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Protein

Cysteine and glycine-rich protein 3

Gene

Csrp3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Positive regulator of myogenesis. Acts as cofactor for myogenic bHLH transcription factors such as MYOD1, and probably MYOG and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3 isoform E47 complex and may promote formation of a functional MYOD1:TCF3 isoform E47:MEF2A complex involved in myogenesis (PubMed:7954791, PubMed:9234731). Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation. The role in regulation of cytoskeleton dynamics by association with CFL2 is reported conflictingly. Proposed to contribute to the maintenance of muscle cell integerity through an actin-based mechanism. Can directly bind to actin filaments, cross-link actin filaments into bundles without polarity selectivity and protect them from dilution- and cofilin-mediated depolymerization; the function seems to involve its self-association. In vitro can inhibit PKC/PRKCA activity. Proposed to be involved in cardiac stress signaling by down-regulating excessive PKC/PRKCA signaling (By similarity).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Developmental protein
Biological processDifferentiation, Myogenesis, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine and glycine-rich protein 3
Alternative name(s):
Cysteine-rich protein 3
Short name:
CRP3
LIM domain protein, cardiac
Muscle LIM protein
Gene namesi
Name:Csrp3
Synonyms:Clp, Mlp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71092 Csrp3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000757291 – 194Cysteine and glycine-rich protein 3Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei95PhosphoserineBy similarity1
Modified residuei111PhosphoserineBy similarity1
Modified residuei153PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by PKC/PRKCA.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP50463
PRIDEiP50463

PTM databases

iPTMnetiP50463
PhosphoSitePlusiP50463

Expressioni

Tissue specificityi

High in striated muscle and adult heart.

Interactioni

Subunit structurei

Self-associates. Oligomeric in the cytoplasm and monomeric in the nucleus (PubMed:16963613). Homooligomers preferentially form along the actin cytoskeleton (By similarity). Interacts with TCAP, ACTN2 and NRAP (By similarity). Interacts with LDHD, SPTB, MYOD1, MYOG, MYF6. Interacts with GLRX3 (via C-terminus); GLRX3 and calcineurin compete for interaction with CSRP3 (PubMed:9234731, PubMed:10751147, PubMed:12127981, PubMed:18258855). Interacts with CFL2; the stoichiometry influences F-actin depolymerization and possibly two molecules of CFL2 can interact with one molecule of CSRP3 resulting in the highest functional impact; the interaction is stronger with phosphorylated CFL2 (By similarity).By similarity5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

IntActiP50463, 5 interactors
STRINGi10116.ENSRNOP00000019310

Structurei

3D structure databases

ProteinModelPortaliP50463
SMRiP50463
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 61LIM zinc-binding 1PROSITE-ProRule annotationAdd BLAST52
Domaini120 – 171LIM zinc-binding 2PROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 5Interaction with TCAPBy similarity5
Regioni94 – 105Interaction with CLF2By similarityAdd BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi64 – 69Nuclear localization signalSequence analysis1 Publication6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi63 – 78Gly-richAdd BLAST16
Compositional biasi177 – 185Gly-rich9

Domaini

LIM zinc-binding domain 1 is required for self-association. LIM zinc-binding domain 1 and LIM zinc-binding domain 2 both are required for optimal actin-bundling activity (By similarity). LIM zinc-binding domain 1 mediates binding to MYOD1. LIM zinc-binding domain 2 mediates binding to SPTB (PubMed:9234731, PubMed:10751147).By similarity2 Publications

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiENOG410ITI8 Eukaryota
ENOG410Z840 LUCA
HOGENOMiHOG000111233
HOVERGENiHBG051143
InParanoidiP50463
KOiK09377
PhylomeDBiP50463

Family and domain databases

InterProiView protein in InterPro
IPR001781 Znf_LIM
PfamiView protein in Pfam
PF00412 LIM, 2 hits
SMARTiView protein in SMART
SM00132 LIM, 2 hits
PROSITEiView protein in PROSITE
PS00478 LIM_DOMAIN_1, 2 hits
PS50023 LIM_DOMAIN_2, 2 hits

Sequencei

Sequence statusi: Complete.

P50463-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNWGGGAKC GACDKTVYHA EEIQCNGRSF HKTCFHCMAC RKALDSTTVA
60 70 80 90 100
AHESEIYCKV CYGRKYGPKG IGFGQGAGCL STDTGEHLGL QFQQSPKPAR
110 120 130 140 150
AATTSNPSKF SAKFGESEKC PRCGKSVYAA EKVMGGGKPW HKTCFPCAIC
160 170 180 190
GKSLESTNVT DKDGELYCKV CYAKNFGPTG IGFGGLTHQV EKKE
Length:194
Mass (Da):20,803
Last modified:October 1, 1996 - v1
Checksum:i2D6848C271BA7EAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81193 mRNA Translation: CAA57065.1
PIRiA55099
RefSeqiNP_476485.1, NM_057144.1
UniGeneiRn.11345

Genome annotation databases

GeneIDi117505
KEGGirno:117505
UCSCiRGD:71092 rat

Similar proteinsi

Entry informationi

Entry nameiCSRP3_RAT
AccessioniPrimary (citable) accession number: P50463
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health