ID   AGAP1_MOUSE             Reviewed;         857 AA.
AC   Q8BXK8; Q3UHA0; Q6ZPX9; Q8BZG0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1;
DE            Short=AGAP-1;
DE   AltName: Full=Centaurin-gamma-2;
DE            Short=Cnt-g2;
GN   Name=Agap1; Synonyms=Centg2, Kiaa1099;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adrenal gland, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12640130; DOI=10.1128/mcb.23.7.2476-2488.2003;
RA   Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.;
RT   "GGAPs, a new family of bifunctional GTP-binding and GTPase-activating
RT   proteins.";
RL   Mol. Cell. Biol. 23:2476-2488(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15381706; DOI=10.1074/jbc.m410565200;
RA   Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.;
RT   "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl
RT   cyclase.";
RL   J. Biol. Chem. 279:49346-49354(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND THR-836, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: GTPase-activating protein for ARF1 and, to a lesser extent,
CC       ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-
CC       dependent trafficking of proteins in the endosomal-lysosomal system (By
CC       similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC       3,4,5-trisphosphate (PIP3) and, to a lesser extent, by
CC       phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidic acid
CC       potentiates PIP2 stimulation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with several subunits of the AP-3 protein
CC       complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3 and GUCY1B3 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associates with the
CC       endocytic compartment. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain and
CC       kidney. {ECO:0000269|PubMed:15381706}.
CC   -!- DEVELOPMENTAL STAGE: At 12.5 dpc, expression is restricted to neural
CC       tube, forebrain and midbrain. {ECO:0000269|PubMed:12640130}.
CC   -!- DOMAIN: The PH domain mediates AP-3 binding.
CC   -!- PTM: Phosphorylated on tyrosines. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the centaurin gamma-like family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98099.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK035494; BAC29078.1; -; mRNA.
DR   EMBL; AK046523; BAC32770.1; -; mRNA.
DR   EMBL; AK147503; BAE27957.1; -; mRNA.
DR   EMBL; AK129289; BAC98099.2; ALT_INIT; mRNA.
DR   CCDS; CCDS15149.1; -.
DR   RefSeq; NP_001032213.1; NM_001037136.1.
DR   RefSeq; NP_835220.1; NM_178119.3.
DR   AlphaFoldDB; Q8BXK8; -.
DR   SMR; Q8BXK8; -.
DR   BioGRID; 237241; 4.
DR   CORUM; Q8BXK8; -.
DR   IntAct; Q8BXK8; 2.
DR   MINT; Q8BXK8; -.
DR   STRING; 10090.ENSMUSP00000027521; -.
DR   iPTMnet; Q8BXK8; -.
DR   PhosphoSitePlus; Q8BXK8; -.
DR   SwissPalm; Q8BXK8; -.
DR   MaxQB; Q8BXK8; -.
DR   PaxDb; 10090-ENSMUSP00000027521; -.
DR   PeptideAtlas; Q8BXK8; -.
DR   ProteomicsDB; 296077; -.
DR   Pumba; Q8BXK8; -.
DR   Antibodypedia; 34463; 159 antibodies from 25 providers.
DR   DNASU; 347722; -.
DR   Ensembl; ENSMUST00000027521.15; ENSMUSP00000027521.9; ENSMUSG00000055013.17.
DR   GeneID; 347722; -.
DR   KEGG; mmu:347722; -.
DR   UCSC; uc007byw.1; mouse.
DR   AGR; MGI:2653690; -.
DR   CTD; 116987; -.
DR   MGI; MGI:2653690; Agap1.
DR   VEuPathDB; HostDB:ENSMUSG00000055013; -.
DR   eggNOG; KOG0705; Eukaryota.
DR   GeneTree; ENSGT00940000154793; -.
DR   InParanoid; Q8BXK8; -.
DR   OMA; WYGANIK; -.
DR   OrthoDB; 1449795at2759; -.
DR   PhylomeDB; Q8BXK8; -.
DR   TreeFam; TF317762; -.
DR   BioGRID-ORCS; 347722; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Agap1; mouse.
DR   PRO; PR:Q8BXK8; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8BXK8; Protein.
DR   Bgee; ENSMUSG00000055013; Expressed in retinal neural layer and 266 other cell types or tissues.
DR   ExpressionAtlas; Q8BXK8; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd08853; ArfGap_AGAP2; 1.
DR   CDD; cd04103; Centaurin_gamma; 1.
DR   CDD; cd01250; PH_AGAP; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001806; Small_GTPase.
DR   PANTHER; PTHR45819:SF1; ARF-GAP WITH GTPASE, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; Q8BXK8; MM.
PE   1: Evidence at protein level;
KW   Acetylation; ANK repeat; Cytoplasm; GTP-binding; GTPase activation;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Protein transport;
KW   Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..857
FT                   /note="Arf-GAP with GTPase, ANK repeat and PH domain-
FT                   containing protein 1"
FT                   /id="PRO_0000074219"
FT   DOMAIN          346..588
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          609..729
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REPEAT          768..797
FT                   /note="ANK 1"
FT   REPEAT          801..830
FT                   /note="ANK 2"
FT   ZN_FING         624..647
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          66..276
FT                   /note="Small GTPase-like"
FT   REGION          267..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         122..126
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         178..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPQ3"
FT   MOD_RES         521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPQ3"
FT   MOD_RES         605
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPQ3"
FT   MOD_RES         663
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         836
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        424
FT                   /note="K -> R (in Ref. 2; BAC98099)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        668
FT                   /note="D -> Y (in Ref. 1; BAC29078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        700
FT                   /note="S -> P (in Ref. 1; BAE27957)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        811
FT                   /note="Q -> H (in Ref. 1; BAC29078)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   857 AA;  94411 MW;  A88AF73A4BB50815 CRC64;
     MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV IAIEDAFVNS
     QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL
     LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD
     AISSTNPRVI DDVRARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI
     GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT
     ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS
     LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSACAPI
     SSPKTNGLAK DMSSLHISPN SGNVTSASGS QMASGISLVS FNSRPDGMHQ RSYSVSSADQ
     WSDATVIANS AISSDTGLGD SVCSSPSISS STSPKLDPPP SPHANRKKHR RKKSTSNFKA
     DGLSGTAEEQ EENLEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK
     SRLTSQSEAM ALQSIRNMRG NSHCVDCDTQ NPNWASLNLG ALMCIECSGI HRNLGTHLSR
     VRSLDLDDWP MELIKVMSSI GNELANSVWE EGSQGRTKPS LDSTREEKER WIRAKYEQKL
     FLAPLPCTEF SLGQQLLRAT AEEDLRTVIL LLAHGSRDEV NETCGEGDGR TALHLACRKG
     NVVLAQLLIW YGVDVMARDA HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS
     RKSNSRNNSS GRAPSVI
//