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Search results 1 to 6 out of 6 for Asap1

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Domain
Description: ASAP1 is an Arf GAP that associates with and regulates actin-based structures. It is also involved in actin remodeling affecting cell spreading and cell migration []. ASAP1 contains BAR, PH, Arf GAP, Ank repeats, Proline-rich, E/DLPPKP repeat, and SH3 domains. It binds to focal adhesion kinase (FAK) via its SH3 domain []. The BAR domain of ASAP1 is also critical for its cellular function in regulation of actin-based structures [].This entry includes the SH3 domain of ASAP1.
Protein Domain
Type: Family
Description: ASAPs (ASAP1, ASAP2, and ASAP3) function as Arf-specific GTPase-activating proteins (GAPs), participate in rhodopsin trafficking, are associated with tumour cell metastasis, modulate phagocytosis, promote cell proliferation, facilitate vesicle budding, Golgi exocytosis, and regulate vesicle coat assembly via a Bin/Amphiphysin/Rvs domain [, , ]. Each member has a BAR, PH, Arf GAP, Ank repeat and proline rich domains. ASAP1 and ASAP2 also have a SH3 domain at the C terminus []. The ASAP family is named for the first identified member, ASAP1 [].
Protein Domain
Type: Domain
Description: ASAP1 is an Arf GTPase activating protein (GAP) with activity towards Arf1 and Arf5 but not Arf6 However, it has been shown to bind GTP-Arf6 stably without GAP activity []. It has been implicated in cell growth, migration, and survival, as well as in tumor invasion and malignancy. It binds paxillin and cortactin, two components of invadopodia which are essential for tumor invasiveness. It also binds focal adhesion kinase (FAK) and the SH2/SH3 adaptor CrkL [, ]. ASAP1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain [].This entry represents the BAR domain of ASAP1. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains [].
Protein Domain
Type: Domain
Description: ASAPs (ASAP1, ASAP2, and ASAP3) function as Arf-specific GTPase-activating proteins (GAPs), participate in rhodopsin trafficking, are associated with tumor cell metastasis, modulate phagocytosis, promote cell proliferation, facilitate vesicle budding, Golgi exocytosis, and regulate vesicle coat assembly via a Bin/Amphiphysin/Rvs domain [, , ]. Each member has a BAR, PH, Arf GAP, Ank repeat and proline rich domains. ASAP1 and ASAP2 also have a SH3 domain at the C terminus []. ASAP1 has been implicated in regulating cell motility and invasion []. This entry represents the SH3 domain of ASAP1.
Protein Domain
Type: Domain
Description: This entry includes the family M35 Zn2+-metallopeptidase extracellular domain from proteins characterized as peptidyl-Lys metalloendopeptidases (MEP; peptidyllysine metalloproteinase; EC 3.4.24.20; MEROPS identifier M35.004), including some well-characterized domains in Armillaria mellea [], Aeromonas salmonicida subsp. achromogenes (AsaP1) [, ]and Grifola frondosa (GfMEP) [, , ]. These proteins specifically cleave peptidyl-lysine bonds (-X-Lys- where X may even be Pro) in proteins and peptides. AsaP1 peptidase (MEROPS identifier M35.003) has been shown to be important in the virulence of A. salmonicida subsp. achromogenes, having a major role in the fish innate immune response []. AsaP1 is synthesized as an inactive precursor, the structure of which shows that the propeptide inhibits activity by inserting a lysine into the S1' pocket of active site [].Peptidase family M35 contains metalloendopeptidases known as Asp-zincins, in which a single catalytic zinc ion is ligated by two histidines in an HExxH motif and an aspartic acid in a GTXDXXYG or similar motif C-terminal to the HExxH motif. The glutamic acid in the HExxH motif is a catalytic residue [].
Protein Domain
Type: Domain
Description: This entry represents the PH domain of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing proteins (ASAPs). ASAPs (ASAP1, ASAP2, and ASAP3) function as Arf-specific GTPase-activating proteins (GAPs), participate in rhodopsin trafficking, are associated with tumour cell metastasis, modulate phagocytosis, promote cell proliferation, facilitate vesicle budding, Golgi exocytosis, and regulate vesicle coat assembly via a Bin/Amphiphysin/Rvs domain [, , ]. Each member has a BAR, PH, Arf GAP, Ank repeat and proline rich domains. ASAP1 and ASAP2 also have a SH3 domain at the C terminus []. The ASAP family is named for the first identified member, ASAP1 [].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 [].