Full text data of ARFGAP3
ARFGAP3
(ARFGAP1)
[Confidence: low (only semi-automatic identification from reviews)]
ADP-ribosylation factor GTPase-activating protein 3; ARF GAP 3
ADP-ribosylation factor GTPase-activating protein 3; ARF GAP 3
UniProt
Q9NP61
ID ARFG3_HUMAN Reviewed; 516 AA.
AC Q9NP61; E9PB03; Q9BSC6; Q9H9J0; Q9NT10; Q9NUP5; Q9Y4V3; Q9Y4V4;
read moreDT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE Short=ARF GAP 3;
GN Name=ARFGAP3; Synonyms=ARFGAP1;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10704287; DOI=10.1006/geno.1999.6095;
RA Zhang C., Yu Y., Zhang S., Liu M., Xing G., Wei H., Bi J., Liu X.,
RA Zhou G., Dong C., Hu Z., Zhang Y., Luo L., Wu C., Zhao S., He F.;
RT "Characterization, chromosomal assignment, and tissue expression of a
RT novel human gene belonging to the ARF GAP family.";
RL Genomics 63:400-408(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J.,
RA Knowles S., Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ARG-355.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ARG-355.
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-516 (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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-516 (ISOFORM 1), AND
RP VARIANT ARG-355.
RC TISSUE=Placenta;
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 [8]
RP FUNCTION, AND ENZYME REGULATION.
RX PubMed=11172815; DOI=10.1016/S0014-5793(01)02134-2;
RA Liu X., Zhang C., Xing G., Chen Q., He F.;
RT "Functional characterization of novel human ARFGAP3.";
RL FEBS Lett. 490:79-83(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17760859; DOI=10.1111/j.1600-0854.2007.00631.x;
RA Frigerio G., Grimsey N., Dale M., Majoul I., Duden R.;
RT "Two human ARFGAPs associated with COP-I-coated vesicles.";
RL Traffic 8:1644-1655(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-453, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-453, AND
RP MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-331, 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 [13]
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 [14]
RP STRUCTURE BY NMR OF 1-136.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ARFGAP domain of ADP-ribosylation factor
RT GTPase-activating protein 3 (ARFGAP 3).";
RL Submitted (NOV-2005) to the PDB data bank.
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-355, AND MASS SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-290.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation
CC factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to
CC dissociation of coatomer from Golgi-derived membranes to allow
CC fusion with target membranes.
CC -!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=Also found on
CC peripheral punctate structures likely to be endoplasmic reticulum-
CC Golgi intermediate compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NP61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP61-2; Sequence=VSP_046888;
CC Note=Gene prediction based on EST data;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in
CC endocrine glands (pancreas, pituitary gland, salivary gland, and
CC prostate) and testis with a much higher expression in the testis
CC than in the ovary.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher level in adult thymus,
CC brain and lung, than in corresponding fetal tissues. Expressed at
CC lower level in spleen, heart, kidney and liver during development.
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- CAUTION: Was originally (PubMed:10704287) termed ARFGAP1.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92076.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14236.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF111847; AAF40310.1; -; mRNA.
DR EMBL; AL159143; CAB76901.1; -; mRNA.
DR EMBL; CR456382; CAG30268.1; -; mRNA.
DR EMBL; AL049757; CAI21510.1; -; Genomic_DNA.
DR EMBL; AL049758; CAI21510.1; JOINED; Genomic_DNA.
DR EMBL; AL049758; CAI20950.1; -; Genomic_DNA.
DR EMBL; AL049757; CAI20950.1; JOINED; Genomic_DNA.
DR EMBL; BC005122; AAH05122.1; -; mRNA.
DR EMBL; AL137598; CAB70834.1; -; mRNA.
DR EMBL; AK002083; BAA92076.1; ALT_INIT; mRNA.
DR EMBL; AK022768; BAB14236.1; ALT_INIT; mRNA.
