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ADAP2_HUMAN
ID   ADAP2_HUMAN             Reviewed;         381 AA.
AC   Q9NPF8; Q8N4Q6; Q96SD5;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Arf-GAP with dual PH domain-containing protein 2;
DE   AltName: Full=Centaurin-alpha-2;
DE            Short=Cnt-a2;
GN   Name=ADAP2; Synonyms=CENTA2;
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).
RX   PubMed=12018390; DOI=10.1078/0171-9335-00242;
RA   Whitley P., Gibbard A.M., Koumanov F., Oldfield S., Kilgour E.E.,
RA   Prestwich G.D., Holman G.D.;
RT   "Identification of centaurin-alpha2: a phosphatidylinositide-binding
RT   protein present in fat, heart and skeletal muscle.";
RL   Eur. J. Cell Biol. 81:222-230(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=10843809; DOI=10.1006/geno.2000.6179;
RA   Jenne D.E., Tinschert S., Stegmann E., Reimann H., Nuernberg P., Horn D.,
RA   Naumann I., Buske A., Thiel G.;
RT   "A common set of at least 11 functional genes is lost in the majority of
RT   NF1 patients with gross deletions.";
RL   Genomics 66:93-97(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Bertsch U., Illies C., Mayr G.W.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Leukocyte;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=14690521; DOI=10.1046/j.1471-4159.2003.02143.x;
RA   Hanck T., Stricker R., Sedehizade F., Reiser G.;
RT   "Identification of gene structure and subcellular localization of human
RT   centaurin alpha 2, and p42IP4, a family of two highly homologous, Ins
RT   1,3,4,5-P4-/PtdIns 3,4,5-P3-binding, adapter proteins.";
RL   J. Neurochem. 88:326-336(2004).
CC   -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC       family (Potential). Binds phosphatidylinositol 3,4,5-trisphosphate
CC       (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Possesses a
CC       stoichiometry of two binding sites for InsP4 with identical affinity.
CC       {ECO:0000269|PubMed:14690521, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9NPF8; Q9Y6K9: IKBKG; NbExp=2; IntAct=EBI-718895, EBI-81279;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14690521}. Cell
CC       membrane {ECO:0000269|PubMed:14690521}. Note=Constitutively associated
CC       with the plasma membrane. Excluded from the nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NPF8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NPF8-2; Sequence=VSP_011180;
CC   -!- TISSUE SPECIFICITY: Highly expressed in placenta, spleen, kidney,
CC       skeletal muscle and adrenal gland. Weakly expressed in thyroid, liver,
CC       heart, lung, small intestine, peripheral blood leukocytes. Not detected
CC       in spinal cord, brain, stomach, trachea, colon, lymph node and bone
CC       marrow. {ECO:0000269|PubMed:14690521}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
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DR   EMBL; AJ238994; CAB88383.1; -; mRNA.
DR   EMBL; AJ272195; CAB77266.1; -; mRNA.
DR   EMBL; AJ242782; CAC40651.1; -; mRNA.
DR   EMBL; BC033758; AAH33758.1; -; mRNA.
DR   CCDS; CCDS11261.1; -. [Q9NPF8-1]
DR   RefSeq; NP_001333643.1; NM_001346714.1. [Q9NPF8-2]
DR   RefSeq; NP_060874.1; NM_018404.2. [Q9NPF8-1]
DR   AlphaFoldDB; Q9NPF8; -.
DR   SMR; Q9NPF8; -.
DR   BioGRID; 120915; 13.
DR   IntAct; Q9NPF8; 5.
DR   STRING; 9606.ENSP00000329468; -.
DR   iPTMnet; Q9NPF8; -.
DR   PhosphoSitePlus; Q9NPF8; -.
DR   BioMuta; ADAP2; -.
DR   DMDM; 27923749; -.
DR   jPOST; Q9NPF8; -.
DR   MassIVE; Q9NPF8; -.
DR   PaxDb; Q9NPF8; -.
DR   PeptideAtlas; Q9NPF8; -.
DR   PRIDE; Q9NPF8; -.
DR   ProteomicsDB; 81987; -. [Q9NPF8-1]
DR   ProteomicsDB; 81988; -. [Q9NPF8-2]
DR   Antibodypedia; 26908; 187 antibodies from 30 providers.
