2CT4


Conserved Protein Domain Family
SH3_CIP4-like

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cd11911: SH3_CIP4-like 
Click on image for an interactive view with Cn3D
Src Homology 3 domain of Cdc42-Interacting Protein 4
This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. Members of this subfamily typically contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of CIP4 associates with Gapex-5, a Rab31 GEF. 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: 212844
Aligned: 24 rows
Threshold Bit Score: 71.907
Created: 31-May-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             # #  #    #                  ##                 # ##   
2CT4_A         9 HCVAIYHFEGSse-gTISMAEGEDLSLMEEDkgDGWTRVRRKe----gGEGYVPTSYLRV 63  human
NP_001097501 603 KCRALYPFEASse-gSIPMSEGEELQVIEIDqgDGWTRVRREnnsngwDEGFVPTSYIEI 661 fruit fly
XP_002413948 521 RALAMYPFDAQse-gSIPMEEGEEFLVVEVDqgDGWTRVRREn----lEEGFVPTSYLEV 575 black-legged tick
ADY43796     461 TCTALYPFEGGse-gTMAMNEGDEMVLIEKDegDGWTRVRHIss---gREGFVPTSYLQC 516 pig roundworm
EFV55871     452 KAVALYDFDGTte-gTTSVHENEQLLVLEIDtgDGWTKIRKVnsttseSDGFVPTSYLSL 510 Trichinella spiralis
NP_741723    531 EAIAQFAFDGAqd-gTIRMEANEKLWLIEKDegDGWTRVRKEnn---sADGFVPSSYLKV 586 nematode
EFX66384     580 TCRALYAFEAQse-gSIPLHEGEELLVIEVDqgDGWTRVRRNsg---fEEGFVPTSYIQC 635 common water flea
CBY35567     278 RATVLFDFTGEkshdTISVRTGEIIDVSMRDv-DGWSKIKKVen---gEEGYIPTTYFKL 333 Oikopleura dioica
Q5T0N5       542 HCKAIYPFDGHne-gTLAMKEGEVLYIIEEDkgDGWTRARRQn----gEEGYVPTSYIDV 596 human
Q8R511       553 TCKALYTFEGQne-gTISVVEGETLSVIEEDkgDGWTRIRRNe----dEEGYVPTSYVEV 607 Norway rat

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