DR PIR; T46305; T46305.
DR RefSeq; NP_001135765.1; NM_001142293.1.
DR RefSeq; NP_055385.3; NM_014570.4.
DR UniGene; Hs.685225; -.
DR PDB; 2CRW; NMR; -; A=1-136.
DR PDBsum; 2CRW; -.
DR ProteinModelPortal; Q9NP61; -.
DR SMR; Q9NP61; 3-136.
DR IntAct; Q9NP61; 4.
DR STRING; 9606.ENSP00000263245; -.
DR PhosphoSite; Q9NP61; -.
DR DMDM; 21263420; -.
DR PaxDb; Q9NP61; -.
DR PeptideAtlas; Q9NP61; -.
DR PRIDE; Q9NP61; -.
DR DNASU; 26286; -.
DR Ensembl; ENST00000263245; ENSP00000263245; ENSG00000242247.
DR Ensembl; ENST00000437119; ENSP00000388791; ENSG00000242247.
DR GeneID; 26286; -.
DR KEGG; hsa:26286; -.
DR UCSC; uc010gzf.2; human.
DR CTD; 26286; -.
DR GeneCards; GC22M043192; -.
DR HGNC; HGNC:661; ARFGAP3.
DR HPA; HPA000638; -.
DR MIM; 612439; gene.
DR neXtProt; NX_Q9NP61; -.
DR PharmGKB; PA35024; -.
DR eggNOG; COG5347; -.
DR HOVERGEN; HBG050563; -.
DR InParanoid; Q9NP61; -.
DR KO; K12493; -.
DR OMA; NEGGPEQ; -.
DR OrthoDB; EOG7B8S42; -.
DR PhylomeDB; Q9NP61; -.
DR EvolutionaryTrace; Q9NP61; -.
DR GeneWiki; ARFGAP3; -.
DR GenomeRNAi; 26286; -.
DR NextBio; 48617; -.
DR PRO; PR:Q9NP61; -.
DR ArrayExpress; Q9NP61; -.
DR Bgee; Q9NP61; -.
DR CleanEx; HS_ARFGAP1; -.
DR CleanEx; HS_ARFGAP3; -.
DR Genevestigator; Q9NP61; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008060; F:ARF GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0008565; F:protein transporter activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IEP:UniProtKB.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
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; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; ER-Golgi transport; Golgi apparatus; GTPase activation;
KW Membrane; Metal-binding; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1 516 ADP-ribosylation factor GTPase-activating
FT protein 3.
FT /FTId=PRO_0000074193.
FT DOMAIN 10 126 Arf-GAP.
FT ZN_FING 25 48 C4-type.
FT COILED 243 263 Potential.
FT COMPBIAS 348 377 Ser-rich.
FT MOD_RES 231 231 Phosphoserine.
FT MOD_RES 331 331 Phosphoserine.
FT MOD_RES 370 370 Phosphoserine.
FT MOD_RES 453 453 Phosphoserine.
FT VAR_SEQ 88 131 Missing (in isoform 2).
FT /FTId=VSP_046888.
FT VARIANT 231 231 S -> G (in dbSNP:rs9607957).
FT /FTId=VAR_055523.
FT VARIANT 290 290 E -> G (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036177.
FT VARIANT 355 355 S -> R (in dbSNP:rs1018448).
FT /FTId=VAR_013447.
FT VARIANT 370 370 S -> G (in dbSNP:rs16986123).
FT /FTId=VAR_055524.
FT VARIANT 468 468 Q -> H (in dbSNP:rs35498349).
FT /FTId=VAR_055525.
FT VARIANT 482 482 A -> T (in dbSNP:rs36003980).
FT /FTId=VAR_055526.
FT VARIANT 490 490 Q -> R (in dbSNP:rs11551619).
FT /FTId=VAR_055527.
FT CONFLICT 339 339 K -> R (in Ref. 7; BAA92076).
