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Database: UniProt
Entry: Q8WWN8
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ID   ARAP3_HUMAN             Reviewed;        1544 AA.
AC   Q8WWN8; B4DIT1; D3DQE3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3;
DE   AltName: Full=Centaurin-delta-3;
DE            Short=Cnt-d3;
GN   Name=ARAP3; Synonyms=CENTD3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF 307-ARG-ARG-308,
RP   FUNCTION, AND INTERACTION WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
RX   PubMed=11804589; DOI=10.1016/s1097-2765(02)00434-3;
RA   Krugmann S., Anderson K.E., Ridley S.H., Risso N., McGregor A.,
RA   Coadwell J., Davidson K., Eguinoa A., Ellson C.D., Lipp P., Manifava M.,
RA   Ktistakis N., Painter G., Thuring J.W., Cooper M.A., Lim Z.-Y.,
RA   Holmes A.B., Dove S.K., Michell R.H., Grewal A., Nazarian A.,
RA   Erdjument-Bromage H., Tempst P., Stephens L.R., Hawkins P.T.;
RT   "Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho
RT   GTPases, by selective capture on phosphoinositide affinity matrices.";
RL   Mol. Cell 9:95-108(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   REVIEW.
RX   PubMed=12015138; DOI=10.1016/s0960-9822(02)00860-6;
RA   Santy L.C., Casanova J.E.;
RT   "GTPase signaling: bridging the GAP between ARF and Rho.";
RL   Curr. Biol. 12:R360-R362(2002).
RN   [6]
RP   ROLE IN THE INTERNALIZATION OF ANTHRAX TOXIN.
RX   PubMed=15569923; DOI=10.1073/pnas.0407794101;
RA   Lu Q., Wei W., Kowalski P.E., Chang A.C.Y., Cohen S.N.;
RT   "EST-based genome-wide gene inactivation identifies ARAP3 as a host protein
RT   affecting cellular susceptibility to anthrax toxin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:17246-17251(2004).
RN   [7]
RP   INTERACTION WITH INPPL1.
RX   PubMed=17314030; DOI=10.1016/j.cellsig.2006.12.015;
RA   Raaijmakers J.H., Deneubourg L., Rehmann H., de Koning J., Zhang Z.,
RA   Krugmann S., Erneux C., Bos J.L.;
RT   "The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2
RT   in a SAM domain-dependent manner.";
RL   Cell. Signal. 19:1249-1257(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1444, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1444 AND SER-1480, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1444, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   STRUCTURE BY NMR OF 1-80, AND INTERACTION WITH INPPL1.
RX   PubMed=19765305; DOI=10.1186/1472-6807-9-59;
RA   Leone M., Cellitti J., Pellecchia M.;
RT   "The Sam domain of the lipid phosphatase Ship2 adopts a common model to
RT   interact with Arap3-Sam and EphA2-Sam.";
RL   BMC Struct. Biol. 9:59-59(2009).
RN   [12]
RP   VARIANTS [LARGE SCALE ANALYSIS] TRP-471; MET-1085 AND PRO-1428.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-
CC       activating protein that modulates actin cytoskeleton remodeling by
CC       regulating ARF and RHO family members. Is activated by
CC       phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can
CC       be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2)
CC       binding, albeit with lower efficiency. Acts on ARF6, RAC1, RHOA and
CC       CDC42. Plays a role in the internalization of anthrax toxin.
CC       {ECO:0000269|PubMed:11804589, ECO:0000269|PubMed:15569923}.
CC   -!- SUBUNIT: Interacts (via SAM domain) with INPPL1/SHIP2.
CC       {ECO:0000269|PubMed:11804589, ECO:0000269|PubMed:17314030,
CC       ECO:0000269|PubMed:19765305}.
CC   -!- INTERACTION:
CC       Q8WWN8; Q96B97: SH3KBP1; NbExp=4; IntAct=EBI-4402732, EBI-346595;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell
CC       projection, ruffle {ECO:0000250}. Note=Cytoplasmic, and associated with
CC       F-actin-rich membrane ruffles and lamellipodia. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8WWN8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WWN8-2; Sequence=VSP_056214, VSP_056215;
CC   -!- PTM: Tyrosine phosphorylated at a low basal level. PDGF treatment
CC       stimulates phosphorylation. Tyrosine phosphorylation is increased in
CC       cells that are in the process of becoming attached to a substrate and
CC       that start spreading and flattening (By similarity). {ECO:0000250}.