DR   DNASU; 55803; -.
DR   Ensembl; ENST00000330889.8; ENSP00000329468.3; ENSG00000184060.11. [Q9NPF8-1]
DR   GeneID; 55803; -.
DR   KEGG; hsa:55803; -.
DR   MANE-Select; ENST00000330889.8; ENSP00000329468.3; NM_018404.3; NP_060874.1.
DR   UCSC; uc002hfx.4; human. [Q9NPF8-1]
DR   CTD; 55803; -.
DR   DisGeNET; 55803; -.
DR   GeneCards; ADAP2; -.
DR   HGNC; HGNC:16487; ADAP2.
DR   HPA; ENSG00000184060; Low tissue specificity.
DR   MIM; 608635; gene.
DR   neXtProt; NX_Q9NPF8; -.
DR   OpenTargets; ENSG00000184060; -.
DR   PharmGKB; PA26405; -.
DR   VEuPathDB; HostDB:ENSG00000184060; -.
DR   eggNOG; KOG0703; Eukaryota.
DR   GeneTree; ENSGT00940000156498; -.
DR   InParanoid; Q9NPF8; -.
DR   OMA; MVLKEQW; -.
DR   OrthoDB; 1274375at2759; -.
DR   PhylomeDB; Q9NPF8; -.
DR   TreeFam; TF324540; -.
DR   PathwayCommons; Q9NPF8; -.
DR   SignaLink; Q9NPF8; -.
DR   BioGRID-ORCS; 55803; 11 hits in 1064 CRISPR screens.
DR   ChiTaRS; ADAP2; human.
DR   GeneWiki; CENTA2; -.
DR   GenomeRNAi; 55803; -.
DR   Pharos; Q9NPF8; Tbio.
DR   PRO; PR:Q9NPF8; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9NPF8; protein.
DR   Bgee; ENSG00000184060; Expressed in monocyte and 180 other tissues.
DR   ExpressionAtlas; Q9NPF8; baseline and differential.
DR   Genevisible; Q9NPF8; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005740; C:mitochondrial envelope; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; IDA:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB.
DR   GO; GO:0007507; P:heart development; IEP:UniProtKB.
DR   GO; GO:0048017; P:inositol lipid-mediated signaling; IDA:MGI.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR   GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR   CDD; cd13252; PH1_ADAP; 1.
DR   CDD; cd01251; PH2_ADAP; 1.
DR   Gene3D; 1.10.220.150; -; 1.
DR   Gene3D; 2.30.29.30; -; 2.
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; IPR037849; PH1_ADAP.
DR   InterPro; IPR037851; PH2_ADAP.
DR   InterPro; IPR001849; PH_domain.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 2.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF57863; SSF57863; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; GTPase activation;
KW   Membrane; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..381
FT                   /note="Arf-GAP with dual PH domain-containing protein 2"
FT                   /id="PRO_0000074206"
FT   DOMAIN          9..131
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   DOMAIN          132..233
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          255..361
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   ZN_FING         25..48
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   VAR_SEQ         269
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011180"
FT   CONFLICT        12
FT                   /note="L -> P (in Ref. 3; CAC40651)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  44349 MW;  4FAE208072A92C01 CRC64;
     MGDRERNKKR LLELLRAPDT GNAHCADCGA ADPDWASYKL GIFICLNCCG VHRNFPDISR
     VKSVRLDFWD DSIVEFMIHN GNLRVKAKFE ARVPAFYYIP QANDCLVLKE QWIRAKYERR
     EFMADGETIS LPGNREGFLW KRGRDNSQFL RRKFVLLARE GLLKYFTKEQ GKSPKAVISI
     KDLNATFQTE KIGHPHGLQI TYRRDGHTRN LFVYHESGKE IVDWFNALRA ARLQYLKMAF
     PELPESELVP FLTRNYLKQG FMEKTGPKQK EPFKKRWFAL DCHERRLLYY KNPLDAFEQG
     QVFLGNKEQG YEAYEDLPKG IRGNRWKAGL TIVTPERRFV LTCPSEKEQQ EWLESLRGVL
     SSPLTPLNRL TASTESGRSS R
 
 
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