FT CONFLICT 401 401 T -> A (in Ref. 7; BAA92076).
FT CONFLICT 458 458 S -> P (in Ref. 7; BAB14236).
FT HELIX 6 18
FT TURN 20 22
FT STRAND 26 28
FT TURN 38 41
FT HELIX 46 55
FT TURN 57 59
FT STRAND 65 67
FT HELIX 73 80
FT HELIX 84 94
FT HELIX 101 104
FT HELIX 108 126
FT STRAND 129 131
SQ SEQUENCE 516 AA; 56928 MW; E355E56A5D867F8E CRC64;
MGDPSKQDIL TIFKRLRSVP TNKVCFDCGA KNPSWASITY GVFLCIDCSG SHRSLGVHLS
FIRSTELDSN WSWFQLRCMQ VGGNASASSF FHQHGCSTND TNAKYNSRAA QLYREKIKSL
ASQATRKHGT DLWLDSCVVP PLSPPPKEED FFASHVSPEV SDTAWASAIA EPSSLTSRPV
ETTLENNEGG QEQGPSVEGL NVPTKATLEV SSIIKKKPNQ AKKGLGAKKG SLGAQKLANT
CFNEIEKQAQ AADKMKEQED LAKVVSKEES IVSSLRLAYK DLEIQMKKDE KMNISGKKNV
DSDRLGMGFG NCRSVISHSV TSDMQTIEQE SPIMAKPRKK YNDDSDDSYF TSSSSYFDEP
VELRSSSFSS WDDSSDSYWK KETSKDTETV LKTTGYSDRP TARRKPDYEP VENTDEAQKK
FGNVKAISSD MYFGRQSQAD YETRARLERL SASSSISSAD LFEEPRKQPA GNYSLSSVLP
NAPDMAQFKQ GVRSVAGKLS VFANGVVTSI QDRYGS
//
ID ARFG3_HUMAN Reviewed; 516 AA.
AC Q9NP61; E9PB03; Q9BSC6; Q9H9J0; Q9NT10; Q9NUP5; Q9Y4V3; Q9Y4V4;
read moreDT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE Short=ARF GAP 3;
GN Name=ARFGAP3; Synonyms=ARFGAP1;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10704287; DOI=10.1006/geno.1999.6095;
RA Zhang C., Yu Y., Zhang S., Liu M., Xing G., Wei H., Bi J., Liu X.,
RA Zhou G., Dong C., Hu Z., Zhang Y., Luo L., Wu C., Zhao S., He F.;
RT "Characterization, chromosomal assignment, and tissue expression of a
RT novel human gene belonging to the ARF GAP family.";
RL Genomics 63:400-408(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J.,
RA Knowles S., Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ARG-355.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ARG-355.
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-516 (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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-516 (ISOFORM 1), AND
RP VARIANT ARG-355.
RC TISSUE=Placenta;
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 [8]
RP FUNCTION, AND ENZYME REGULATION.
RX PubMed=11172815; DOI=10.1016/S0014-5793(01)02134-2;
RA Liu X., Zhang C., Xing G., Chen Q., He F.;
RT "Functional characterization of novel human ARFGAP3.";
RL FEBS Lett. 490:79-83(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17760859; DOI=10.1111/j.1600-0854.2007.00631.x;
RA Frigerio G., Grimsey N., Dale M., Majoul I., Duden R.;
RT "Two human ARFGAPs associated with COP-I-coated vesicles.";
RL Traffic 8:1644-1655(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-453, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-453, AND
RP MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-331, 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 [13]
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 [14]
RP STRUCTURE BY NMR OF 1-136.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ARFGAP domain of ADP-ribosylation factor
RT GTPase-activating protein 3 (ARFGAP 3).";
RL Submitted (NOV-2005) to the PDB data bank.
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-355, AND MASS SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-290.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation
CC factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to
CC dissociation of coatomer from Golgi-derived membranes to allow
CC fusion with target membranes.
