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0DDEF2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionDevelopment and differentiation-enhancing factor 2 (pyk2 c-terminus associated protein) (pap) (paxillin-associated protein with arfgap activity 3) (pag3).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008047 enzyme activator activity (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry describes a family of small GTPase activating proteins.or example ARF1-directed GTPase-activating protein.he cycle control GTPaseactivating protein (GAP) GCS1 which is important for the regulation ofthe ADP ribosylation factor ARF. member of the Ras superfamily of GTP-bindingproteins . The GTP-bound form of ARF is essential for the maintenance of normalGolgi morphology.t participates in recruitment of coat proteins which arerequired for budding and fission of membranes. Before the fusion with anacceptor compartment the membrane must be uncoated. This step required thehydrolysis of GTP associated to ARF. These proteins contain a characteristic zinc finger motif(Cys-x2-Cys-x(16.7)-x2-Cys) which displays some similarity to the C4-typeGATA zinc finger. The ARFGAP domain display no obvious similarity to other GAPproteins. The 3D structure of the ARFGAP domain of the PYK2-associated protein beta hasbeen solved . It consists of a three-stranded beta-sheet surrounded by 5alpha helices. The domain is organized around a central zinc atom which iscoordinated by 4 cysteines. The ARFGAP domain is clearlyunrelated to the other GAP proteins structures which are exclusively helical.Classical GAP proteins accelerate GTPase activity by supplying an argininefinger to the active site. The crystal structure of ARFGAP bound to ARFrevealed that the ARFGAP domain does not supply an arginine to the active sitewhich suggests a more indirect role of the ARFGAP domain in the GTPasehydrolysis . The Rev protein of human immunodeficiency virus type 1 (HIV-1) facilitates nuclear export of unspliced and partly-spliced viral RNAs . Rev contains an RNA-binding domain and an effector domain; the latter is believed to interact with a cellular cofactor required for the Rev response and hence HIV-1 replication. Human Rev interacting protein (hRIP) specifically interacts with the Rev effector. The amino acid sequence of hRIP is characterised by an N-terminal.-4 class zinc finger motif.
  IPR001164:Arf GTPase activating protein
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
Phagocytes form the first line of defence against invasion by micro-organisms. Engulfing of bacteria by neutrophils is accompanied by theconsumption of large amounts of oxygen - a so-called respiratory burst.Defects in phagocytosis involving the lack of a respiratory burst giverise to chronic granulomatous disease (CGD).n which patients are pre-disposed to infection.ften from otherwise non-pathogenic bacteria .Regulation of the respiratory burst takes place at the phagocytic vacuole.The process is mediated by NADPH oxidase.hich transports electrons acrossthe plasma membrane to form superoxide (an oxygen molecule with an extraelectron that is toxic to normal cells) in the vacuole interior. Theelectrons are carried across the membrane by a short electron transportchain in the form of an unusual flavocytochrome b .To conserve NADPH and avoid the toxic effects of superoxide.he oxidase remains inactive until it receives an appropriate stimulus. Activationinvolves the participation of a number of cytosolic proteins.ome of which attach to the flavocytochrome. P47phox.67phox and p40phox arespecialised components of phagocytic cells.ll of which contain SH3domains .y means of which they attach to proline-rich regions of otherproteins. Upon activation.47phox and p67phox are phosphorylated and.ith p40phox.ranslocate to the region of the plasma membrane formingthe phagocytic they associates with hydrophilic regionsof the flavocytochrome .
  IPR000108:Neutrophil cytosol factor 2
The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers . The repeat has been found in proteins of diverse function such as transcriptional initiators.ell-cycle regulators.ytoskeletal.on transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures . Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure .
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
SequencesProtein: DDEF2_HUMAN (1006 aa)
mRNA: NM_003887
Local Annotation
Synapse Ontology
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 156 residues, 9264344-9264810Exon2: 26 residues, 9336896-9336969Exon3: 50 residues, 9354879-9355025Exon4: 27 residues, 9376103-9376178Exon5: 18 residues, 9377867-9377917Exon6: 45 residues, 9380700-9380830Exon7: 30 residues, 9385405-9385491Exon8: 27 residues, 9392317-9392393Exon9: 31 residues, 9392672-9392759Exon10: 36 residues, 9402111-9402215Exon11: 25 residues, 9402310-9402380Exon12: 31 residues, 9408387-9408475Exon13: 18 residues, 9413626-9413675Exon14: 57 residues, 9413758-9413925Exon15: 46 residues, 9416335-9416469Exon16: 33 residues, 9426004-9426099Exon17: 65 residues, 9432334-9432524Exon18: 30 residues, 9434487-9434573Exon19: 40 residues, 9436523-9436639Exon20: 24 residues, 9438320-9438388Exon21: 40 residues, 9442824-9442938Exon22: 86 residues, 9445873-9446126Exon23: 47 residues, 9448641-9448776Exon24: 57 residues, 9451061-9451227Exon25: 18 residues, 9457602-9457652Exon26: 31 residues, 9458321-9458410Exon27: 43 residues, 9458853-9458976Exon28: 810 residues, 9460832-9463257Exon29: 2 residues, -Jump to DDEF2_HUMAN  
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Loci Cluster (Details)Loci: 4421 9641557-9688557 ~-47K 19981(YWHAQ)(-)Loci: 3142 9264344-9463257 ~-199K 19972(DDEF2)(+)Link out to UCSC