ID   ARFG1_MOUSE             Reviewed;         414 AA.
AC   Q9EPJ9; A8WIR9; A8WIS1; Q3TI52; Q8BMM6; Q8BMQ7;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=ADP-ribosylation factor GTPase-activating protein 1;
DE            Short=ARF GAP 1;
DE   AltName: Full=ADP-ribosylation factor 1 GTPase-activating protein;
DE            Short=ARF1 GAP;
DE   AltName: Full=ARF1-directed GTPase-activating protein;
GN   Name=Arfgap1; Synonyms=Arf1gap;
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 [MRNA] (ISOFORM 1).
RA   Venkateswarlu K.;
RT   "Cloning and functional characterisation of mouse ARF1GAP.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, Pituitary, Placenta, and Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135; SER-342; SER-345;
RP   SER-347; SER-360 AND SER-362, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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 (GAP) for the ADP ribosylation
CC       factor 1 (ARF1). Involved in membrane trafficking and /or vesicle
CC       transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is
CC       required for the dissociation of coat proteins from Golgi-derived
CC       membranes and vesicles, a prerequisite for vesicle's fusion with target
CC       compartment. Probably regulates ARF1-mediated transport via its
CC       interaction with the KDELR proteins and TMED2. Overexpression induces
CC       the redistribution of the entire Golgi complex to the endoplasmic
CC       reticulum, as when ARF1 is deactivated. Its activity is stimulated by
CC       phosphoinosides and inhibited by phosphatidylcholine (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ARF1. Interacts with the COPI coat proteins,
CC       KDELR1 and TMED2. It is probably a component of the COPI coat protein
CC       complex. The interaction with TMED2 inhibits the GAP activity (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9EPJ9; Q5S006: Lrrk2; NbExp=3; IntAct=EBI-6288020, EBI-2693710;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC       {ECO:0000250}. Note=Associates with the Golgi complex. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EPJ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPJ9-2; Sequence=VSP_011303;
CC   -!- DOMAIN: The region downstream of Arf-GAP domain is essential to GAP
CC       activity in vivo. This region may be required for its targeting to
CC       Golgi membranes (By similarity). {ECO:0000250}.
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DR   EMBL; AJ401461; CAC18721.1; -; mRNA.
DR   EMBL; AK030295; BAC26883.1; -; mRNA.
DR   EMBL; AK030520; BAC27002.1; -; mRNA.
DR   EMBL; AK145879; BAE26720.1; -; mRNA.
DR   EMBL; AK168007; BAE39994.1; -; mRNA.
DR   EMBL; BX649560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS17190.1; -. [Q9EPJ9-1]
DR   CCDS; CCDS50843.1; -. [Q9EPJ9-2]
DR   RefSeq; NP_001171177.1; NM_001177706.1. [Q9EPJ9-2]
DR   RefSeq; NP_001171178.1; NM_001177707.1.
DR   RefSeq; NP_001171179.1; NM_001177708.1.
DR   RefSeq; NP_001171180.1; NM_001177709.1. [Q9EPJ9-2]
DR   RefSeq; NP_665703.2; NM_145760.3. [Q9EPJ9-1]
DR   RefSeq; XP_017173503.1; XM_017318014.1.
DR   AlphaFoldDB; Q9EPJ9; -.
DR   SMR; Q9EPJ9; -.
DR   BioGRID; 230805; 17.
DR   IntAct; Q9EPJ9; 1.
DR   STRING; 10090.ENSMUSP00000029092; -.
DR   GlyGen; Q9EPJ9; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9EPJ9; -.
DR   PhosphoSitePlus; Q9EPJ9; -.
DR   SwissPalm; Q9EPJ9; -.
DR   EPD; Q9EPJ9; -.
DR   jPOST; Q9EPJ9; -.
DR   MaxQB; Q9EPJ9; -.
DR   PaxDb; 10090-ENSMUSP00000029092; -.