CC -!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=Also found on
CC peripheral punctate structures likely to be endoplasmic reticulum-
CC Golgi intermediate compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NP61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP61-2; Sequence=VSP_046888;
CC Note=Gene prediction based on EST data;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in
CC endocrine glands (pancreas, pituitary gland, salivary gland, and
CC prostate) and testis with a much higher expression in the testis
CC than in the ovary.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher level in adult thymus,
CC brain and lung, than in corresponding fetal tissues. Expressed at
CC lower level in spleen, heart, kidney and liver during development.
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- CAUTION: Was originally (PubMed:10704287) termed ARFGAP1.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92076.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14236.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF111847; AAF40310.1; -; mRNA.
DR EMBL; AL159143; CAB76901.1; -; mRNA.
DR EMBL; CR456382; CAG30268.1; -; mRNA.
DR EMBL; AL049757; CAI21510.1; -; Genomic_DNA.
DR EMBL; AL049758; CAI21510.1; JOINED; Genomic_DNA.
DR EMBL; AL049758; CAI20950.1; -; Genomic_DNA.
DR EMBL; AL049757; CAI20950.1; JOINED; Genomic_DNA.
DR EMBL; BC005122; AAH05122.1; -; mRNA.
DR EMBL; AL137598; CAB70834.1; -; mRNA.
DR EMBL; AK002083; BAA92076.1; ALT_INIT; mRNA.
DR EMBL; AK022768; BAB14236.1; ALT_INIT; mRNA.
DR PIR; T46305; T46305.
DR RefSeq; NP_001135765.1; NM_001142293.1.
DR RefSeq; NP_055385.3; NM_014570.4.
DR UniGene; Hs.685225; -.
DR PDB; 2CRW; NMR; -; A=1-136.
DR PDBsum; 2CRW; -.
DR ProteinModelPortal; Q9NP61; -.
DR SMR; Q9NP61; 3-136.
DR IntAct; Q9NP61; 4.
DR STRING; 9606.ENSP00000263245; -.
DR PhosphoSite; Q9NP61; -.
DR DMDM; 21263420; -.
DR PaxDb; Q9NP61; -.
DR PeptideAtlas; Q9NP61; -.
DR PRIDE; Q9NP61; -.
DR DNASU; 26286; -.
DR Ensembl; ENST00000263245; ENSP00000263245; ENSG00000242247.
DR Ensembl; ENST00000437119; ENSP00000388791; ENSG00000242247.
DR GeneID; 26286; -.
DR KEGG; hsa:26286; -.
DR UCSC; uc010gzf.2; human.
DR CTD; 26286; -.
DR GeneCards; GC22M043192; -.
DR HGNC; HGNC:661; ARFGAP3.
DR HPA; HPA000638; -.
DR MIM; 612439; gene.
DR neXtProt; NX_Q9NP61; -.
DR PharmGKB; PA35024; -.
DR eggNOG; COG5347; -.
DR HOVERGEN; HBG050563; -.
DR InParanoid; Q9NP61; -.
DR KO; K12493; -.
DR OMA; NEGGPEQ; -.
DR OrthoDB; EOG7B8S42; -.
DR PhylomeDB; Q9NP61; -.
DR EvolutionaryTrace; Q9NP61; -.
DR GeneWiki; ARFGAP3; -.
DR GenomeRNAi; 26286; -.
DR NextBio; 48617; -.
DR PRO; PR:Q9NP61; -.
DR ArrayExpress; Q9NP61; -.
DR Bgee; Q9NP61; -.
DR CleanEx; HS_ARFGAP1; -.
DR CleanEx; HS_ARFGAP3; -.
DR Genevestigator; Q9NP61; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008060; F:ARF GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0008565; F:protein transporter activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IEP:UniProtKB.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
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; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; ER-Golgi transport; Golgi apparatus; GTPase activation;
KW Membrane; Metal-binding; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1 516 ADP-ribosylation factor GTPase-activating
FT protein 3.
