2DE0


Conserved Protein Domain Family
SH3_Fut8

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cd11792: SH3_Fut8 
Click on image for an interactive view with Cn3D
Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8)
Fut8 catalyzes the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype. Fut8 is also implicated to play roles in aging and cancer metastasis. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear. 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: 212726
Aligned: 30 rows
Threshold Bit Score: 73.7807
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             # #  #                       #                            ##              #
2DE0_X       444 NQIAIYAHQPRt--------------------ADEIPMEPGDIIGVAGNh-----------wDGYSKGVNRKlgRTGLYP 492 human
NP_504555    493 EVIVIEDHIAQn--------------------NKEIDLKVGDKVGIAGNh-----------wNGYSKGTNRQtyKEGVFP 541 nematode
XP_002108642 337 RHKAIYPHAARr--------------------QGEIDLAVGDIIAVAGNh-----------wDGYSKGRVQGkgWDGLYP 385 Trichoplax adha...
XP_002166972  36 KTRVIWPHTAKg--------------------RSELDLRVGDVIGIAGNh-----------wNGQAKGLLHNlqKTGLFP 84  green hydra
XP_002125085 505 IQVAIYPHTANa-------------------tTHEIELKIGDIIYTDTNl-----------wNGYFRGRTRRtgEVGMYP 554 Ciona intestinalis
XP_002170367 478 AMKVIWPNIKTs--------------------NDELKLDIGDTIKIAGNh-----------wDGKSIGKNLLtqEVGSFF 526 green hydra
XP_002408966 422 PRRVLYEHRALn--------------------HKELWLRSGDIVERLGDhsvigearrkkmwDGYSVGTLPGtiLTGLYP 481 black-legged tick
XP_002121481 488 KQVAIMDHKPPtsqlcngttf-rspipemrkwTCELELRVGDQLQSFGYmy----------hSYLSGGYNRRskLHGVYP 556 Ciona intestinalis
NP_001128497 418 LHKAVMDHKPSlgfckraapdmrqidlskmelMCEIEIKVGDIIEVSPEsy----------hGYRSAGKNVRtqMFGAYP 487 Ciona intestinalis
XP_002131079 419 VHEAIMNHNPTrdecqrafmqmsptylsqmedMCEIELKIGDKIEVWPEif----------hGYKSGGRNFRtqKFGAYP 488 Ciona intestinalis
Feature 1         ##   
2DE0_X       493 SYKVRE 498 human
NP_504555    542 SYKVVN 547 nematode
XP_002108642 386 SYKTED 391 Trichoplax adhaerens
XP_002166972  85 AYKIED 90  green hydra
XP_002125085 555 TYKVKD 560 Ciona intestinalis
XP_002170367 527 SYKAED 532 green hydra
XP_002408966 482 LYKTVP 487 black-legged tick
XP_002121481 557 THKVKD 562 Ciona intestinalis
NP_001128497 488 LFKVKD 493 Ciona intestinalis
XP_002131079 489 MFKVKE 494 Ciona intestinalis

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