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DR   EMBL; AJ310567; CAC83946.1; -; mRNA.
DR   EMBL; AK295768; BAG58593.1; -; mRNA.
DR   EMBL; AC022420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471062; EAW61904.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61905.1; -; Genomic_DNA.
DR   CCDS; CCDS4266.1; -. [Q8WWN8-1]
DR   PIR; E59431; E59431.
DR   RefSeq; NP_071926.4; NM_022481.5. [Q8WWN8-1]
DR   PDB; 2KG5; NMR; -; A=1-80.
DR   PDB; 2LNW; NMR; -; B=1404-1412.
DR   PDB; 5JCP; X-ray; 2.10 A; A/B=906-1107.
DR   PDB; 5JD0; X-ray; 2.30 A; A/B=906-1107.
DR   PDB; 7A9B; X-ray; 2.00 A; A/B=1414-1429.
DR   PDB; 7YIR; X-ray; 2.10 A; A=284-385.
DR   PDB; 7YIS; X-ray; 3.30 A; A=284-385.
DR   PDBsum; 2KG5; -.
DR   PDBsum; 2LNW; -.
DR   PDBsum; 5JCP; -.
DR   PDBsum; 5JD0; -.
DR   PDBsum; 7A9B; -.
DR   PDBsum; 7YIR; -.
DR   PDBsum; 7YIS; -.
DR   AlphaFoldDB; Q8WWN8; -.
DR   SMR; Q8WWN8; -.
DR   BioGRID; 122163; 94.
DR   IntAct; Q8WWN8; 5.
DR   MINT; Q8WWN8; -.
DR   STRING; 9606.ENSP00000239440; -.
DR   GlyGen; Q8WWN8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8WWN8; -.
DR   PhosphoSitePlus; Q8WWN8; -.
DR   BioMuta; ARAP3; -.
DR   DMDM; 73619965; -.
DR   EPD; Q8WWN8; -.
DR   jPOST; Q8WWN8; -.
DR   MassIVE; Q8WWN8; -.
DR   MaxQB; Q8WWN8; -.
DR   PaxDb; 9606-ENSP00000239440; -.
DR   PeptideAtlas; Q8WWN8; -.
DR   ProteomicsDB; 4328; -.
DR   ProteomicsDB; 74915; -. [Q8WWN8-1]
DR   Pumba; Q8WWN8; -.
DR   Antibodypedia; 27363; 125 antibodies from 30 providers.
DR   DNASU; 64411; -.
DR   Ensembl; ENST00000239440.9; ENSP00000239440.4; ENSG00000120318.16. [Q8WWN8-1]
DR   Ensembl; ENST00000513878.5; ENSP00000421468.1; ENSG00000120318.16. [Q8WWN8-2]
DR   GeneID; 64411; -.
DR   KEGG; hsa:64411; -.
DR   MANE-Select; ENST00000239440.9; ENSP00000239440.4; NM_022481.6; NP_071926.4.
DR   UCSC; uc003llm.4; human. [Q8WWN8-1]
DR   AGR; HGNC:24097; -.
DR   CTD; 64411; -.
DR   DisGeNET; 64411; -.
DR   GeneCards; ARAP3; -.
DR   HGNC; HGNC:24097; ARAP3.
DR   HPA; ENSG00000120318; Low tissue specificity.
DR   MIM; 606647; gene.
DR   neXtProt; NX_Q8WWN8; -.
DR   OpenTargets; ENSG00000120318; -.
DR   PharmGKB; PA164715983; -.
DR   VEuPathDB; HostDB:ENSG00000120318; -.
DR   eggNOG; KOG1117; Eukaryota.
DR   GeneTree; ENSGT00940000158869; -.
DR   HOGENOM; CLU_002900_0_0_1; -.
