1VYU,1T0H,1VYV


Conserved Protein Domain Family
SH3_CACNB

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cd11863: SH3_CACNB 
Click on image for an interactive view with Cn3D
Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta
Voltage-dependent calcium channels (Ca(V)s) are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Statistics
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PSSM-Id: 212797
Aligned: 22 rows
Threshold Bit Score: 100.815
Created: 31-Mar-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
peptide ligand
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:peptide ligand binding site [polypeptide binding site]
Evidence:
  • Comment:based on the binding of peptide ligands to the SH3 domains of other superfamily members
  • Comment:SH3 domains typically bind proline-rich ligands, preferentially to PxxP motifs.
  • Citation:PMID 7664083
  • Citation:PMID 7735837
  • Comment:flanking hinge and loops (RT and n-Src) confer sequence specificity for ligand residues outside the core binding motif

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1              # #  #            #                 ##               # ## 
1VYU_A        47 FAVRTNVSYCGVl--dEECPVQGSGVNFEAKDFLHIKEKYsNDWWIGRLVkeggDIAFIPSPQR 108 Norway rat
Q8R3Z5       103 FAVRTNVGYNPSp--gDEVPVQGVAITFEPKDFLHIKEKYnNDWWIGRLVkegcEVGFIPSPVK 164 house mouse
1T0H_A        49 FAVRTNVRYSAAq--eDDVPVPGXAISFEAKDFLHVKEKFnNDWWIGRLVkegcEIGFIPSPVK 110 Norway rat
2654496       77 FAMRANYGYNGAe--dDDSPIHGMALSFEPKDFLHIKEKFnNDWLIGRVVregcDIGFIPSPSK 138 Cyanea capillata
CBY20685     148 FAVRANIFFYGVp--cDDCPASGNQVTFEARDYIHIKEKYsTDWWIGRLVregcELGFVPSAAK 209 Oikopleura dioica
XP_002110341  36 FAVRANVGFNGSv--dDDSPLPGYAVSFDSKSFLHVIEEFnEEWWIGRVVkvgaGFGFVPSPIK 97  Trichoplax adhaerens
H87731        60 FAVQAMRDYDGSl--dEKSPLKDHTISFNTNDFIHIHTKFnSDWWIGRIVrshsEFGFVPTARR 121 nematode
CBY08324      54 FTVKTSVGYNGKieddAPLIGHGKFVSFEPDDFLHIKEKYdEFWWIGRVVspdsELGFIPSPTK 117 Oikopleura dioica
CBY42208      99 FSVRAKLGFIAGtk-dLCGNLRDYLVTFENKDYLHIIEKFnNDWWIGRVVregcDFCFIPSPLK 161 Oikopleura dioica
ACK86666      41 FAIRSNIAFNAEylspEDVPLPAHMITFGVKDFLHVKERFnQDWWIARLVriggSLGFIPSPAK 104 Dugesia japonica

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