Full text data of ARFGAP1
ARFGAP1
(ARF1GAP)
[Confidence: low (only semi-automatic identification from reviews)]
ADP-ribosylation factor GTPase-activating protein 1; ARF GAP 1 (ADP-ribosylation factor 1 GTPase-activating protein; ARF1 GAP; ARF1-directed GTPase-activating protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
ADP-ribosylation factor GTPase-activating protein 1; ARF GAP 1 (ADP-ribosylation factor 1 GTPase-activating protein; ARF1 GAP; ARF1-directed GTPase-activating protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8N6T3
ID ARFG1_HUMAN Reviewed; 406 AA.
AC Q8N6T3; B7ZBI3; E1P5I9; Q6PK71; Q96KC4; Q96T02; Q9NSU3; Q9NVF6;
read moreAC Q9UIL0;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 22-JAN-2014, entry version 117.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Fetal brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-406 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-406 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Ueki N.;
RT "HRI NTT human fetal brain cDNA project.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND SER-304, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-231, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND THR-189, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-128 IN COMPLEX WITH ZINC
RP IONS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the ARFGAP domain of human ARFGAP1.";
RL Submitted (FEB-2009) to the PDB data bank.
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
CC target compartment. Probably regulates ARF1-mediated transport via
CC its interaction with the KDELR proteins and TMED2. Overexpression
CC induces the redistribution of the entire Golgi complex to the
CC endoplasmic reticulum, as when ARF1 is deactivated. Its activity
CC is stimulated by phosphoinosides and inhibited by
CC phosphatidylcholine (By similarity).
CC -!- SUBUNIT: Interacts with ARF1. Interacts with the COPI coat
CC proteins, KDELR1 and TMED2. The interaction with TMED2 inhibits
CC the GAP activity (By similarity).
CC -!- INTERACTION:
CC Q5S007:LRRK2; NbExp=6; IntAct=EBI-6288865, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC (By similarity). Note=Associates with the Golgi complex (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N6T3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6T3-2; Sequence=VSP_000298, VSP_000299;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8N6T3-3; Sequence=VSP_021818;
CC -!- DOMAIN: The region downstream of Arf-GAP domain is essential to
CC GAP activity in vivo. This region may be required for its
CC targeting to Golgi membranes (By similarity).
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55009.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55113.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAB70901.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR EMBL; AK001629; BAA91796.1; -; mRNA.
DR EMBL; AK027268; BAB55009.1; ALT_INIT; mRNA.
DR EMBL; AK027441; BAB55113.1; ALT_INIT; mRNA.
DR EMBL; AL121827; CAX12645.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75292.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75294.1; -; Genomic_DNA.
DR EMBL; BC000786; AAH00786.1; -; mRNA.
DR EMBL; BC006085; AAH06085.1; -; mRNA.
DR EMBL; BC011876; AAH11876.1; -; mRNA.
DR EMBL; BC028233; AAH28233.1; -; mRNA.
DR EMBL; AL137744; CAB70901.1; ALT_SEQ; mRNA.
DR EMBL; AB015340; BAA88117.1; -; mRNA.
DR PIR; T46298; T46298.
DR RefSeq; NP_001268411.1; NM_001281482.1.
DR RefSeq; NP_001268412.1; NM_001281483.1.
DR RefSeq; NP_001268413.1; NM_001281484.1.
DR RefSeq; NP_060679.1; NM_018209.3.
DR RefSeq; NP_783202.1; NM_175609.2.
DR UniGene; Hs.25584; -.
DR PDB; 3DWD; X-ray; 2.40 A; A/B=1-128.
DR PDB; 3O47; X-ray; 2.80 A; A/B=1-140.
DR PDBsum; 3DWD; -.
DR PDBsum; 3O47; -.
DR ProteinModelPortal; Q8N6T3; -.
DR SMR; Q8N6T3; 3-153.
DR IntAct; Q8N6T3; 19.
DR MINT; MINT-1409968; -.
DR STRING; 9606.ENSP00000314615; -.
DR PhosphoSite; Q8N6T3; -.
DR DMDM; 27923731; -.
DR PaxDb; Q8N6T3; -.
DR PRIDE; Q8N6T3; -.
DR DNASU; 55738; -.
DR Ensembl; ENST00000353546; ENSP00000314615; ENSG00000101199.
DR Ensembl; ENST00000370275; ENSP00000359298; ENSG00000101199.