DR   InParanoid; Q8WWN8; -.
DR   OMA; CETVFQS; -.
DR   OrthoDB; 4835at2759; -.
DR   PhylomeDB; Q8WWN8; -.
DR   TreeFam; TF105769; -.
DR   PathwayCommons; Q8WWN8; -.
DR   Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR   SignaLink; Q8WWN8; -.
DR   SIGNOR; Q8WWN8; -.
DR   BioGRID-ORCS; 64411; 15 hits in 1154 CRISPR screens.
DR   ChiTaRS; ARAP3; human.
DR   EvolutionaryTrace; Q8WWN8; -.
DR   GeneWiki; CENTD3; -.
DR   GenomeRNAi; 64411; -.
DR   Pharos; Q8WWN8; Tbio.
DR   PRO; PR:Q8WWN8; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q8WWN8; Protein.
DR   Bgee; ENSG00000120318; Expressed in apex of heart and 156 other cell types or tissues.
DR   ExpressionAtlas; Q8WWN8; baseline and differential.
DR   Genevisible; Q8WWN8; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB.
DR   CDD; cd17902; ArfGap_ARAP3; 1.
DR   CDD; cd13253; PH1_ARAP; 1.
DR   CDD; cd13254; PH2_ARAP; 1.
DR   CDD; cd13256; PH3_ARAP; 1.
DR   CDD; cd13259; PH5_ARAP; 1.
DR   CDD; cd04385; RhoGAP_ARAP; 1.
DR   CDD; cd09490; SAM_Arap1_2_3; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR037858; RhoGAP_ARAP.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45899:SF4; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR45899; RHO GTPASE ACTIVATING PROTEIN AT 15B, ISOFORM C; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 5.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 5.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 3.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW   Cytoplasm; Cytoskeleton; GTPase activation; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..1544
FT                   /note="Arf-GAP with Rho-GAP domain, ANK repeat and PH
FT                   domain-containing protein 3"
FT                   /id="PRO_0000074215"
FT   DOMAIN          4..68
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          287..379
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          394..483
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          480..611
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   DOMAIN          907..1088
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   DOMAIN          1117..1210
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   DOMAIN          1223..1325
FT                   /note="PH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   ZN_FING         504..527
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          64..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1422..1544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..98
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1422..1458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1510..1544
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1348
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R5G7"
FT   MOD_RES         1403
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R5G7"
FT   MOD_RES         1408
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R5G7"
FT   MOD_RES         1444
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VAR_SEQ         1..338
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056214"
FT   VAR_SEQ         1371..1383
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056215"
FT   VARIANT         218
FT                   /note="D -> H (in dbSNP:rs1031904)"
FT                   /id="VAR_048330"
FT   VARIANT         471
FT                   /note="R -> W (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs1562420371)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036180"
FT   VARIANT         1085
FT                   /note="I -> M (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036181"
FT   VARIANT         1428
FT                   /note="T -> P (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs61749636)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036182"
FT   MUTAGEN         307..308
FT                   /note="RR->AA: Loss of PtdIns(3,4,5)P3 binding."
