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ADP-ribosylation factor GTPase-activating protein AGD3 (ARF GAP AGD3) (Protein ARF-GAP DOMAIN 3) (AtAGD3) (Protein FORKED 2) (Protein SCARFACE) (Protein VASCULAR NETWORK 3)

 AGD3_ARATH              Reviewed;         827 AA.
Q5W7F2; Q0WNK6; Q9LYU6;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
02-JUN-2021, entry version 138.
RecName: Full=ADP-ribosylation factor GTPase-activating protein AGD3;
Short=ARF GAP AGD3;
AltName: Full=Protein ARF-GAP DOMAIN 3;
Short=AtAGD3;
AltName: Full=Protein FORKED 2 {ECO:0000303|PubMed:19363154, ECO:0000303|PubMed:19473324};
AltName: Full=Protein SCARFACE;
AltName: Full=Protein VASCULAR NETWORK 3 {ECO:0000303|PubMed:19363154};
Name=AGD3;
Synonyms=FKD2 {ECO:0000303|PubMed:19363154, ECO:0000303|PubMed:19473324},
SFC, VAN3 {ECO:0000303|PubMed:19363154};
OrderedLocusNames=At5g13300 {ECO:0000312|Araport:AT5G13300};
ORFNames=T31B5.120 {ECO:0000312|EMBL:CAB86637.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY AUXIN, SUBUNIT, SUBCELLULAR
LOCATION, AND FUNCTION.
STRAIN=cv. Landsberg erecta;
PubMed=15743878; DOI=10.1242/dev.01716;
Koizumi K., Naramoto S., Sawa S., Yahara N., Ueda T., Nakano A.,
Sugiyama M., Fukuda H.;
"VAN3 ARF-GAP-mediated vesicle transport is involved in leaf vascular
network formation.";
Development 132:1699-1711(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana reference
genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 419-827.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=10887076;
Koizumi K., Sugiyama M., Fukuda H.;
"A series of novel mutants of Arabidopsis thaliana that are defective in
the formation of continuous vascular network: calling the auxin signal flow
canalization hypothesis into question.";
Development 127:3197-3204(2000).
[6]
FUNCTION.
PubMed=10887077;
Deyholos M.K., Cordner G., Beebe D., Sieburth L.E.;
"The SCARFACE gene is required for cotyledon and leaf vein patterning.";
Development 127:3205-3213(2000).
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12644670; DOI=10.1104/pp.013052;
Vernoud V., Horton A.C., Yang Z., Nielsen E.;
"Analysis of the small GTPase gene superfamily of Arabidopsis.";
Plant Physiol. 131:1191-1208(2003).
[8]
INTERACTION WITH DRP1A.
PubMed=15923323; DOI=10.1104/pp.105.061689;
Sawa S., Koizumi K., Naramoto S., Demura T., Ueda T., Nakano A., Fukuda H.;
"DRP1A is responsible for vascular continuity synergistically working with
VAN3 in Arabidopsis.";
Plant Physiol. 138:819-826(2005).
[9]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-518 AND CYS-519.
PubMed=16698946; DOI=10.1105/tpc.105.039008;
Sieburth L.E., Muday G.K., King E.J., Benton G., Kim S., Metcalf K.E.,
Meyers L., Seamen E., Van Norman J.M.;
"SCARFACE encodes an ARF-GAP that is required for normal auxin efflux and
vein patterning in Arabidopsis.";
Plant Cell 18:1396-1411(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by mass
spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[11]
MUTAGENESIS OF GLY-321, SUBCELLULAR LOCATION, INTERACTION WITH VAB, AND
ACTIVITY REGULATION.
PubMed=19363154; DOI=10.1242/dev.030098;
Naramoto S., Sawa S., Koizumi K., Uemura T., Ueda T., Friml J., Nakano A.,
Fukuda H.;
"Phosphoinositide-dependent regulation of VAN3 ARF-GAP localization and
activity essential for vascular tissue continuity in plants.";
Development 136:1529-1538(2009).
[12]
MUTAGENESIS OF LEU-317 AND GLY-321, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND PH DOMAIN.
PubMed=19473324; DOI=10.1111/j.1365-313x.2009.03920.x;
Carland F., Nelson T.;
"CVP2- and CVL1-mediated phosphoinositide signaling as a regulator of the
ARF GAP SFC/VAN3 in establishment of foliar vein patterns.";
Plant J. 59:895-907(2009).
