1I49,1I4D


Conserved Protein Domain Family
BAR_Arfaptin_like

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cd00011: BAR_Arfaptin_like 
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The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-like proteins, a dimerization module that binds and bends membranes
The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization, lipid binding and curvature sensing module present in Arfaptins, PICK1, ICA69, and similar proteins. Arfaptins are ubiquitously expressed proteins implicated in mediating cross-talk between Rac, a member of the Rho family GTPases, and Arf (ADP-ribosylation factor) small GTPases. Arfaptins bind to GTP-bound Arf1, Arf5, and Arf6, with strongest binding to GTP-Arf1. Arfaptins also binds to Rac-GTP and Rac-GDP with similar affinities. The Arfs are thought to bind to the same surface as Rac, and their binding is mutually exclusive. Protein Interacting with C Kinase 1 (PICK1) plays a key role in the trafficking of AMPA receptors, which are critical for regulating synaptic strength and may be important in cellular processes involved in learning and memory. Islet cell autoantigen 69-kDa (ICA69) is a diabetes-associated autoantigen that is involved in membrane trafficking at the Golgi complex in neurosecretory cells. ICA69 associates with PICK1 through their BAR domains to form a heterodimer which is involved in regulating the synaptic targeting and surface expression of AMPA receptors. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Statistics
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PSSM-Id: 153270
View PSSM: cd00011
Aligned: 4 rows
Threshold Bit Score: 245.218
Threshold Setting Gi: 14277759
Created: 4-Sep-2001
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interfaceRac binding
Conserved site includes 33 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Structure:1I49; interface between monomers of human Arfaptin dimer; defined at 4A contacts.
    View structure with Cn3D
  • Structure:1I4D; interface between monomers of human Arfaptin dimer-Rac complex; defined at 4A contacts.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                     ##     #   #  #  ##  #  ##   # ##  #  ##    ## ##  #   #        
1I49_A      6 DLELELQIELLRETKRKYESVLQLGRALTAHLYSLLQTQHALGDAFADLSQKSPELq--EEFGYNAETQKLLCKNGETLL 83  human
1I4D_A      6 DLELELQIELLRETKRKYESVLQLGRALTAHLYSLLQTQHALGDAFADLSQKSPELq--EEFGYNAETQKLLCKNGETLL 83  human
NP_963881  54 DADLDAKLEFFRSVQSTCTELLKVIEKYQQRITHLSQEENELGLFLRFQAEHDKTKa-gSMMDATSKALCCSAKQRLALC 132 zebrafish
Q62083    146 NDGLVKRLEELERTAELYKGMTEHTKNLLRAFYDVSQTHRAFGDVFSVIGVRDAQPaasEAFVKFADAHRSIEKFGIRLL 225 house mouse
Feature 1                                                                                     
1I49_A     84 GAVNFFVSSINTLVTKTMEDTLMTVKQYEAARLEYDAYRTDLEELSLGprd-----------agTRGRLESAQATFQAHR 152 human
1I4D_A     84 GAVNFFVSSINTLVTKTMEDTLMTVKQYEAARLEYDAYRTDLEELSLGprd-----------agTRGRLESAQATFQAHR 152 human
NP_963881 133 TPLHRLEQKVETFRRRAIADSLLTVSRMEKARTEYRAALLWMKASSQEldpd---------tykQLEKFRMVQAQVRETK 203 zebrafish
Q62083    226 KTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEeysciaarralyrvstGNYEYRLILRCRQEAR 305 house mouse
Feature 1                         #   ##  ## ##      ## ##         
1I49_A    153 DKYEKLRGDVAIKLKFLEENKIkvMHKQLLLFHNAVSAYFAGNQKQLEQTLQQ 205 human
1I4D_A    153 DKYEKLRGDVAIKLKFLEENKIkvMHKQLLLFHNAVSAYFAGNQKQLEQTLQQ 205 human
NP_963881 204 VCFDKLKNDVCQKVDMLGASRCnmLSHSLCTYQTTLLQYWEKTAHVMSGIHEA 256 zebrafish
Q62083    306 ARFSQMRKDVLEKMELLDQKHVqdIVFQLQRFVSTMSKYYNDCYAVLQDADVF 358 house mouse

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