CSRP1_CHICK
ID CSRP1_CHICK Reviewed; 192 AA.
AC P67966; P32965;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH ZYX,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic fibroblast;
RX PubMed=8294495; DOI=10.1083/jcb.124.1.117;
RA Crawford A.W., Pino J.D., Beckerle M.C.;
RT "Biochemical and molecular characterization of the chicken cysteine-rich
RT protein, a developmentally regulated LIM-domain protein that is associated
RT with the actin cytoskeleton.";
RL J. Cell Biol. 124:117-127(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-50; 70-84; 112-130 AND 178-189, AND INTERACTION WITH
RP ZYX.
RX PubMed=1469049; DOI=10.1083/jcb.119.6.1573;
RA Sadler I., Crawford A.W., Michelsen J.W., Beckerle M.C.;
RT "Zyxin and cCRP: two interactive LIM domain proteins associated with the
RT cytoskeleton.";
RL J. Cell Biol. 119:1573-1587(1992).
RN [3]
RP ZINC-BINDING.
RX PubMed=8506279; DOI=10.1073/pnas.90.10.4404;
RA Michelsen J.W., Schmeichel K.L., Beckerle M.C., Winge D.R.;
RT "The LIM motif defines a specific zinc-binding protein domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4404-4408(1993).
RN [4]
RP MUTAGENESIS.
RX PubMed=8157637; DOI=10.1016/s0021-9258(19)78098-3;
RA Michelsen J.W., Sewell A.K., Louis H.A., Olsen J.I., Davis D.R.,
RA Winge D.R., Beckerle M.C.;
RT "Mutational analysis of the metal sites in an LIM domain.";
RL J. Biol. Chem. 269:11108-11113(1994).
RN [5]
RP STRUCTURE BY NMR OF C-TERMINAL LIM DOMAIN.
RX PubMed=7664053; DOI=10.1038/nsb0694-388;
RA Perez-Alvarado G.C., Miles C., Michelsen J.W., Louis H.A., Winge D.R.;
RT "Structure of the carboxy-terminal LIM domain from the cysteine rich
RT protein CRP.";
RL Nat. Struct. Biol. 1:388-398(1994).
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:0000269|PubMed:8294495}.
CC -!- SUBUNIT: Probable monomer. Interacts with ZYX.
CC {ECO:0000269|PubMed:1469049, ECO:0000269|PubMed:8294495}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21291}. Cytoplasm
CC {ECO:0000269|PubMed:8294495}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8294495}. Note=Associates with the actin
CC cytoskeleton. {ECO:0000269|PubMed:8294495}.
CC -!- TISSUE SPECIFICITY: Most prominent in tissues that are enriched in
CC smooth muscle cells, such as gizzard, stomach, and intestine. Lower
CC level in the heart, no expression in liver, skeletal muscle, or brain.
CC {ECO:0000269|PubMed:8294495}.
CC -!- DEVELOPMENTAL STAGE: Expression levels increase dramatically during
CC smooth muscle maturation.
CC -!- DOMAIN: Glycine-rich repeats mediate the association with the actin
CC cytoskeleton. {ECO:0000305}.
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DR EMBL; X73831; CAA52053.1; -; mRNA.
DR PIR; A49648; A49648.
DR PIR; B44358; B44358.
DR PIR; C44358; C44358.
DR RefSeq; NP_990579.1; NM_205248.1.
DR RefSeq; XP_015154179.1; XM_015298693.1.
DR PDB; 1B8T; NMR; -; A=1-192.
DR PDB; 1CTL; NMR; -; A=108-192.
DR PDBsum; 1B8T; -.
DR PDBsum; 1CTL; -.
DR AlphaFoldDB; P67966; -.
DR SMR; P67966; -.
DR STRING; 9031.ENSGALP00000000423; -.
DR PaxDb; P67966; -.
DR Ensembl; ENSGALT00000000424; ENSGALP00000000423; ENSGALG00000000318.
DR GeneID; 396176; -.
DR KEGG; gga:396176; -.
DR CTD; 1465; -.
DR VEuPathDB; HostDB:geneid_396176; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000156777; -.
DR HOGENOM; CLU_054591_1_0_1; -.
DR InParanoid; P67966; -.
DR OMA; VQCEGHS; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; P67966; -.
DR EvolutionaryTrace; P67966; -.
DR PRO; PR:P67966; -.
DR Proteomes; UP000000539; Chromosome 26.
DR Bgee; ENSGALG00000000318; Expressed in colon and 13 other tissues.
DR GO; GO:0031252; C:cell leading edge; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005925; C:focal adhesion; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IDA:AgBase.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0042805; F:actinin binding; IBA:GO_Central.
DR GO; GO:0051393; F:alpha-actinin binding; IPI:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:AgBase.
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 DisProt; DP00922; -.
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; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW LIM domain; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1469049"
FT CHAIN 2..192
FT /note="Cysteine and glycine-rich protein 1"
FT /id="PRO_0000075719"
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"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1B8T"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1B8T"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1B8T"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1CTL"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1B8T"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1B8T"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:1B8T"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:1B8T"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1CTL"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1CTL"
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