-!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor
(ARF). Involved in the spatial control of provascular differentiation.
Required for the formation of the normal pattern of continuous
secondary veins. Involved in auxin signaling but not in polar auxin
transport or in auxin responses. Required for PIN1 internalization in
roots. {ECO:0000269|PubMed:10887076, ECO:0000269|PubMed:10887077,
ECO:0000269|PubMed:15743878, ECO:0000269|PubMed:16698946}.
-!- ACTIVITY REGULATION: ARF GAP activity strongly enhanced by
phosphatidylinositol 4-monophosphate (PIP) and moderately enhanced by
phosphatidylinositol 4,5-bisphosphate (PIP2).
{ECO:0000269|PubMed:19363154}.
-!- SUBUNIT: Homodimer (PubMed:15743878). Interacts with DRP1A
(PubMed:15923323). Interacts with VAB (PubMed:19363154).
{ECO:0000269|PubMed:15743878, ECO:0000269|PubMed:15923323,
ECO:0000269|PubMed:19363154}.
-!- INTERACTION:
Q5W7F2; P42697: DRP1A; NbExp=4; IntAct=EBI-994222, EBI-994234;
Q5W7F2; Q8W4K5: VAB; NbExp=5; IntAct=EBI-994222, EBI-10769249;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
{ECO:0000269|PubMed:15743878, ECO:0000269|PubMed:19363154}. Note=BAR
and PH domains are essential for the proper localization. Localization
seems to be regulated by CVP2 and CVL1 activity as the
phosphatidylinositol 4-monophosphate (PIP)-binding by the PH domain is
required for the TGN localization. {ECO:0000269|PubMed:19363154}.
-!- TISSUE SPECIFICITY: Broadly expressed. Detected in developing veins of
the leaf and root (PubMed:19473324). Detected in roots, hypocotyls,
cotyledons, leaves, siliques and shoot apical meristems
(PubMed:16698946). {ECO:0000269|PubMed:16698946,
ECO:0000269|PubMed:19473324}.
-!- DEVELOPMENTAL STAGE: Expression refined to procambial cells during
embryogenesis. {ECO:0000269|PubMed:19473324}.
-!- INDUCTION: Up-regulated by auxin. {ECO:0000269|PubMed:15743878}.
-!- DOMAIN: The PH domain is responsive of the binding to phosphoinositol
(PubMed:19473324). The BAR domain is required and sufficient for
homodimerization (PubMed:15743878). {ECO:0000269|PubMed:15743878,
ECO:0000269|PubMed:19473324}.
-!- MISCELLANEOUS: Binds to phosphatidylinositol (PI), phosphatidylinositol
4-monophosphate (PIP) and phosphatidylinositol 4,5-bisphosphate (PIP2)
but not to phosphatidic acid (PA), phosphatidylcholine (PC) or
phosphatidylethanolamine (PE). {ECO:0000269|PubMed:15743878}.
-!- SEQUENCE CAUTION:
Sequence=CAB86637.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; AL163491; CAB86637.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED91878.1; -; Genomic_DNA.
EMBL; AB194395; BAD69588.1; -; mRNA.
EMBL; AK229433; BAF01293.1; -; mRNA.
PIR; T48577; T48577.
RefSeq; NP_196834.3; NM_121333.4.
BioGRID; 16449; 4.
IntAct; Q5W7F2; 3.
STRING; 3702.AT5G13300.1; -.
iPTMnet; Q5W7F2; -.
PaxDb; Q5W7F2; -.
PRIDE; Q5W7F2; -.
ProteomicsDB; 243286; -.
EnsemblPlants; AT5G13300.1; AT5G13300.1; AT5G13300.
GeneID; 831171; -.
Gramene; AT5G13300.1; AT5G13300.1; AT5G13300.
KEGG; ath:AT5G13300; -.
Araport; AT5G13300; -.
TAIR; locus:2183916; AT5G13300.
eggNOG; KOG0521; Eukaryota.
HOGENOM; CLU_016029_1_0_1; -.
InParanoid; Q5W7F2; -.
OMA; KAMQNRH; -.
OrthoDB; 751525at2759; -.
PhylomeDB; Q5W7F2; -.
PRO; PR:Q5W7F2; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q5W7F2; baseline and differential.
