AGD12_ARATH
ID AGD12_ARATH Reviewed; 337 AA.
AC Q9FVJ3; O49557; Q0WNN1; Q8L9H2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein AGD12;
DE Short=ARF GAP AGD12;
DE AltName: Full=Protein ARF-GAP DOMAIN 12;
DE Short=AtAGD12;
DE AltName: Full=Zinc- and calcium-binding protein;
DE Short=AtZAC;
GN Name=AGD12; Synonyms=ZAC; OrderedLocusNames=At4g21160; ORFNames=F7J7.100;
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], MUTAGENESIS OF CYS-33, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [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). Binds phosphatidylinositol 3-monophosohate (PI-3-P) and anionic
CC phospholipids.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11202441}.
CC Cell membrane {ECO:0000269|PubMed:11202441}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC Low levels of expression in seeds and stems.
CC {ECO:0000269|PubMed:11202441}.
CC -!- DOMAIN: The C2 domain binds anionic phospholipids promiscuously in the
CC presence of calcium while the N-terminal region (1-174) show a specific
CC affinity for phosphatidylinositol 3-monophosohate.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17535.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79116.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF177381; AAG09280.1; -; mRNA.
DR EMBL; AL021960; CAA17535.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79116.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84411.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84412.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84413.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84414.1; -; Genomic_DNA.
DR EMBL; AY062549; AAL32627.1; -; mRNA.
DR EMBL; BT008822; AAP68261.1; -; mRNA.
DR EMBL; AY088434; AAM65970.1; -; mRNA.
DR EMBL; AK229406; BAF01268.1; -; mRNA.
DR PIR; T04947; T04947.
DR RefSeq; NP_567620.1; NM_118235.4.
DR RefSeq; NP_849416.1; NM_179085.3.
DR RefSeq; NP_974581.1; NM_202852.2.
DR RefSeq; NP_974582.1; NM_202853.3.
DR AlphaFoldDB; Q9FVJ3; -.
DR SMR; Q9FVJ3; -.
DR BioGRID; 13155; 1.
DR IntAct; Q9FVJ3; 1.
DR STRING; 3702.AT4G21160.3; -.
DR iPTMnet; Q9FVJ3; -.
DR PaxDb; Q9FVJ3; -.
DR PRIDE; Q9FVJ3; -.
DR ProteomicsDB; 244695; -.
DR EnsemblPlants; AT4G21160.1; AT4G21160.1; AT4G21160.
DR EnsemblPlants; AT4G21160.2; AT4G21160.2; AT4G21160.
DR EnsemblPlants; AT4G21160.3; AT4G21160.3; AT4G21160.
DR EnsemblPlants; AT4G21160.4; AT4G21160.4; AT4G21160.
DR GeneID; 827864; -.
DR Gramene; AT4G21160.1; AT4G21160.1; AT4G21160.
DR Gramene; AT4G21160.2; AT4G21160.2; AT4G21160.
DR Gramene; AT4G21160.3; AT4G21160.3; AT4G21160.
DR Gramene; AT4G21160.4; AT4G21160.4; AT4G21160.
DR KEGG; ath:AT4G21160; -.
DR Araport; AT4G21160; -.
DR TAIR; locus:2127338; AT4G21160.
DR eggNOG; KOG0703; Eukaryota.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_045472_0_1_1; -.
DR InParanoid; Q9FVJ3; -.
DR OMA; DSFRIKP; -.
DR OrthoDB; 987311at2759; -.
DR PhylomeDB; Q9FVJ3; -.
DR PRO; PR:Q9FVJ3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FVJ3; baseline and differential.
DR Genevisible; Q9FVJ3; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005096; F:GTPase activator activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IDA:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; TAS:TAIR.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR044518; ARF_GAP_AGD11/12/13.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR PANTHER; PTHR46220; PTHR46220; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00168; C2; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Golgi apparatus; GTPase activation; Membrane;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..337
FT /note="ADP-ribosylation factor GTPase-activating protein
FT AGD12"
FT /id="PRO_0000352503"
FT DOMAIN 15..137
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 164..281
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 30..53
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MUTAGEN 33
FT /note="C->S: Loss of zinc and PI-3-P binding."
FT /evidence="ECO:0000269|PubMed:11202441"
FT CONFLICT 141
FT /note="G -> V (in Ref. 5; AAM65970)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="A -> V (in Ref. 6; BAF01268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37145 MW; A2E56C4F66FE9FE1 CRC64;
MSYSGAGLGK PGSGKRRIRD LLTQSDNRVC ADCGAPDPKW ASANIGVFIC LKCCGVHRSL
GSHISKVLSV TLDEWSDEEV DSMIEIGGNA SANSIYEAFI PEGSSKPGPD ASHDQRMRFI
RSKYEHQEFL KPSLRITSVR GSSTKTPAFL SSSLSKKIVD SFRTNSSSQQ PQLEGMVEFI
GLLKVTIKKG TNMAIRDMMS SDPYVVLTLG QQKAQSTVVK SNLNPVWNEE LMLSVPHNYG
SVKLQVFDYD TFSADDIMGE AEIDIQPLIT SAMAFGDPEM FGDMQIGKWL KSHDNALIED
SIINIADGKV KQEVQIKLQN VESGELELEM EWLPLEQ