DR Ensembl; ENST00000370283; ENSP00000359306; ENSG00000101199.
DR GeneID; 55738; -.
DR KEGG; hsa:55738; -.
DR UCSC; uc002yem.3; human.
DR CTD; 55738; -.
DR GeneCards; GC20P061904; -.
DR H-InvDB; HIX0174713; -.
DR HGNC; HGNC:15852; ARFGAP1.
DR HPA; HPA051019; -.
DR MIM; 608377; gene.
DR neXtProt; NX_Q8N6T3; -.
DR PharmGKB; PA164741246; -.
DR eggNOG; COG5347; -.
DR HOVERGEN; HBG050562; -.
DR KO; K12492; -.
DR OMA; GWDNQNW; -.
DR OrthoDB; EOG7C8GH3; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; ARFGAP1; human.
DR EvolutionaryTrace; Q8N6T3; -.
DR GeneWiki; ARFGAP1; -.
DR GenomeRNAi; 55738; -.
DR NextBio; 60684; -.
DR PRO; PR:Q8N6T3; -.
DR ArrayExpress; Q8N6T3; -.
DR Bgee; Q8N6T3; -.
DR CleanEx; HS_ARFGAP1; -.
DR Genevestigator; Q8N6T3; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
DR InterPro; IPR001164; ArfGAP.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; ER-Golgi transport; Golgi apparatus; GTPase activation;
KW Metal-binding; Phosphoprotein; Polymorphism; Protein transport;
KW Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1 406 ADP-ribosylation factor GTPase-activating
FT protein 1.
FT /FTId=PRO_0000074190.
FT DOMAIN 7 124 Arf-GAP.
FT ZN_FING 22 45 C4-type.
FT MOD_RES 135 135 Phosphothreonine.
FT MOD_RES 189 189 Phosphothreonine.
FT MOD_RES 231 231 N6-acetyllysine.
FT MOD_RES 304 304 Phosphoserine.
FT VAR_SEQ 239 239 K -> KFWGHKQQPEP (in isoform 2).
FT /FTId=VSP_000298.
FT VAR_SEQ 279 406 VQGVGSKGWRDVTTFFSGKAEGPLDSPSEGHSYQNSGLDHF
FT QNSNIDQSFWETFGSAEPTKTRKSPSSDSWTCADTSTERRS
FT SDSWEVWGSASTNRNSNSDGGEGGEGTKKAVPPAVPTDDGW
FT DNQNW -> CQRRLCCHQSHCSAGHLGRAFCPVSWHEALCG
FT QTGREEQASLLPPKHVVGALEVCARGCPRCHVPHTPGTAAE
FT WPGRLCLSRESVVRDGGTSPPFFRGKQRAPWTAPRRATVIR
FT TAVWTTSKTAT (in isoform 3).
FT /FTId=VSP_021818.
FT VAR_SEQ 279 280 Missing (in isoform 2).
FT /FTId=VSP_000299.
FT VARIANT 184 184 V -> M (in dbSNP:rs2273499).
FT /FTId=VAR_015187.
FT CONFLICT 274 274 Q -> R (in Ref. 1; BAB55009).
FT HELIX 4 14
FT TURN 17 20
FT TURN 23 25
FT STRAND 32 34
FT TURN 35 38
FT STRAND 39 41
FT HELIX 43 52
FT TURN 54 56
FT STRAND 59 62
FT HELIX 69 77
FT HELIX 80 88
FT HELIX 99 103
FT HELIX 106 119
SQ SEQUENCE 406 AA; 44668 MW; CAE41828DE660621 CRC64;
MASPRTRKVL KEVRVQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR GLGVHLSFVR
SVTMDKWKDI ELEKMKAGGN AKFREFLESQ EDYDPCWSLQ EKYNSRAAAL FRDKVVALAE
GREWSLESSP AQNWTPPQPR TLPSMVHRVS GQPQSVTASS DKAFEDWLND DLGSYQGAQG
NRYVGFGNTP PPQKKEDDFL NNAMSSLYSG WSSFTTGASR FASAAKEGAT KFGSQASQKA
SELGHSLNEN VLKPAQEKVK EGKIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAEG
PLDSPSEGHS YQNSGLDHFQ NSNIDQSFWE TFGSAEPTKT RKSPSSDSWT CADTSTERRS
SDSWEVWGSA STNRNSNSDG GEGGEGTKKA VPPAVPTDDG WDNQNW
//
ID ARFG1_HUMAN Reviewed; 406 AA.