Genevisible; Q5W7F2; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:TAIR.
GO; GO:0006897; P:endocytosis; IMP:TAIR.
GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
CDD; cd07606; BAR_SFC_plant; 1.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 3.30.40.160; -; 1.
InterPro; IPR035670; AGD1/2/3/4_BAR_plant.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR037278; ARFGAP/RecO.
InterPro; IPR001164; ArfGAP_dom.
InterPro; IPR038508; ArfGAP_dom_sf.
InterPro; IPR004148; BAR_dom.
InterPro; IPR001849; PH_domain.
Pfam; PF01412; ArfGap; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00405; REVINTRACTNG.
SMART; SM00248; ANK; 3.
SMART; SM00105; ArfGap; 1.
SMART; SM00721; BAR; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57863; SSF57863; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
PROSITE; PS50115; ARFGAP; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
ANK repeat; Coiled coil; Developmental protein; Golgi apparatus;
GTPase activation; Metal-binding; Phosphoprotein; Reference proteome;
Repeat; Zinc; Zinc-finger.
CHAIN 1..827
/note="ADP-ribosylation factor GTPase-activating protein
AGD3"
/id="PRO_0000332940"
DOMAIN 1..225
/note="BAR"
DOMAIN 292..430
/note="PH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
DOMAIN 501..643
/note="Arf-GAP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
REPEAT 728..757
/note="ANK 1"
REPEAT 761..790
/note="ANK 2"
REPEAT 794..825
/note="ANK 3"
ZN_FING 516..539
/note="C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
REGION 246..269
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 439..467
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COILED 116..139
/evidence="ECO:0000255"
COILED 223..253
/evidence="ECO:0000255"
COMPBIAS 253..269
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 451..465
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 445
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18433157"
MUTAGEN 317
/note="L->F: In fkd2-2; vein pattern defects."
/evidence="ECO:0000269|PubMed:19473324"
MUTAGEN 321
/note="G->E: In van3-2 and fkd2-1; reduced ARF GAP
activity, mis-localization and vein pattern defects."
/evidence="ECO:0000269|PubMed:19363154,
ECO:0000269|PubMed:19473324"
MUTAGEN 518
/note="D->N: In scf-6; intermediate vein pattern defects."
/evidence="ECO:0000269|PubMed:16698946"
MUTAGEN 519
/note="C->Y: In scf-1; strong vein pattern defects."
/evidence="ECO:0000269|PubMed:16698946"
SEQUENCE 827 AA; 92524 MW; 59FF5BAA10584DD7 CRC64;
MHFTKLDDSP MFRKQLQSME ESAEILRERS LKFYKGCRKY TEGLGEAYDG DIAFASALET
FGGGHNDPIS VAFGGPVMTK FTIALREIGT YKEVLRSQVE HILNDRLLQF ANMDLHEVKE
ARKRFDKASL TYDQAREKFL SLRKGTKSDV AAALEQELHT SRSMFEQARF NLVTALSNVE
AKKRFEFLEA VSGTMDAHLR YFKQGYELLH QMEPYINQVL TYAQQSRERS NYEQAALNEK
MQEYKRQVDR ESRWGSNGSN GSPNGDGIQA IGRSSHKMID AVMQSAARGK VQTIRQGYLS
KRSSNLRGDW KRRFFVLDSR GMLYYYRKQC SKPSGSGSQL SGQRNSSELG SGLLSRWLSS
NNHGHGGVHD EKSVARHTVN LLTSTIKVDA DQSDLRFCFR IISPTKNYTL QAESALDQMD
WIEKITGVIA SLLSSQVPEQ RLPGSPMGSG HHRSASESSS YESSEYDHPT TEEFVCERSF
LGYNERPSRS FQPQRSIRKG EKPIDALRKV CGNDKCADCG APEPDWASLN LGVLVCIECS
GVHRNLGVHI SKVRSLTLDV KVWEPSVISL FQALGNTFAN TVWEELLHSR SAIHFDPGLT
VSDKSRVMVT GKPSYADMIS IKEKYIQAKY AEKLFVRRSR DSDFPQSAAQ QMWDAVSGND
KKAVYRLIVN GDADVNYVYD QTSSSSLTLS RVILVPERPK REDVLLRLRN ELLDRTGSSS
NISPEGSGGS SLLHCACEKA DLGMVELLLQ YGANVNASDS SGQTPLHCCL LRGKVTIARL
LLTRGADPEA MNREGKTALD IAAESNFTDP EVLALLSDTN GYNHRQC


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WP2324: AGE/RAGE pathway
WP1685: Peptidoglycan biosynthesis
WP2371: Parkinsons Disease Pathway
WP1616: ABC transporters