FT                   /evidence="ECO:0000269|PubMed:11804589"
FT   HELIX           9..13
FT                   /evidence="ECO:0007829|PDB:2KG5"
FT   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:2KG5"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:2KG5"
FT   HELIX           22..27
FT                   /evidence="ECO:0007829|PDB:2KG5"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:2KG5"
FT   HELIX           41..47
FT                   /evidence="ECO:0007829|PDB:2KG5"
FT   HELIX           52..62
FT                   /evidence="ECO:0007829|PDB:2KG5"
FT   TURN            63..67
FT                   /evidence="ECO:0007829|PDB:2KG5"
FT   HELIX           909..911
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   STRAND          918..920
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           921..933
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   TURN            934..936
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   TURN            938..942
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           947..960
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           961..963
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   TURN            968..970
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           973..986
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   STRAND          987..989
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           994..996
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           997..1004
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           1009..1022
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           1025..1043
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           1045..1048
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           1052..1064
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           1071..1082
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           1084..1087
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   HELIX           1092..1099
FT                   /evidence="ECO:0007829|PDB:5JCP"
FT   STRAND          1420..1424
FT                   /evidence="ECO:0007829|PDB:7A9B"
SQ   SEQUENCE   1544 AA;  169844 MW;  40C03A22591B2B6F CRC64;
     MAAPQDLDIA VWLATVHLEQ YADTFRRHGL ATAGAARGLG HEELKQLGIS ATGHRKRILR
     LLQTGTEEGS LDPKSDSAME PSPSPAPQAQ PPKPVPKPRT VFGGLSGPAT TQRPGLSPAL
     GGPGVSRSPE PSPRPPPLPT SSSEQSSALN TVEMMPNSIY FGLDSRGRAQ AAQDKAPDSS
     QISAPTPALR PTTGTVHIMD PGCLYYGVQP VGTPGAPDRR ESRGVCQGRA EHRLSRQDLE
     AREDAGYASL ELPGDSTLLS PTLETEETSD DLISPYASFS FTADRLTPLL SGWLDKLSPQ
     GNYVFQRRFV QFNGRSLMYF GSDKDPFPKG VIPLTAIEMT RSSKDNKFQV ITGQRVFVFR
     TESEAQRDMW CSTLQSCLKE QRLLGHPRPP QPPRPLRTGM LELRGHKAKV FAALSPGELA
     LYKSEQAFSL GIGICFIELQ GCSVRETKSR SFDLLTPHRC FSFTAESGGA RQSWAAALQE
     AVTETLSDYE VAEKIWSNRA NRQCADCGSS RPDWAAVNLG VVICKQCAGQ HRALGSGISK
     VQSLKLDTSV WSNEIVQLFI VLGNDRANRF WAGTLPPGEG LHPDATPGPR GEFISRKYRL
     GLFRKPHPQY PDHSQLLQAL CAAVARPNLL KNMTQLLCVE AFEGEEPWFP PAPDGSCPGL
     LPSDPSPGVY NEVVVRATYS GFLYCSPVSN KAGPSPPRRG RDAPPRLWCV LGAALEMFAS
     ENSPEPLSLI QPQDIVCLGV SPPPTDPGDR FPFSFELILA GGRIQHFGTD GADSLEAWTS
     AVGKWFSPLS CHQLLGPGLL RLGRLWLRSP SHTAPAPGLW LSGFGLLRGD HLFLCSAPGP
     GPPAPEDMVH LRRLQEISVV SAADTPDKKE HLVLVETGRT LYLQGEGRLD FTAWNAAIGG
     AAGGGGTGLQ EQQMSRGDIP IIVDACISFV TQHGLRLEGV YRKGGARARS LRLLAEFRRD
     ARSVKLRPGE HFVEDVTDTL KRFFRELDDP VTSARLLPRW REAAELPQKN QRLEKYKDVI
     GCLPRVNRRT LATLIGHLYR VQKCAALNQM CTRNLALLFA PSVFQTDGRG EHEVRVLQEL
     IDGYISVFDI DSDQVAQIDL EVSLITTWKD VQLSQAGDLI MEVYIEQQLP DNCVTLKVSP
     TLTAEELTNQ VLEMRGTAAG MDLWVTFEIR EHGELERPLH PKEKVLEQAL QWCQLPEPCS
     ASLLLKKVPL AQAGCLFTGI RRESPRVGLL RCREEPPRLL GSRFQERFFL LRGRCLLLLK
     EKKSSKPERE WPLEGAKVYL GIRKKLKPPT PWGFTLILEK MHLYLSCTDE DEMWDWTTSI
     LKAQHDDQQP VVLRRHSSSD LARQKFGTMP LLPIRGDDSG ATLLSANQTL RRLHNRRTLS
     MFFPMKSSQG SVEEQEELEE PVYEEPVYEE VGAFPELIQD TSTSFSTTRE WTVKPENPLT
     SQKSLDQPFL SKSSTLGQEE RPPEPPPGPP SKSSPQARGS LEEQLLQELS SLILRKGETT
     AGLGSPSQPS SPQSPSPTGL PTQTPGFPTQ PPCTSSPPSS QPLT
//
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