FT /FTId=PRO_0000074193.
FT DOMAIN 10 126 Arf-GAP.
FT ZN_FING 25 48 C4-type.
FT COILED 243 263 Potential.
FT COMPBIAS 348 377 Ser-rich.
FT MOD_RES 231 231 Phosphoserine.
FT MOD_RES 331 331 Phosphoserine.
FT MOD_RES 370 370 Phosphoserine.
FT MOD_RES 453 453 Phosphoserine.
FT VAR_SEQ 88 131 Missing (in isoform 2).
FT /FTId=VSP_046888.
FT VARIANT 231 231 S -> G (in dbSNP:rs9607957).
FT /FTId=VAR_055523.
FT VARIANT 290 290 E -> G (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036177.
FT VARIANT 355 355 S -> R (in dbSNP:rs1018448).
FT /FTId=VAR_013447.
FT VARIANT 370 370 S -> G (in dbSNP:rs16986123).
FT /FTId=VAR_055524.
FT VARIANT 468 468 Q -> H (in dbSNP:rs35498349).
FT /FTId=VAR_055525.
FT VARIANT 482 482 A -> T (in dbSNP:rs36003980).
FT /FTId=VAR_055526.
FT VARIANT 490 490 Q -> R (in dbSNP:rs11551619).
FT /FTId=VAR_055527.
FT CONFLICT 339 339 K -> R (in Ref. 7; BAA92076).
FT CONFLICT 401 401 T -> A (in Ref. 7; BAA92076).
FT CONFLICT 458 458 S -> P (in Ref. 7; BAB14236).
FT HELIX 6 18
FT TURN 20 22
FT STRAND 26 28
FT TURN 38 41
FT HELIX 46 55
FT TURN 57 59
FT STRAND 65 67
FT HELIX 73 80
FT HELIX 84 94
FT HELIX 101 104
FT HELIX 108 126
FT STRAND 129 131
SQ SEQUENCE 516 AA; 56928 MW; E355E56A5D867F8E CRC64;
MGDPSKQDIL TIFKRLRSVP TNKVCFDCGA KNPSWASITY GVFLCIDCSG SHRSLGVHLS
FIRSTELDSN WSWFQLRCMQ VGGNASASSF FHQHGCSTND TNAKYNSRAA QLYREKIKSL
ASQATRKHGT DLWLDSCVVP PLSPPPKEED FFASHVSPEV SDTAWASAIA EPSSLTSRPV
ETTLENNEGG QEQGPSVEGL NVPTKATLEV SSIIKKKPNQ AKKGLGAKKG SLGAQKLANT
CFNEIEKQAQ AADKMKEQED LAKVVSKEES IVSSLRLAYK DLEIQMKKDE KMNISGKKNV
DSDRLGMGFG NCRSVISHSV TSDMQTIEQE SPIMAKPRKK YNDDSDDSYF TSSSSYFDEP
VELRSSSFSS WDDSSDSYWK KETSKDTETV LKTTGYSDRP TARRKPDYEP VENTDEAQKK
FGNVKAISSD MYFGRQSQAD YETRARLERL SASSSISSAD LFEEPRKQPA GNYSLSSVLP
NAPDMAQFKQ GVRSVAGKLS VFANGVVTSI QDRYGS
//
MIM
612439
*RECORD*
*FIELD* NO
612439
*FIELD* TI
*612439 ADP-RIBOSYLATION FACTOR GTPase-ACTIVATING PROTEIN 3; ARFGAP3
*FIELD* TX
DESCRIPTION
read more
ADP ribosylation factors (ARFs) are critical in intracellular vesicular
trafficking. GTP hydrolysis by ARFs requires interaction with
GTPase-activating proteins, such as ARFGAP3 (Zhang et al., 2000).