WP1644: DNA replication
WP2032: TSH signaling pathway
WP1692: Protein export
WP346: Protein Modifications
WP1700: Selenoamino acid metabolism
WP525: Mitochondrial Unfolded-Protein Response
WP1657: Glycerolipid metabolism
WP1663: Homologous recombination
WP2218: sGC
WP1438: Influenza A virus infection
WP731: Sterol regulatory element binding protein related
WP1502: Mitochondrial biogenesis
WP1888: Post-translational protein modification
WP813: G Protein Signaling Pathways
WP1673: Naphthalene and anthracene degradation

Related Genes :
[AGD3 FKD2 SFC VAN3 At5g13300 T31B5.120] ADP-ribosylation factor GTPase-activating protein AGD3 (ARF GAP AGD3) (Protein ARF-GAP DOMAIN 3) (AtAGD3) (Protein FORKED 2) (Protein SCARFACE) (Protein VASCULAR NETWORK 3)
[ASAP1 DDEF1 KIAA1249 PAG2] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[Asap1 Ddef1 Kiaa1249 Shag1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[Arfgap1 Arf1gap] ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)
[ARFGAP1 ARF1GAP] ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)
[Asap1 Ddef1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[AGD1 At5g61980 K22G18.9] ADP-ribosylation factor GTPase-activating protein AGD1 (ARF GAP AGD1) (Protein ARF-GAP DOMAIN 1) (AtAGD1)
[ASAP1 DDEF1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[Arfgap1 Arf1gap] ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)
[Git arfgap2 CG16728] ARF GTPase-activating protein Git (ARF GAP GIT) (dGIT protein) (G protein-coupled receptor kinase interacting ArfGAP)
[AGAP3 CENTG3] Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3 (AGAP-3) (CRAM-associated GTPase) (CRAG) (Centaurin-gamma-3) (Cnt-g3) (MR1-interacting protein) (MRIP-1)
[arf-1.2 arf-1 B0336.2] ADP-ribosylation factor 1-like 2 (ADP-ribosylation factor-related protein 1.2)
[ARFGEF1 ARFGEP1 BIG1] Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)
[GN EMB30 GBF3 MIZ2 VAN7 At1g13980 F16A14.20 F7A19.7] ARF guanine-nucleotide exchange factor GNOM (Pattern formation protein EMB30) (Protein EMBRYO DEFECTIVE 30) (Protein MIZU-KUSSEI2) (Protein VASCULAR NETWORK 7)
[ACAP1 CENTB1 KIAA0050] Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1)
[ARFGEF1 ARFGEP1 BIG1] Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)
[ARF1] ADP-ribosylation factor 1
[ARL2BP BART BART1] ADP-ribosylation factor-like protein 2-binding protein (ARF-like 2-binding protein) (ARL2-binding protein) (Binder of ARF2 protein 1)
[GGA1] ADP-ribosylation factor-binding protein GGA1 (Gamma-adaptin-related protein 1) (Golgi-localized, gamma ear-containing, ARF-binding protein 1)
[ARF4 ARF2] ADP-ribosylation factor 4
[ARL3 ARFL3] ADP-ribosylation factor-like protein 3
[Arl3] ADP-ribosylation factor-like protein 3 (ARD3)
[Arl3] ADP-ribosylation factor-like protein 3
[ARL4C ARL7] ADP-ribosylation factor-like protein 4C (ADP-ribosylation factor-like protein 7) (ADP-ribosylation factor-like protein LAK)
[Arf4] ADP-ribosylation factor 4
[G3bp1 G3bp] Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (GAP SH3 domain-binding protein 1) (HDH-VIII)
[Arf4] ADP-ribosylation factor 4
[G3BP1 G3BP] Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (hDH VIII) (GAP SH3 domain-binding protein 1)
[AGFG1 HRB RAB RIP] Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein) (Nucleoporin-like protein RIP) (Rev-interacting protein) (Rev/Rex activation domain-binding protein)
[Agfg1 Hrb Rip] Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein homolog) (Nucleoporin-like protein RIP)

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