ARFG1_MOUSE
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 03-AUG-2022, entry version 157.
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, Pancreas,
RC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 13.
DR IntAct; Q9EPJ9; 1.
DR STRING; 10090.ENSMUSP00000029092; -.
DR iPTMnet; Q9EPJ9; -.
DR PhosphoSitePlus; Q9EPJ9; -.
DR EPD; Q9EPJ9; -.
DR jPOST; Q9EPJ9; -.
DR MaxQB; Q9EPJ9; -.
DR PaxDb; Q9EPJ9; -.
DR PeptideAtlas; Q9EPJ9; -.
DR PRIDE; Q9EPJ9; -.
DR ProteomicsDB; 277274; -. [Q9EPJ9-1]
DR ProteomicsDB; 277275; -. [Q9EPJ9-2]
DR Antibodypedia; 29683; 416 antibodies from 33 providers.
DR DNASU; 228998; -.
DR Ensembl; ENSMUST00000029092; ENSMUSP00000029092; ENSMUSG00000027575. [Q9EPJ9-1]
DR Ensembl; ENSMUST00000108859; ENSMUSP00000104487; ENSMUSG00000027575. [Q9EPJ9-2]
DR Ensembl; ENSMUST00000108860; ENSMUSP00000104488; ENSMUSG00000027575. [Q9EPJ9-2]
DR GeneID; 228998; -.
DR KEGG; mmu:228998; -.
DR UCSC; uc008okj.2; mouse. [Q9EPJ9-1]
DR UCSC; uc008okm.2; mouse. [Q9EPJ9-2]
DR CTD; 55738; -.
DR MGI; MGI:2183559; Arfgap1.
DR VEuPathDB; HostDB:ENSMUSG00000027575; -.
DR eggNOG; KOG0704; Eukaryota.
DR GeneTree; ENSGT00890000139515; -.
DR InParanoid; Q9EPJ9; -.
DR OMA; NVCCDCN; -.
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 74 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 263 other tissues.
DR ExpressionAtlas; Q9EPJ9; baseline and differential.
DR Genevisible; Q9EPJ9; MM.
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 Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
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