CLONING
By large-scale sequencing of clones obtained from a fetal liver cDNA
library, followed by database analysis and 5-prime RACE, Zhang et al.
(2000) cloned ARFGAP3, which they called ARFGAP1. The deduced 516-amino
acid protein has a calculated molecular mass of 57 kD and is 28%
identical to rat Arfgap1 (608377). ARFGAP3 has an N-terminal GATA1
(305371)-type zinc finger motif containing 4 cysteines that is highly
conserved among ARFGAPs, as well as multiple potential phosphorylation
sites. Northern blot analysis detected a 2.7-kb transcript in all fetal
tissues and cancer cell lines examined. RNA dot blot analysis revealed
variable ARFGAP3 expression in all adult and fetal tissues examined.
Highest expression was in testis and endocrine tissues, including
pancreas, adrenal gland, pituitary, salivary gland, and prostate.
Liu et al. (2001) found that fluorescence-tagged ARFGAP3 concentrated in
the perinuclear region of transfected COS-7 cells.
GENE FUNCTION
Using purified recombinant proteins, Liu et al. (2001) demonstrated that
ARFGAP3 stimulated ARF1 (103180)-mediated GTP hydrolysis in a
concentration-dependent manner. Phosphatidylinositol 4,5-bisphosphate
acted as an ARFGAP3 agonist, and phosphatidylcholine acted as an ARFGAP3
antagonist. Overexpression of ARFGAP3 in COS-7 cells reduced
constitutive secretion of secreted alkaline phosphatase (SEAP; 171800),
indicating that ARFGAP3 regulates the early secretory pathway of
proteins.
Using rat, monkey, and human cell lines, Frigerio et al. (2007) showed
that ARFGAP2 (606908) and ARFGAP3 functioned in intracellular
trafficking of COPI (601924)-coated vesicles. Both ARFGAP2 and ARFGAP3
colocalized with COPI subunits in the Golgi complex and peripheral
punctate structures and associated with COPI-coated vesicles generated
from Golgi membranes. Silencing of ARFGAP1 or a combination of ARFGAP2
and ARFGAP3 in HeLa cells did not decrease cell viability, but silencing
of all 3 ARFGAPs caused cell death.
GENE STRUCTURE
Zhang et al. (2000) determined that the ARFGAP3 gene contains 16 exons
and spans about 60 kb. The upstream region is 73.87% GC and includes 2
potential SP1 (189906)-binding sites. It has no CAAT or TATA box
elements.
MAPPING
By radiation hybrid and genomic sequence analyses, Zhang et al. (2000)
mapped the ARFGAP3 gene to chromosome 22q13.2.
*FIELD* RF
1. Frigerio, G.; Grimsey, N.; Dale, M.; Majoul, I.; Duden, R.: Two
human ARFGAPs associated with COP-I-coated vesicles. Traffic 8:
1644-1655, 2007.
2. Liu, X.; Zhang, C.; Xing, G.; Chen, Q.; He, F.: Functional characterization
of novel human ARFGAP3. FEBS Lett. 490: 79-83, 2001.
3. Zhang, C.; Yu, Y.; Zhang, S.; Liu, M.; Xing, G.; Wei, H.; Bi, J.;
Liu, X.; Zhou, G.; Dong, C.; Hu, Z.; Zhang, Y.; Luo, L.; Wu, C.; Zhao,
S.; He, F.: Characterization, chromosomal assignment, and tissue
expression of a novel human gene belonging to the ARF GAP family. Genomics 63:
400-408, 2000.
*FIELD* CD
Patricia A. Hartz: 11/24/2008
*FIELD* ED
mgross: 11/24/2008
*RECORD*
*FIELD* NO
612439
*FIELD* TI
*612439 ADP-RIBOSYLATION FACTOR GTPase-ACTIVATING PROTEIN 3; ARFGAP3
*FIELD* TX
DESCRIPTION
read more
ADP ribosylation factors (ARFs) are critical in intracellular vesicular
trafficking. GTP hydrolysis by ARFs requires interaction with
GTPase-activating proteins, such as ARFGAP3 (Zhang et al., 2000).