AC Q8N6T3; B7ZBI3; E1P5I9; Q6PK71; Q96KC4; Q96T02; Q9NSU3; Q9NVF6;
read moreAC Q9UIL0;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 22-JAN-2014, entry version 117.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Fetal brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-406 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-406 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Ueki N.;
RT "HRI NTT human fetal brain cDNA project.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND SER-304, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-231, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND THR-189, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-128 IN COMPLEX WITH ZINC
RP IONS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the ARFGAP domain of human ARFGAP1.";
RL Submitted (FEB-2009) to the PDB data bank.
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
CC target compartment. Probably regulates ARF1-mediated transport via
CC its interaction with the KDELR proteins and TMED2. Overexpression
CC induces the redistribution of the entire Golgi complex to the
CC endoplasmic reticulum, as when ARF1 is deactivated. Its activity
CC is stimulated by phosphoinosides and inhibited by
CC phosphatidylcholine (By similarity).
CC -!- SUBUNIT: Interacts with ARF1. Interacts with the COPI coat
CC proteins, KDELR1 and TMED2. The interaction with TMED2 inhibits
CC the GAP activity (By similarity).
CC -!- INTERACTION:
CC Q5S007:LRRK2; NbExp=6; IntAct=EBI-6288865, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC (By similarity). Note=Associates with the Golgi complex (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N6T3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6T3-2; Sequence=VSP_000298, VSP_000299;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8N6T3-3; Sequence=VSP_021818;
CC -!- DOMAIN: The region downstream of Arf-GAP domain is essential to
CC GAP activity in vivo. This region may be required for its
CC targeting to Golgi membranes (By similarity).
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55009.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55113.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAB70901.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR EMBL; AK001629; BAA91796.1; -; mRNA.
DR EMBL; AK027268; BAB55009.1; ALT_INIT; mRNA.
DR EMBL; AK027441; BAB55113.1; ALT_INIT; mRNA.
DR EMBL; AL121827; CAX12645.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75292.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75294.1; -; Genomic_DNA.
DR EMBL; BC000786; AAH00786.1; -; mRNA.
DR EMBL; BC006085; AAH06085.1; -; mRNA.
DR EMBL; BC011876; AAH11876.1; -; mRNA.
DR EMBL; BC028233; AAH28233.1; -; mRNA.
DR EMBL; AL137744; CAB70901.1; ALT_SEQ; mRNA.
DR EMBL; AB015340; BAA88117.1; -; mRNA.
DR PIR; T46298; T46298.
DR RefSeq; NP_001268411.1; NM_001281482.1.
DR RefSeq; NP_001268412.1; NM_001281483.1.
DR RefSeq; NP_001268413.1; NM_001281484.1.
DR RefSeq; NP_060679.1; NM_018209.3.
DR RefSeq; NP_783202.1; NM_175609.2.
DR UniGene; Hs.25584; -.
DR PDB; 3DWD; X-ray; 2.40 A; A/B=1-128.
DR PDB; 3O47; X-ray; 2.80 A; A/B=1-140.
DR PDBsum; 3DWD; -.
DR PDBsum; 3O47; -.
DR ProteinModelPortal; Q8N6T3; -.
DR SMR; Q8N6T3; 3-153.
DR IntAct; Q8N6T3; 19.
DR MINT; MINT-1409968; -.
DR STRING; 9606.ENSP00000314615; -.
DR PhosphoSite; Q8N6T3; -.
DR DMDM; 27923731; -.
DR PaxDb; Q8N6T3; -.
DR PRIDE; Q8N6T3; -.
DR DNASU; 55738; -.
DR Ensembl; ENST00000353546; ENSP00000314615; ENSG00000101199.
DR Ensembl; ENST00000370275; ENSP00000359298; ENSG00000101199.
DR Ensembl; ENST00000370283; ENSP00000359306; ENSG00000101199.
DR GeneID; 55738; -.
DR KEGG; hsa:55738; -.
DR UCSC; uc002yem.3; human.
DR CTD; 55738; -.
DR GeneCards; GC20P061904; -.
DR H-InvDB; HIX0174713; -.
DR HGNC; HGNC:15852; ARFGAP1.
DR HPA; HPA051019; -.
DR MIM; 608377; gene.
DR neXtProt; NX_Q8N6T3; -.
DR PharmGKB; PA164741246; -.
