AGD11_ARATH
ID AGD11_ARATH Reviewed; 385 AA.
AC Q8L7A4; Q9SFC0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable ADP-ribosylation factor GTPase-activating protein AGD11;
DE Short=ARF GAP AGD11;
DE AltName: Full=Protein ARF-GAP DOMAIN 11;
DE Short=AtAGD11;
GN Name=AGD11; OrderedLocusNames=At3g07940; ORFNames=F17A17.28;
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 [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 [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor
CC (ARF). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF21204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013483; AAF21204.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74623.1; -; Genomic_DNA.
DR EMBL; AY136381; AAM97047.1; -; mRNA.
DR EMBL; BT002109; AAN72120.1; -; mRNA.
DR RefSeq; NP_187451.2; NM_111673.5.
DR AlphaFoldDB; Q8L7A4; -.
DR SMR; Q8L7A4; -.
DR STRING; 3702.AT3G07940.1; -.
DR iPTMnet; Q8L7A4; -.
DR PaxDb; Q8L7A4; -.
DR PRIDE; Q8L7A4; -.
DR ProteomicsDB; 244857; -.
DR EnsemblPlants; AT3G07940.1; AT3G07940.1; AT3G07940.
DR GeneID; 819985; -.
DR Gramene; AT3G07940.1; AT3G07940.1; AT3G07940.
DR KEGG; ath:AT3G07940; -.
DR Araport; AT3G07940; -.
DR TAIR; locus:2077367; AT3G07940.
DR eggNOG; KOG0703; Eukaryota.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_045472_0_0_1; -.
DR InParanoid; Q8L7A4; -.
DR OMA; ICTQCAG; -.
DR OrthoDB; 722176at2759; -.
DR PhylomeDB; Q8L7A4; -.
DR PRO; PR:Q8L7A4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L7A4; baseline and differential.
DR Genevisible; Q8L7A4; AT.
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:0005543; F:phospholipid binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW Calcium; GTPase activation; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..385
FT /note="Probable ADP-ribosylation factor GTPase-activating
FT protein AGD11"
FT /id="PRO_0000352502"
FT DOMAIN 47..169
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 212..326
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 62..85
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 197..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 385 AA; 42912 MW; A75E89C2A49B0880 CRC64;
MSLGQENVDP VEVSGSHACL YELLCSETPK WTPLRVEDLQ TSSSDPRDRL EKLLKQPGNK
YCADCGSPEP KWVSLSLGVF ICIKCSGVHR SLGVHISKVL SVKLDEWTDD QVDMLVGYGG
NTAVNERFEA CNIDQSKKPK PDSTNEERND FIRKKYEQHQ FMDPKDGALC TYQQPSRTNT
SPPSLCSASH RSTKNRIGHA FRNSWGRRES DHKGPKKSNS MAGMVEFVGL IKVNVVKGTN
LAVRDVMTSD PYVILALGQQ SVKTRVIKNN LNPVWNETLM LSIPEPMPPL KVLVYDKDTF
STDDFMGEAE IDIQPLVSAA KAYETSSIKE PMQLGSWVAS KENTLVSDGI ILLEDGKVKQ
DISLRLQNVE RGVLEIQLEC LPLTQ