CLONING
By large-scale sequencing of clones obtained from a fetal liver cDNA
library, followed by database analysis and 5-prime RACE, Zhang et al.
(2000) cloned ARFGAP3, which they called ARFGAP1. The deduced 516-amino
acid protein has a calculated molecular mass of 57 kD and is 28%
identical to rat Arfgap1 (608377). ARFGAP3 has an N-terminal GATA1
(305371)-type zinc finger motif containing 4 cysteines that is highly
conserved among ARFGAPs, as well as multiple potential phosphorylation
sites. Northern blot analysis detected a 2.7-kb transcript in all fetal
tissues and cancer cell lines examined. RNA dot blot analysis revealed
variable ARFGAP3 expression in all adult and fetal tissues examined.
Highest expression was in testis and endocrine tissues, including
pancreas, adrenal gland, pituitary, salivary gland, and prostate.
Liu et al. (2001) found that fluorescence-tagged ARFGAP3 concentrated in
the perinuclear region of transfected COS-7 cells.
GENE FUNCTION
Using purified recombinant proteins, Liu et al. (2001) demonstrated that
ARFGAP3 stimulated ARF1 (103180)-mediated GTP hydrolysis in a
concentration-dependent manner. Phosphatidylinositol 4,5-bisphosphate
acted as an ARFGAP3 agonist, and phosphatidylcholine acted as an ARFGAP3
antagonist. Overexpression of ARFGAP3 in COS-7 cells reduced
constitutive secretion of secreted alkaline phosphatase (SEAP; 171800),
indicating that ARFGAP3 regulates the early secretory pathway of
proteins.
Using rat, monkey, and human cell lines, Frigerio et al. (2007) showed
that ARFGAP2 (606908) and ARFGAP3 functioned in intracellular
trafficking of COPI (601924)-coated vesicles. Both ARFGAP2 and ARFGAP3
colocalized with COPI subunits in the Golgi complex and peripheral
punctate structures and associated with COPI-coated vesicles generated
from Golgi membranes. Silencing of ARFGAP1 or a combination of ARFGAP2
and ARFGAP3 in HeLa cells did not decrease cell viability, but silencing
of all 3 ARFGAPs caused cell death.
GENE STRUCTURE
Zhang et al. (2000) determined that the ARFGAP3 gene contains 16 exons
and spans about 60 kb. The upstream region is 73.87% GC and includes 2
potential SP1 (189906)-binding sites. It has no CAAT or TATA box
elements.
MAPPING
By radiation hybrid and genomic sequence analyses, Zhang et al. (2000)
mapped the ARFGAP3 gene to chromosome 22q13.2.
*FIELD* RF
1. Frigerio, G.; Grimsey, N.; Dale, M.; Majoul, I.; Duden, R.: Two
human ARFGAPs associated with COP-I-coated vesicles. Traffic 8:
1644-1655, 2007.
2. Liu, X.; Zhang, C.; Xing, G.; Chen, Q.; He, F.: Functional characterization
of novel human ARFGAP3. FEBS Lett. 490: 79-83, 2001.
3. Zhang, C.; Yu, Y.; Zhang, S.; Liu, M.; Xing, G.; Wei, H.; Bi, J.;
Liu, X.; Zhou, G.; Dong, C.; Hu, Z.; Zhang, Y.; Luo, L.; Wu, C.; Zhao,
S.; He, F.: Characterization, chromosomal assignment, and tissue
expression of a novel human gene belonging to the ARF GAP family. Genomics 63:
400-408, 2000.
*FIELD* CD
Patricia A. Hartz: 11/24/2008
*FIELD* ED
mgross: 11/24/2008