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FNBP1L

Gene
FNBP1L
Protein
Formin-binding protein 1-like
Organism
Homo sapiens
Length
605 amino acids
Function
Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens.
Similarity
Belongs to the FNBP1 family.
Mass
70.065 kDa
Sequence
MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTISASKQESGKMDAKTTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTFSIEPVHYCMNEIKTGKPRIPSFRSLKRGWSVKMGPALEDFSHLPPEQRRKKLQQRIDELNRELQKESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGGRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDDPLPAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEKNSKGS

Gene
Fnbp1l
Protein
Formin-binding protein 1-like
Organism
Mus musculus
Length
605 amino acids
Function
Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL-WASPIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens (By similarity).
Similarity
Belongs to the FNBP1 family.
Mass
69.885 kDa
Sequence
MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCIAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTISAAKQESGKMDSKSTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTLSIEPVHYCMNEIKTGKPRIPSFRSLKRGVSLIMGPALEDFSHLPPEQRRKKLQQRIDELNRGLQKEADQKEALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGIRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHSEFDDEFEDDDPLPAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTTYIDVTLEKSSKGS

Gene
Fnbp1l
Protein
Formin-binding protein 1-like
Organism
Rattus norvegicus
Length
605 amino acids
Function
Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL-WASPIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens (By similarity). May negatively regulate neurite extension and axon branching in developing neurons.
Similarity
Belongs to the FNBP1 family.
Mass
69.974 kDa
Sequence
MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCIAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTVSDGTISASKQEGGKMDSKSTAGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSPPNGSQFLTLSIEPVHYCMNEIKTGKPRIPSFRSLKRGWSMKMGPALEDFSHLPPEQRRKKLQQRIDELNRGLQKESDQKEALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGVRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHSEFDDEFEDDDPLPAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTTYIDVTLEKNSKGS

Gene
fnbp1l
Protein
Formin-binding protein 1-like
Organism
Xenopus tropicalis
Length
550 amino acids
Function
Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Promotes cdc42-induced actin polymerization by activating the wasl-waspip complex, the predominant form of wasl/n-wasp in cells. Essential for autophagy of intracellular bacterial pathogens (By similarity).
Similarity
Belongs to the FNBP1 family.
Mass
64.01 kDa
Sequence
MSWGTELWDQFDNLEKHTQWGIDFLDKYAKFVKERLEIEQNYAKQLRNLVKKYCPKRSAKDEEPRFTSCLSFYNILNELNDYAGQREVVAEEMGHRVYAEIMRYSNDIKGERKSHLQEGRKAQQYLDMCLKQMDNSKRKFERECREAEKAQQTYERLDNDSNATKSDVEKAKQQLHLRTHMADESKNEYAAQLQNYNAEQHKHFYIVIPQVYKHLQEMDERRTVKLSECYKGFADAERKVIPIISKCLEGMVQAAKSVDERRDSQIVVDCFKSGFEPNGDYPFEDYSQHIYRTVSDGTISTPKQESLKPDPRVTVGKAKGKLWLFGKKPKGPALEDFSHLPPEQRRKRLQQRIDELSRELQKEMDQKDALNKMKDVYEKNPQMGDPSSLHPKIAETTSNIERLRMEIHKNEAWLSEVEGKVSQRSERRHSAEANHLVAQGRESPEGSYTEDANQEGRVQPQPHAHPEFDDEFDDDEPLPAIGHCKSLYPFDGNNEGTLAMKEGEVLYIIEEDKGDGWTRARKQNGEEGYVPTSYIDITLEKNSKGAVTYI

Gene
fnbp1l
Protein
Formin-binding protein 1-like
Organism
Xenopus laevis
Length
543 amino acids
Function
Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Essential for autophagy of intracellular bacterial pathogens (By similarity). Promotes cdc42-induced actin polymerization by activating the wasl-waspip complex, the predominant form of wasl/n-wasp in cells.
Similarity
Belongs to the FNBP1 family.
Mass
63.33 kDa
Sequence
MSWGTELWDQFDNLEKHTQWGIDFLDKYAKFVKERLEIEQNYAKQLRNLVKKFCPKRSAKDEEPRFTSCLSFYNILNELNDYAGQREVVAEEIGHRVYAEIMRYSNDIKGERKSHLHEGRKAQQYLDMCLKQMDNSKRKFERECREAEKAQQSYERLDNDTNATKSDVEKAKQQLHLRTHMADESKNEYAAQLQNYNAEQHKHFYIVIPQVYKHLQEMDERRTIKLSECYKGFADAERKVIPIISKCLEGMVQAAKSVDERRDSQIVVDCFKSGFEPPGDFPFEDYSQHIYRTVSDGTISTPKQESLKPDPRMTVGKAKGKLWLFGKKPKGPALEDFSHLPPEQRRKRLQQRIDELSRELQKEMDQKDALNKMKDVYEKNPQMGDPGSLHPKIAETTSNIERLRMEIHKNEGWLSEVEGKVSQRSERRHSAEANHLVAQGRESPEGSYTEDANQEGRVQPQHHAHPEFDDEFDDDEPLPAIGHCKSLYPFDGNNEGTLAMKEGEVLYIIEEDKGDGWTRARKQNGEEGYVPTSYIEITLEKKQ