DR eggNOG; COG5347; -.
DR HOVERGEN; HBG050562; -.
DR KO; K12492; -.
DR OMA; GWDNQNW; -.
DR OrthoDB; EOG7C8GH3; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; ARFGAP1; human.
DR EvolutionaryTrace; Q8N6T3; -.
DR GeneWiki; ARFGAP1; -.
DR GenomeRNAi; 55738; -.
DR NextBio; 60684; -.
DR PRO; PR:Q8N6T3; -.
DR ArrayExpress; Q8N6T3; -.
DR Bgee; Q8N6T3; -.
DR CleanEx; HS_ARFGAP1; -.
DR Genevestigator; Q8N6T3; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
DR InterPro; IPR001164; ArfGAP.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; ER-Golgi transport; Golgi apparatus; GTPase activation;
KW Metal-binding; Phosphoprotein; Polymorphism; Protein transport;
KW Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1 406 ADP-ribosylation factor GTPase-activating
FT protein 1.
FT /FTId=PRO_0000074190.
FT DOMAIN 7 124 Arf-GAP.
FT ZN_FING 22 45 C4-type.
FT MOD_RES 135 135 Phosphothreonine.
FT MOD_RES 189 189 Phosphothreonine.
FT MOD_RES 231 231 N6-acetyllysine.
FT MOD_RES 304 304 Phosphoserine.
FT VAR_SEQ 239 239 K -> KFWGHKQQPEP (in isoform 2).
FT /FTId=VSP_000298.
FT VAR_SEQ 279 406 VQGVGSKGWRDVTTFFSGKAEGPLDSPSEGHSYQNSGLDHF
FT QNSNIDQSFWETFGSAEPTKTRKSPSSDSWTCADTSTERRS
FT SDSWEVWGSASTNRNSNSDGGEGGEGTKKAVPPAVPTDDGW
FT DNQNW -> CQRRLCCHQSHCSAGHLGRAFCPVSWHEALCG
FT QTGREEQASLLPPKHVVGALEVCARGCPRCHVPHTPGTAAE
FT WPGRLCLSRESVVRDGGTSPPFFRGKQRAPWTAPRRATVIR
FT TAVWTTSKTAT (in isoform 3).
FT /FTId=VSP_021818.
FT VAR_SEQ 279 280 Missing (in isoform 2).
FT /FTId=VSP_000299.
FT VARIANT 184 184 V -> M (in dbSNP:rs2273499).
FT /FTId=VAR_015187.
FT CONFLICT 274 274 Q -> R (in Ref. 1; BAB55009).
FT HELIX 4 14
FT TURN 17 20
FT TURN 23 25
FT STRAND 32 34
FT TURN 35 38
FT STRAND 39 41
FT HELIX 43 52
FT TURN 54 56
FT STRAND 59 62
FT HELIX 69 77
FT HELIX 80 88
FT HELIX 99 103
FT HELIX 106 119
SQ SEQUENCE 406 AA; 44668 MW; CAE41828DE660621 CRC64;
MASPRTRKVL KEVRVQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR GLGVHLSFVR
SVTMDKWKDI ELEKMKAGGN AKFREFLESQ EDYDPCWSLQ EKYNSRAAAL FRDKVVALAE
GREWSLESSP AQNWTPPQPR TLPSMVHRVS GQPQSVTASS DKAFEDWLND DLGSYQGAQG
NRYVGFGNTP PPQKKEDDFL NNAMSSLYSG WSSFTTGASR FASAAKEGAT KFGSQASQKA
SELGHSLNEN VLKPAQEKVK EGKIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAEG
PLDSPSEGHS YQNSGLDHFQ NSNIDQSFWE TFGSAEPTKT RKSPSSDSWT CADTSTERRS
SDSWEVWGSA STNRNSNSDG GEGGEGTKKA VPPAVPTDDG WDNQNW
//
MIM
608377
*RECORD*
*FIELD* NO
608377
*FIELD* TI
*608377 ADP-RIBOSYLATION FACTOR GTPase-ACTIVATING PROTEIN 1; ARFGAP1
*FIELD* TX
DESCRIPTION
read more
Protein coats deform flat lipid membranes into buds and capture membrane
proteins to form transport vesicles. The assembly-disassembly cycle of
the COPI coat (601924) on Golgi membranes is coupled to the GTP-GDP
cycle of the small G protein ARF1 (103180). ARFGAP1 contributes to
vesicle budding by increasing the GTPase activity of ARF1 (Bigay et al.,
2003).
