3MPX


Conserved Protein Domain Family
PH1_FGD5

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cd15792: PH1_FGD5 
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FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 5, N-terminal Pleckstrin Homology (PH) domain
FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Statistics
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PSSM-Id: 275435
View PSSM: cd15792
Aligned: 5 rows
Threshold Bit Score: 227.028
Threshold Setting Gi: 326671800
Created: 17-Oct-2014
Updated: 22-Oct-2014
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
3MPX_A        231 VRGQGDLLQPGREFLKEGTLXKVTGKNRRPRHLFLXNDVLLYTYPQKdGKYRLKNTLAVANXKVSRPVxekvpYALKIET 310  human
XP_001919894 1121 VRGKRDLLQPGRVFVKEGTLMKVSRKSRQPRHLFLMNDVMLYTYPQQdGKYRLKNTLTLSGMKVSKPIidnvlNTLRIEV 1200 zebrafish
XP_007060013 1218 VRGQSNLLQPGREFLKEGTLMKVSGKNRHPRHLFLMNDILLYTYPQKdGKYRLKNTLAVSGMRVNRPVtekaqNVLKIEY 1297 green sea turtle
XP_005997888 1405 RGHSHHFLQPGREFVKEGTLMKVSTRSKNPRHLFLMNDVLLYTYPQKnGKYRLKNTLAVAGLKISRPVlekatNVLKIEN 1484 coelacanth
XP_002938283 1209 VRGQRSLLQPGREFVKEGTLMKVSGRNRHPRHLFLMNDVLLYTYPLKdGKYRLKNTLSIPGMRVSRPIvenaqNVLKVEC 1288 western clawe...
3MPX_A        311 SESCLXLSASSCAERDEWYGCLSRALPEDYKAQALAAFHHSVE 353  human
XP_001919894 1201 SDVTITLSASSLGEREDWFHTLSRAIADHAAGLNTFSSSSEAR 1243 zebrafish
XP_007060013 1298 AEHCLNLSASSCSERDEWYSCISRTIPDDYKAHNASTFHNSIE 1340 green sea turtle
XP_005997888 1485 AECCLTLSASSCSERDEWYSTLTRTIHDSCRIQSASGSDSTSE 1527 coelacanth
XP_002938283 1289 MERCLMLSASSCTERDEWYSCISRTVQEYYKAPTVSIYNNLEI 1331 western clawed frog
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