AGAP1_MOUSE
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 03-AUG-2022, entry version 159.
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 MaxQB; Q8BXK8; -.
DR PaxDb; Q8BXK8; -.
DR PeptideAtlas; Q8BXK8; -.
DR PRIDE; Q8BXK8; -.
DR ProteomicsDB; 296077; -.
DR Antibodypedia; 34463; 150 antibodies from 25 providers.
DR DNASU; 347722; -.
DR Ensembl; ENSMUST00000027521; ENSMUSP00000027521; ENSMUSG00000055013.
DR GeneID; 347722; -.
DR KEGG; mmu:347722; -.
DR UCSC; uc007byw.1; mouse.
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; 751525at2759; -.
DR PhylomeDB; Q8BXK8; -.
DR TreeFam; TF317762; -.
DR BioGRID-ORCS; 347722; 2 hits in 72 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 264 other tissues.
DR ExpressionAtlas; Q8BXK8; baseline and differential.
DR Genevisible; Q8BXK8; MM.
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:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
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 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; SM00174; RHO; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57863; SSF57863; 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.
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