CLONING
Huber et al. (2001) cloned rat Arfgap1, which they called Gap1. It
encodes a deduced 45-kD protein. The catalytic domain of rat Arfgap1
resides within the first 130 to 140 amino acids and contains the
essential zinc finger structure.
GENE FUNCTION
Using rat Arfgap1 as a model enzyme, Huber et al. (2001) described
methods for assaying the hydrolysis of GTP by ARFGAP1. They also noted
that a yeast ARFGAP, Gcs1, interacts with phospholipid vesicles. The
interaction is greatest with vesicles containing
phosphatidylethanolamine and is stimulated by diacylglycerols bearing 1
or 2 unsaturated fatty acids.
Bigay et al. (2003) found that the curvature of the lipid bilayer
affects the catalytic activity of eukaryotic Arfgap1. As the curvature
approached that of a typical transport vesicle, the rate of
Arfgap1-catalyzed GTP hydrolysis in Arf1 and the rate of COPI
disassembly from membranes increased more than 2 orders of magnitude.
MAPPING
Hartz (2004) mapped the ARFGAP1 gene to chromosome 20q13.33 based on an
alignment of the ARFGAP1 sequence (GenBank GENBANK AK001629) with the
genomic sequence.
*FIELD* RF
1. Bigay, J.; Gounon, P.; Robineau, S.; Antonny, B.: Lipid packing
sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer
curvature. Nature 426: 563-566, 2003.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/7/2004.
3. Huber, I.; Rotman, M.; Pick, E.; Makler, V.; Rothem, L.; Cukierman,
E.; Cassel, D.: Expression, purification, and properties of ADP-ribosylation
factor (ARF) GTPase activating protein-1. Methods Enzymol. 329:
307-316, 2001.
*FIELD* CD
Patricia A. Hartz: 1/7/2004
*FIELD* ED
mgross: 01/07/2004
*RECORD*
*FIELD* NO
608377
*FIELD* TI
*608377 ADP-RIBOSYLATION FACTOR GTPase-ACTIVATING PROTEIN 1; ARFGAP1
*FIELD* TX
DESCRIPTION
read more
Protein coats deform flat lipid membranes into buds and capture membrane
proteins to form transport vesicles. The assembly-disassembly cycle of
the COPI coat (601924) on Golgi membranes is coupled to the GTP-GDP
cycle of the small G protein ARF1 (103180). ARFGAP1 contributes to
vesicle budding by increasing the GTPase activity of ARF1 (Bigay et al.,
2003).
CLONING
Huber et al. (2001) cloned rat Arfgap1, which they called Gap1. It
encodes a deduced 45-kD protein. The catalytic domain of rat Arfgap1
resides within the first 130 to 140 amino acids and contains the
essential zinc finger structure.
GENE FUNCTION
Using rat Arfgap1 as a model enzyme, Huber et al. (2001) described
methods for assaying the hydrolysis of GTP by ARFGAP1. They also noted
that a yeast ARFGAP, Gcs1, interacts with phospholipid vesicles. The
interaction is greatest with vesicles containing
phosphatidylethanolamine and is stimulated by diacylglycerols bearing 1
or 2 unsaturated fatty acids.
Bigay et al. (2003) found that the curvature of the lipid bilayer
affects the catalytic activity of eukaryotic Arfgap1. As the curvature
approached that of a typical transport vesicle, the rate of
Arfgap1-catalyzed GTP hydrolysis in Arf1 and the rate of COPI
disassembly from membranes increased more than 2 orders of magnitude.
MAPPING
Hartz (2004) mapped the ARFGAP1 gene to chromosome 20q13.33 based on an
alignment of the ARFGAP1 sequence (GenBank GENBANK AK001629) with the
genomic sequence.
*FIELD* RF
1. Bigay, J.; Gounon, P.; Robineau, S.; Antonny, B.: Lipid packing
sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer
curvature. Nature 426: 563-566, 2003.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/7/2004.
3. Huber, I.; Rotman, M.; Pick, E.; Makler, V.; Rothem, L.; Cukierman,
E.; Cassel, D.: Expression, purification, and properties of ADP-ribosylation
factor (ARF) GTPase activating protein-1. Methods Enzymol. 329:
307-316, 2001.
*FIELD* CD
Patricia A. Hartz: 1/7/2004
*FIELD* ED
mgross: 01/07/2004