2MBX,3FS7,1A75,1TTX


Conserved Protein Domain Family
EFh_parvalbumin_beta

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cd16255: EFh_parvalbumin_beta 
Click on image for an interactive view with Cn3D
EF-hand, calcium binding motif, found in beta-parvalbumin
Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).
Statistics
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PSSM-Id: 319998
Aligned: 10 rows
Threshold Bit Score: 134.088
Created: 19-Nov-2014
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:Ca binding site [ion binding site]
Evidence:
  • Structure:2MBX; Gadus morhua parvalbumin Gad M 1 binds two Ca2+ ions.
  • Structure:3FS7; Gallus gallus beta-parvalbumin binds two Ca2+ ions.
  • Structure:1TTX; Homo sapiens beta parvalbumin binds two Ca2+ ions.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                   # # #   #  #                         
2MBX_A         9 DADITAALAACKAEGSFDHKAFFTKVGLAAkspaDIKKVFEIIDQDKSDFVEEDELKLFLQNFSagaralsdaETKVFLK 88  Atlantic cod
3FS7_A         9 AKDIESALSSCQAADSFNYKSFFSTVGLSSktpdQIKKVFGILDQDKSGFIEEEELQLFLKNFSssarvltsaETKAFLA 88  chicken
1A75_A         8 DADCAAAVKACEAADSFSYKAFFAKCGLSGksadDIKKAFVFIDQDKSGFIEEDELKLFLQVFKagaraltdaETKAFLK 87  whiting
1TTX_A         9 ADDIAAALQECRDPDTFEPQKFFQTSGLSKmsanQVKDVFRFIDNDQSGYLDEEELKFFLQKFEsgareltesETKSLMA 88  human
P05940         9 EADISAALQNCQAADSFNFKTFFAQSGLSSksadDVKNVFAILDQDRSGFIEEEELKLFLQNFSasaraltdaETKAFLA 88  African clawed ...
WP_026052281   9 DADVTAALQACQAVDSFNYKGFFAKVGLSAktpdVIKKAFAVIDQDKSGFIEEDELKLFLQNFSagaraltdaETKAFLK 88  Herbaspirillum
XP_007891755   9 AADIASAVSQCSAVNSFCHKKFFTTCGLSKksetDVKKVFKVLDQDQSGYIEDAELKLFLQSFStgarelteaETAAFLK 88  elephant shark
NP_001279781   9 ASDIDSAISQFSAPDSLNLKKFFEASGLSRksadEVAKVFEIMDQDNNGFIEKEEIKKFLQFFSsrartlteaEIQIFIA 88  elephant shark
XP_007907985   9 AGDVAAALAQCKAADSFSFKQFCATSGLAKkssdTVNKIFNIIDEDGSGYIEAKELKFFLQNFSsdarelgdsEIKTVLS 88  elephant shark
XP_007891758   9 ASDISNAIKECQALESFDFKKFFQTSGLSRksadEIKNVFLAMDDDDSGYIELDELKFFLQRFSpiarvlteaETEAFLK 88  elephant shark
Feature 1          # # #      #       
2MBX_A        89 AGDSDGDGKIGVDEFGAMIKA 109 Atlantic cod
3FS7_A        89 AGDTDGDGKIGVEEFQSLVKA 109 chicken
1A75_A        88 AGDSDGDGAIGVEEWVALVKA 108 whiting
1TTX_A        89 AADNDGDGKIGAEEFQEMVHS 109 human
P05940        89 AGDSDGDGKIGVEEFQSLVKP 109 African clawed frog
WP_026052281  89 AGDSDGDGKIGVDEFAAMVKA 109 Herbaspirillum
XP_007891755  89 AGDEDGDGMIGADEFWKLVSA 109 elephant shark
NP_001279781  89 AGDKDSDGKIGITEFQRMVSA 109 elephant shark
XP_007907985  89 AMGMSDDGKMNATEFQKLVSA 109 elephant shark
XP_007891758  89 AADTDGDERIGTQEFVTLVMS 109 elephant shark

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