CSRP3_BOVIN
ID CSRP3_BOVIN Reviewed; 194 AA.
AC Q4U0T9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cysteine and glycine-rich protein 3;
DE AltName: Full=Cysteine-rich protein 3;
DE Short=CRP3;
GN Name=CSRP3;
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 [MRNA].
RC STRAIN=Korean; TISSUE=Skeletal muscle;
RA Yu S.L., Chung H.J., Jung K.C., Lee Y.J., Lee J.H., Yoon D.H., Lee S.H.,
RA Sang B.C.;
RT "Characterization of cysteine- and glycine-rich protein 3 (CSRP3) in Korean
RT cattle.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Positive regulator of myogenesis. Acts as cofactor for
CC myogenic bHLH transcription factors such as MYOD1, and probably MYOG
CC and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3 isoform
CC E47 complex and may promote formation of a functional MYOD1:TCF3
CC isoform E47:MEF2A complex involved in myogenesis. Plays a crucial and
CC specific role in the organization of cytosolic structures in
CC cardiomyocytes. Could play a role in mechanical stretch sensing. May be
CC a scaffold protein that promotes the assembly of interacting proteins
CC at Z-line structures. It is essential for calcineurin anchorage to the
CC Z line. Required for stress-induced calcineurin-NFAT activation. The
CC role in regulation of cytoskeleton dynamics by association with CFL2 is
CC reported conflictingly. Proposed to contribute to the maintenance of
CC muscle cell integrity through an actin-based mechanism. Can directly
CC bind to actin filaments, cross-link actin filaments into bundles
CC without polarity selectivity and protect them from dilution- and
CC cofilin-mediated depolymerization; the function seems to involve its
CC self-association. In vitro can inhibit PKC/PRKCA activity. Proposed to
CC be involved in cardiac stress signaling by down-regulating excessive
CC PKC/PRKCA signaling (By similarity). {ECO:0000250|UniProtKB:P50461,
CC ECO:0000250|UniProtKB:P50462}.
CC -!- SUBUNIT: Self-associates. Oligomeric in the cytoplasm and monomeric in
CC the nucleus. Homooligomers preferentially form along the actin
CC cytoskeleton. Interacts with TCAP, LDHD, MYOD1, MYOG, ACTN2, NRAP,
CC MYF6. Interacts (via N-terminus) with GLRX3 (via C-terminus) and
CC PPP3CA; GLRX3 and calcineurin compete for interaction with CSRP3.
CC Interacts with CFL2; the stoichiometry influences F-actin
CC depolymerization and possibly two molecules of CFL2 can interact with
CC one molecule of CSRP3 resulting in the highest functional impact; the
CC interaction is stronger with phosphorylated CFL2 (By similarity).
CC {ECO:0000250|UniProtKB:P50461, ECO:0000250|UniProtKB:P50462,
CC ECO:0000250|UniProtKB:P50463}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P50463}.
CC Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm
CC {ECO:0000250|UniProtKB:P50463}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:P50462}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:P50461}. Note=Nucleocytoplasmic shuttling
CC protein. Mainly cytoplasmic. In the Z line, found associated with GLRX3
CC (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P50462,
CC ECO:0000250|UniProtKB:P50463}.
CC -!- DOMAIN: LIM zinc-binding domain 1 is required for self-association. LIM
CC zinc-binding domain 1 and LIM zinc-binding domain 2 both are required
CC for optimal actin-bundling activity. LIM zinc-binding domain 1 mediates
CC binding to MYOD1. LIM zinc-binding domain 2 mediates binding to SPTB.
CC {ECO:0000250|UniProtKB:P50461, ECO:0000250|UniProtKB:P50463}.
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DR EMBL; DQ022067; AAY45897.1; -; mRNA.
DR EMBL; BC103108; AAI03109.1; -; mRNA.
DR RefSeq; NP_001019860.1; NM_001024689.3.
DR AlphaFoldDB; Q4U0T9; -.
DR STRING; 9913.ENSBTAP00000030304; -.
DR PaxDb; Q4U0T9; -.
DR Ensembl; ENSBTAT00000030320; ENSBTAP00000030304; ENSBTAG00000011869.
DR GeneID; 540407; -.
DR KEGG; bta:540407; -.
DR CTD; 8048; -.
DR VEuPathDB; HostDB:ENSBTAG00000011869; -.
DR VGNC; VGNC:27775; CSRP3.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000159533; -.
DR HOGENOM; CLU_054591_1_1_1; -.
DR InParanoid; Q4U0T9; -.
DR OMA; TCYGRRY; -.
DR OrthoDB; 1214165at2759; -.
DR TreeFam; TF313758; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000011869; Expressed in cardiac ventricle and 71 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042805; F:actinin binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0031433; F:telethonin binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
DR GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0035995; P:detection of muscle stretch; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0060537; P:muscle tissue development; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0070528; P:protein kinase C signaling; IEA:Ensembl.
DR GO; GO:0033365; P:protein localization to organelle; IEA:Ensembl.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0033292; P:T-tubule organization; IEA:Ensembl.
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 Actin-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; LIM domain; Metal-binding; Myogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..194
FT /note="Cysteine and glycine-rich protein 3"
FT /id="PRO_0000075726"
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 1..5
FT /note="Interaction with TCAP"
FT /evidence="ECO:0000250|UniProtKB:P50461"
FT REGION 94..106
FT /note="Interaction with CLF2"
FT /evidence="ECO:0000250|UniProtKB:P50461"
FT MOTIF 64..69
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P50463, ECO:0000255"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50462"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50463"
SQ SEQUENCE 194 AA; 20953 MW; DDE7A1E928FB7B1D CRC64;
MPNWGGGAKC GACEKTVYHA EEIQCNGRSF HKTCFHCMAC RKALDSTTVA AHESEIYCKV
CYGRRYGPKG IGYGQGAGCL STDTGEHLGL QFQQSPKQAR SATTSSNPSK FAKFGESEKC
PRCGKSVYAA EKVMGGGKPW HKTCFRCAIC GKSLESTNVT DKDGELYCKV CYAKNFGPTG
IGFGGLTHQV EKKD
