K.;
RT   "Solution structure of the carboxyl-terminal LIM domain from quail
RT   cysteine-rich protein CRP2.";
RL   J. Biol. Chem. 272:12001-12007(1997).
CC   -!- FUNCTION: Interacts with zyxin. May be a component of a signal
CC       transduction pathway that mediates adhesion-stimulated changes in gene
CC       expression. Totally down-regulated in transformed cells.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; Z21643; CAA79759.1; -; mRNA.
DR   PIR; S41761; S41761.
DR   PDB; 1A7I; NMR; -; A=1-81.
DR   PDB; 1CXX; NMR; -; A=82-194.
DR   PDB; 1IBI; NMR; -; A=82-194.
DR   PDB; 1QLI; NMR; -; A=82-194.
DR   PDBsum; 1A7I; -.
DR   PDBsum; 1CXX; -.
DR   PDBsum; 1IBI; -.
DR   PDBsum; 1QLI; -.
DR   AlphaFoldDB; Q05158; -.
DR   SMR; Q05158; -.
DR   Ensembl; ENSCJPT00005027650; ENSCJPP00005020016; ENSCJPG00005016171.
DR   GeneTree; ENSGT00940000154980; -.
DR   EvolutionaryTrace; Q05158; -.
DR   Proteomes; UP000694412; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   DisProt; DP00438; -.
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   3D-structure; Developmental protein; Differentiation; LIM domain;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..194
FT                   /note="Cysteine and glycine-rich protein 2"
FT                   /id="PRO_0000075725"
FT   DOMAIN          10..61
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          120..171
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          85..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           64..69
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        96..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1A7I"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:1A7I"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:1A7I"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:1A7I"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:1A7I"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:1A7I"
FT   HELIX           60..65
FT                   /evidence="ECO:0007829|PDB:1A7I"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:1QLI"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:1CXX"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:1CXX"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:1CXX"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:1QLI"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:1CXX"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:1CXX"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:1IBI"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:1IBI"
FT   HELIX           169..174
FT                   /evidence="ECO:0007829|PDB:1CXX"
SQ   SEQUENCE   194 AA;  20911 MW;  D59CA624D1C1269E CRC64;
     MPNWGGGNKC GACGRTVYHA EEVQCDGRSF HRCCFLCMVC RKNLDSTTVA IHDAEVYCKS
     CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESSPSPHR PTTNPNTSKF AQKFGGAEKC
     SRCGDSVYAA EKVIGAGKPW HKNCFRCAKC GKSLESTTLT EKEGEIYCKG CYAKNFGPKG
     FGYGQGAGAL VHAQ