AGD7_ARATH
ID AGD7_ARATH Reviewed; 456 AA.
AC O80925;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein AGD7;
DE Short=ARF GAP AGD7;
DE AltName: Full=Protein ARF-GAP DOMAIN 7;
DE Short=AtAGD7;
DE AltName: Full=Protein PDE1 SUPPRESSOR 1;
GN Name=AGD7; Synonyms=ASP1; OrderedLocusNames=At2g37550; ORFNames=F13M22.5;
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], AND TISSUE SPECIFICITY.
RX PubMed=11572485; DOI=10.1093/dnares/8.4.189;
RA Oshitani-Okamoto S., Kuromori T., Goto M., Yamamoto M.;
RT "Arabidopsis cDNA clones isolated by transcomplementation of the fission
RT yeast cAMP phosphodiesterase mutant.";
RL DNA Res. 8:189-192(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, INTERACTION WITH ARF1, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17307897; DOI=10.1104/pp.106.095091;
RA Min M.K., Kim S.J., Miao Y., Shin J., Jiang L., Hwang I.;
RT "Overexpression of Arabidopsis AGD7 causes relocation of Golgi-localized
RT proteins to the endoplasmic reticulum and inhibits protein trafficking in
RT plant cells.";
RL Plant Physiol. 143:1601-1614(2007).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, 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 [8]
RP IDENTIFICATION BY 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). Involved in protein trafficking by controlling ARF1 activity;
CC may participate in COPI vesicle formation at the Golgi complex.
CC {ECO:0000269|PubMed:17307897}.
CC -!- ACTIVITY REGULATION: Activated by binding to phosphatidic acid.
CC {ECO:0000269|PubMed:17307897}.
CC -!- SUBUNIT: Interacts with ARF1. {ECO:0000269|PubMed:17307897}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17307897}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flower buds and
CC flowers. {ECO:0000269|PubMed:11572485}.
CC -!- MISCELLANEOUS: Plants overexpressing AGD7 show a relocation of proteins
CC from the Golgi complex to the endoplasmic reticulum.
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DR EMBL; AB017876; BAA75744.1; -; mRNA.
DR EMBL; AC004684; AAC23626.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09414.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09415.1; -; Genomic_DNA.
DR EMBL; AY034983; AAK59488.1; -; mRNA.
DR EMBL; AF436828; AAL32010.1; -; mRNA.
DR EMBL; AY063077; AAL34251.1; -; mRNA.
DR EMBL; AY103310; AAM65362.1; -; mRNA.
DR PIR; T02521; T02521.
DR RefSeq; NP_001031503.1; NM_001036426.1.
DR RefSeq; NP_181291.1; NM_129310.3.
DR AlphaFoldDB; O80925; -.
DR SMR; O80925; -.
DR BioGRID; 3675; 1.
DR STRING; 3702.AT2G37550.1; -.
DR iPTMnet; O80925; -.
DR MetOSite; O80925; -.
DR PaxDb; O80925; -.
DR PRIDE; O80925; -.
DR ProteomicsDB; 244879; -.
DR EnsemblPlants; AT2G37550.1; AT2G37550.1; AT2G37550.
DR EnsemblPlants; AT2G37550.2; AT2G37550.2; AT2G37550.
DR GeneID; 818331; -.
DR Gramene; AT2G37550.1; AT2G37550.1; AT2G37550.
DR Gramene; AT2G37550.2; AT2G37550.2; AT2G37550.
DR KEGG; ath:AT2G37550; -.
DR Araport; AT2G37550; -.
DR TAIR; locus:2040691; AT2G37550.
DR eggNOG; KOG0704; Eukaryota.
DR HOGENOM; CLU_044516_1_0_1; -.
DR InParanoid; O80925; -.
DR OMA; GGWAGWD; -.
DR OrthoDB; 1155557at2759; -.
DR PhylomeDB; O80925; -.
DR PRO; PR:O80925; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80925; baseline and differential.
DR Genevisible; O80925; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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 ER-Golgi transport; Golgi apparatus; GTPase activation; Metal-binding;
KW Phosphoprotein; Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..456
FT /note="ADP-ribosylation factor GTPase-activating protein
FT AGD7"
FT /id="PRO_0000352499"
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 122..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M354"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
SQ SEQUENCE 456 AA; 49252 MW; CCAE49B17B7B7CC6 CRC64;
MAAARRLRTL QSQPENKVCV DCSQKNPQWA SISYGIFMCL ECSGKHRGLG VHISFVRSVT
MDSWSEIQIK KMDAGGNERL NNFLAQYGIS KETDIISKYN SNAASVYRDR IQALAEGRQW
RDPPIVKESV GGGLMNKKPP LSQGGGRDSG NGGWDNWDND DSFRSTDMRR NQSAGDFRSS
GGRGAPAKSK SSEDIYSRSQ LEASAANKES FFAKRMAENE SKPEGLPPSQ GGKYVGFGSS
PGPAPRSNQQ SGGGDVFSVM SEGFGRLSLV AASAANVVQT GTMEFTSKVK EGGLDQTVSE
TVNVVASKTT EIGQRTWGIM KGVMAIASQK VEEFTKEEAS TWNQQNKTEG NGYYQNSGIG
NKTANSSFGG SQSSSSGHNN SYRNSNSWDD WGEENNSKKE AAPKVSTSND DDDGGWAGWD
DNDAKDDDFY YQPASDKKSV GHNGKSDTAW TGGGFL
