Overview
| Uniprot ID | P50461 |
|---|
| Protein Name | Cysteine and glycine-rich protein 3 |
|---|
| Gene Name | CSRP3 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 109 |
VTTSNPSKFTAKFGE |
Function
Positive regulator of myogenesis. Acts as a 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 (By similarity). 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 (By similarity). The role in regulation of cytoskeleton dynamics by association with CFL2 is reported conflictingly: Shown to enhance CFL2-mediated F-actin depolymerization dependent on the CSRP3:CFL2 molecular ratio, and also shown to reduce the ability of CLF1 and CFL2 to enhance actin depolymerization (PubMed:19752190, PubMed:24934443). Proposed to contribute to the maintenance of muscle cell integrity 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 (PubMed:24934443). In vitro can inhibit PKC/PRKCA activity (PubMed:27353086). Proposed to be involved in cardiac stress signaling by down-regulating excessive PKC/PRKCA signaling (By similarity)
Protein Sequence
10
MPNWGGGAKC
20
GACEKTVYHA
30
EEIQCNGRSF
40
HKTCFHCMAC
50
RKALDSTTVA
60
AHESEIYCKV
70
CYGRRYGPKG
80
IGYGQGAGCL
90
STDTGEHLGL
100
QFQQSPKPAR
110
SVTTSNPSKF
120
TAKFGESEKC
130
PRCGKSVYAA
140
EKVMGGGKPW
150
HKTCFRCAIC
160
GKSLESTNVT
170
DKDGELYCKV
180
CYAKNFGPTG
190
IGFGGLTQQV
EKKE
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005856 |
cytoskeleton |
| Molecular Function |
GO:0042802 |
identical protein binding |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0008307 |
structural constituent of muscle |
| Molecular Function |
GO:0031433 |
telethonin binding |
| Biological Process |
GO:0060048 |
cardiac muscle contraction |
| Biological Process |
GO:0003300 |
cardiac muscle hypertrophy |
| Biological Process |
GO:0048738 |
cardiac muscle tissue development |
| Biological Process |
GO:0055003 |
cardiac myofibril assembly |
| Biological Process |
GO:0035995 |
detection of muscle stretch |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0072594 |
establishment of protein localization to organelle |
| Biological Process |
GO:0006874 |
intracellular calcium ion homeostasis |
| Biological Process |
GO:0060537 |
muscle tissue development |
| Biological Process |
GO:1903919 |
negative regulation of actin filament severing |
| Biological Process |
GO:0045662 |
negative regulation of myoblast differentiation |
| Biological Process |
GO:1903920 |
positive regulation of actin filament severing |
| Biological Process |
GO:0045663 |
positive regulation of myoblast differentiation |
| Biological Process |
GO:0045944 |
positive regulation of transcription by RNA polymerase II |
| Biological Process |
GO:0002026 |
regulation of the force of heart contraction |
| Biological Process |
GO:0045214 |
sarcomere organization |
| Biological Process |
GO:0007519 |
skeletal muscle tissue development |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0030018 |
Z disc |
| Molecular Function |
GO:0003779 |
actin binding |
| Molecular Function |
GO:0042805 |
actinin binding |
Reference
[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.