DR   PeptideAtlas; Q9EPJ9; -.
DR   ProteomicsDB; 277274; -. [Q9EPJ9-1]
DR   ProteomicsDB; 277275; -. [Q9EPJ9-2]
DR   Pumba; Q9EPJ9; -.
DR   Antibodypedia; 29683; 462 antibodies from 33 providers.
DR   DNASU; 228998; -.
DR   Ensembl; ENSMUST00000029092.13; ENSMUSP00000029092.7; ENSMUSG00000027575.20. [Q9EPJ9-1]
DR   Ensembl; ENSMUST00000108859.8; ENSMUSP00000104487.2; ENSMUSG00000027575.20. [Q9EPJ9-2]
DR   Ensembl; ENSMUST00000108860.8; ENSMUSP00000104488.2; ENSMUSG00000027575.20. [Q9EPJ9-2]
DR   GeneID; 228998; -.
DR   KEGG; mmu:228998; -.
DR   UCSC; uc008okj.2; mouse. [Q9EPJ9-1]
DR   UCSC; uc008okm.2; mouse. [Q9EPJ9-2]
DR   AGR; MGI:2183559; -.
DR   CTD; 55738; -.
DR   MGI; MGI:2183559; Arfgap1.
DR   VEuPathDB; HostDB:ENSMUSG00000027575; -.
DR   eggNOG; KOG0704; Eukaryota.
DR   GeneTree; ENSGT00890000139515; -.
DR   InParanoid; Q9EPJ9; -.
DR   OMA; MSKLWEV; -.
DR   OrthoDB; 389572at2759; -.
DR   PhylomeDB; Q9EPJ9; -.
DR   TreeFam; TF105931; -.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR   BioGRID-ORCS; 228998; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Arfgap1; mouse.
DR   PRO; PR:Q9EPJ9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9EPJ9; Protein.
DR   Bgee; ENSMUSG00000027575; Expressed in humerus cartilage element and 266 other cell types or tissues.
DR   ExpressionAtlas; Q9EPJ9; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IBA:GO_Central.
DR   GO; GO:0030100; P:regulation of endocytosis; IDA:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   CDD; cd08830; ArfGap_ArfGap1; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   PANTHER; PTHR46395; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN 1; 1.
DR   PANTHER; PTHR46395:SF1; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN 1; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   Genevisible; Q9EPJ9; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; ER-Golgi transport;
KW   Golgi apparatus; GTPase activation; Metal-binding; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..414
FT                   /note="ADP-ribosylation factor GTPase-activating protein 1"
FT                   /id="PRO_0000074191"
FT   DOMAIN          7..124
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   ZN_FING         22..45
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          296..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         135
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT   MOD_RES         189
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT   MOD_RES         231
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         349
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6T3"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         379
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62848"
FT   VAR_SEQ         259..280
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_011303"
FT   CONFLICT        112
FT                   /note="R -> K (in Ref. 1; CAC18721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="N -> K (in Ref. 1; CAC18721)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   414 AA;  45288 MW;  72A3279D185714C0 CRC64;
     MASPRTRKVL KEVRAQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR GLGVHLSFVR
     SVTMDKWKDI ELEKMKAGGN AKFREFLETQ DDYEPSWSLQ DKYSSRAAAL FRDKVATLAE
     GKEWSLESSP AQNWTPPQPK TLQFTAHRAS GQPQSAAASG DKAFEDWLND DLGSYQGAQE
     NRYVGFGNTV PPQKREDDFL NNAMSSLYSG WSSFTTGASK FASAAKEGAT KFGSQASQKA
     SELGHSLNEN VLKPAQEKVK EGRIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAED
     SSDRPLEGHS YQNSSGDNSQ NSNIDQSFWE TFGSAEPPKA KSPSSDSWTC ADASTGRRSS
     DSWDVWGSGS ASNNKNSNSD GWESWEGASG EGRAKATKKA APSTADEGWD NQNW
//