1NEU


Conserved Protein Domain Family
IgV_P0-like

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cd05715: IgV_P0-like 
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins
The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.
Statistics
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PSSM-Id: 409380
Aligned: 6 rows
Threshold Bit Score: 196.881
Created: 12-Sep-2007
Updated: 25-Oct-2021
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:tetramer interface [polypeptide binding site]
Evidence:
  • Comment:Tetrameric association of P0ex domains inferred from crystal contacts and supported by analytical ultracentrifugation.
  • Citation:PMID 8816707
  • Comment:P0ex tetramer is comprised of four molecules arranged around a central hole.
  • Comment:P0ex domains, may come from one membrane surface as tetramers, that link to POex tetramers from the opposing membrane surface.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1      # #           #       #                                              #  #      
1NEU_A      1 IVVYTDREVYGAVGSQVTLHCSFWSsewv-sddISFTWRYQPeggrDAISIFHYAk--GQPYIDevgtFKERIQWVGDPS 77  Norway rat
ABF47243   34 MDVLVPALINALNGSDVRITCTFTScykldpskFAMNWTYQEts-nSTEEMFMTYkntYKMIPLkpsrFGERVMFTGNLD 112 zebrafish
O60487     27 VEIYTSRVLEAVNGTDARLKCTFSSfapv-gdaLTVTWNFRPldggPEQFVFYYH---IDPFQPmsgrFKDRVSWDGNPE 102 human
O60939     30 MEVTVPATLNVLNGSDARLPCTFNScytvnhkqFSLNWTYQEcn-nCSEEMFLQFr--MKIINLklerFQDRVEFSGNPS 106 human
O95297     38 LEVYTPKEIFVANGTQGKLTCKFKStstt-gglTSVSWSFQPegadTTVSFFHYSq--GQVYLGnyppFKDRISWAGDLD 114 human
XP_416652  20 VEVTTPEEMFVENETDVKLPCTFTSaevi-ssaASVSWSFQPegaaTRISFFYYSn--GKPYTGkdipFKDRVTWAGDLN 96  chicken
Feature 1             ##                              
1NEU_A     78 WKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 117 Norway rat
ABF47243  113 KNDLSITISDVQLTDEGIYNCYVRNPPDRIQGHGTIQFAV 152 zebrafish
O60487    103 RYDASILLWKLQFDDNGTYTCQVKNPPDVDGVIGEIRLSV 142 human
O60939    107 KYDVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQV 146 human
O95297    115 KKDASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYV 154 human
XP_416652  97 KKDASISISNMQFQDNGTYICDVKNPPDIVVKPGEIRLRV 136 chicken

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