AGD6_ARATH
ID AGD6_ARATH Reviewed; 459 AA.
AC Q9M354; Q9FVH2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Probable ADP-ribosylation factor GTPase-activating protein AGD6;
DE Short=ARF GAP AGD6;
DE AltName: Full=Protein ARF-GAP DOMAIN 6;
DE Short=AtAGD6;
DE AltName: Full=Protein ZIGA2;
GN Name=AGD6; Synonyms=ZIG2, ZIGA2; OrderedLocusNames=At3g53710;
GN ORFNames=F5K20.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11202441; DOI=10.1023/a:1026509002161;
RA Jensen R.B., Lykke-Andersen K., Frandsen G.I., Nielsen H.B., Haseloff J.,
RA Jespersen H.M., Mundy J., Skriver K.;
RT "Promiscuous and specific phospholipid binding by domains in ZAC, a
RT membrane-associated Arabidopsis protein with an ARF GAP zinc finger and a
RT C2 domain.";
RL Plant Mol. Biol. 44:799-814(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12644670; DOI=10.1104/pp.013052;
RA Vernoud V., Horton A.C., Yang Z., Nielsen E.;
RT "Analysis of the small GTPase gene superfamily of Arabidopsis.";
RL Plant Physiol. 131:1191-1208(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor
CC (ARF). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9M354; Q9LIC6: PRA1F3; NbExp=3; IntAct=EBI-21138098, EBI-2010961;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG17006.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF184146; AAG17006.1; ALT_FRAME; mRNA.
DR EMBL; AL132960; CAB88333.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79130.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79131.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64695.1; -; Genomic_DNA.
DR EMBL; BT030393; ABO45696.1; -; mRNA.
DR PIR; T45911; T45911.
DR RefSeq; NP_001030854.1; NM_001035777.2.
DR RefSeq; NP_001319740.1; NM_001339627.1.
DR RefSeq; NP_190939.1; NM_115231.4.
DR AlphaFoldDB; Q9M354; -.
DR SMR; Q9M354; -.
DR BioGRID; 9855; 2.
DR IntAct; Q9M354; 2.
DR STRING; 3702.AT3G53710.1; -.
DR iPTMnet; Q9M354; -.
DR PaxDb; Q9M354; -.
DR PRIDE; Q9M354; -.
DR ProteomicsDB; 244878; -.
DR EnsemblPlants; AT3G53710.1; AT3G53710.1; AT3G53710.
DR EnsemblPlants; AT3G53710.2; AT3G53710.2; AT3G53710.
DR EnsemblPlants; AT3G53710.3; AT3G53710.3; AT3G53710.
DR GeneID; 824538; -.
DR Gramene; AT3G53710.1; AT3G53710.1; AT3G53710.
DR Gramene; AT3G53710.2; AT3G53710.2; AT3G53710.
DR Gramene; AT3G53710.3; AT3G53710.3; AT3G53710.
DR KEGG; ath:AT3G53710; -.
DR Araport; AT3G53710; -.
DR TAIR; locus:2084360; AT3G53710.
DR eggNOG; KOG0704; Eukaryota.
DR HOGENOM; CLU_044516_1_0_1; -.
DR InParanoid; Q9M354; -.
DR OMA; AWDLLMN; -.
DR OrthoDB; 1155557at2759; -.
DR PhylomeDB; Q9M354; -.
DR PRO; PR:Q9M354; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M354; baseline and differential.
DR Genevisible; Q9M354; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR044519; ARF_GAP_AGD6/7.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR PANTHER; PTHR47021; PTHR47021; 1.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..459
FT /note="Probable ADP-ribosylation factor GTPase-activating
FT protein AGD6"
FT /id="PRO_0000352498"
FT DOMAIN 4..120
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 19..42
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 118..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 307
FT /note="T -> I (in Ref. 1; AAG17006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 49724 MW; A9C91A4AA56F3950 CRC64;
MAATRQLRTL QSQPENKVCV DCAQKNPQWA SVSYGIFMCL ECSGKHRGLG VHISFVRSVT
MDSWSAIQIK KMEAGGNERL NKFFAQYGIA KETDIISKYN SNAASVYRDR IQALAEGRPW
NDPPVVKEAN KKPPLAQGGY GNNNNNNNGG WDSWDNDDSY KSDMRRNQSA NDFRASGNRE
GAHVKSKSSE DIYTRSQLEA SAAGKESFFA RRMAENESKP EGLPPSQGGK YVGFGSSSAP
PPRNNQQDDV FSVVSQGFGR LSLVAASAAQ SAASVVQTGT KEFTSKVKEG GYDHKVSETV
NVVANKTTEI GHRTWGIMKG VMAMATQKVE EFTKEGSTSW NQQSENEGNG YYQNFGNGNK
AANSSVGGGR PQSSSTSGHY NNSQNSNSWD SWGENENKKT EAVAPKGSSA SNDDDGWTGW
DDHDAKDDGF DGHYQSAGDK KSAGHNGKSD TAWTGGGFL
