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 24-JAN-2024, entry version 166.
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; 14.
DR IntAct; Q9NPF8; 5.
DR STRING; 9606.ENSP00000464121; -.
DR iPTMnet; Q9NPF8; -.
DR PhosphoSitePlus; Q9NPF8; -.
DR BioMuta; ADAP2; -.
DR DMDM; 27923749; -.
DR jPOST; Q9NPF8; -.
DR MassIVE; Q9NPF8; -.
DR PaxDb; 9606-ENSP00000329468; -.
DR PeptideAtlas; Q9NPF8; -.
DR ProteomicsDB; 81987; -. [Q9NPF8-1]
DR ProteomicsDB; 81988; -. [Q9NPF8-2]
DR Antibodypedia; 26908; 216 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 AGR; HGNC:16487; -.
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; CAKAKYE; -.
DR OrthoDB; 1022106at2759; -.
DR PhylomeDB; Q9NPF8; -.
DR TreeFam; TF324540; -.
DR PathwayCommons; Q9NPF8; -.
DR SignaLink; Q9NPF8; -.
DR BioGRID-ORCS; 55803; 12 hits in 1142 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 182 other cell types or 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 CDD; cd08844; ArfGap_ADAP2; 1.
DR CDD; cd13252; PH1_ADAP; 1.
DR CDD; cd01251; PH2_ADAP; 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); 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 PANTHER; PTHR46021; ARF-GAP WITH DUAL PH DOMAIN-CONTAINING PROTEIN 1-LIKE PROTEIN; 1.
DR PANTHER; PTHR46021:SF6; ARF-GAP WITH DUAL PH DOMAIN-CONTAINING PROTEIN 2; 1.
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; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
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
//
