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Protein

ADP-ribosylation factor GTPase-activating protein AGD12

Gene

AGD12

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein (GAP) for ADP ribosylation factor (ARF). Binds phosphatidylinositol 3-monophosohate (PI-3-P) and anionic phospholipids.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri30 – 5324C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • GTPase activator activity Source: TAIR
  • metal ion binding Source: UniProtKB-KW
  • phospholipid binding Source: TAIR

GO - Biological processi

  • intracellular protein transport Source: TAIR
  • positive regulation of GTPase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor GTPase-activating protein AGD12
Short name:
ARF GAP AGD12
Alternative name(s):
Protein ARF-GAP DOMAIN 12
Short name:
AtAGD12
Zinc- and calcium-binding protein
Short name:
AtZAC
Gene namesi
Name:AGD12
Synonyms:ZAC
Ordered Locus Names:At4g21160
ORF Names:F7J7.100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G21160.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: TAIR
  • plasma membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331C → S: Loss of zinc and PI-3-P binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337ADP-ribosylation factor GTPase-activating protein AGD12PRO_0000352503Add
BLAST

Proteomic databases

PaxDbiQ9FVJ3.
PRIDEiQ9FVJ3.

PTM databases

iPTMnetiQ9FVJ3.

Expressioni

Tissue specificityi

Expressed in roots, leaves, flowers and siliques. Low levels of expression in seeds and stems.1 Publication

Gene expression databases

GenevisibleiQ9FVJ3. AT.

Interactioni

Protein-protein interaction databases

BioGridi13155. 1 interaction.
IntActiQ9FVJ3. 1 interaction.
STRINGi3702.AT4G21160.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FVJ3.
SMRiQ9FVJ3. Positions 18-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 137123Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini168 – 26295C2PROSITE-ProRule annotationAdd
BLAST

Domaini

The C2 domain binds anionic phospholipids promiscuously in the presence of calcium while the N-terminal region (1-174) show a specific affinity for phosphatidylinositol 3-monophosohate.

Sequence similaritiesi

Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
Contains 1 C2 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri30 – 5324C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0703. Eukaryota.
KOG1030. Eukaryota.
COG5347. LUCA.
HOGENOMiHOG000238659.
InParanoidiQ9FVJ3.
KOiK12486.
OMAiSEGMVEF.
PhylomeDBiQ9FVJ3.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR001164. ArfGAP.
IPR000008. C2_dom.
[Graphical view]
PfamiPF01412. ArfGap. 1 hit.
PF00168. C2. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00105. ArfGap. 1 hit.
SM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50115. ARFGAP. 1 hit.
PS50004. C2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FVJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYSGAGLGK PGSGKRRIRD LLTQSDNRVC ADCGAPDPKW ASANIGVFIC
60 70 80 90 100
LKCCGVHRSL GSHISKVLSV TLDEWSDEEV DSMIEIGGNA SANSIYEAFI
110 120 130 140 150
PEGSSKPGPD ASHDQRMRFI RSKYEHQEFL KPSLRITSVR GSSTKTPAFL
160 170 180 190 200
SSSLSKKIVD SFRTNSSSQQ PQLEGMVEFI GLLKVTIKKG TNMAIRDMMS
210 220 230 240 250
SDPYVVLTLG QQKAQSTVVK SNLNPVWNEE LMLSVPHNYG SVKLQVFDYD
260 270 280 290 300
TFSADDIMGE AEIDIQPLIT SAMAFGDPEM FGDMQIGKWL KSHDNALIED
310 320 330
SIINIADGKV KQEVQIKLQN VESGELELEM EWLPLEQ
Length:337
Mass (Da):37,145
Last modified:March 1, 2001 - v1
Checksum:iA2E56C4F66FE9FE1
GO

Sequence cautioni

The sequence CAA17535.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79116.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411G → V in AAM65970 (Ref. 5) Curated
Sequence conflicti214 – 2141A → V in BAF01268 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177381 mRNA. Translation: AAG09280.1.
AL021960 Genomic DNA. Translation: CAA17535.1. Sequence problems.
AL161554 Genomic DNA. Translation: CAB79116.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84411.1.
CP002687 Genomic DNA. Translation: AEE84412.1.
CP002687 Genomic DNA. Translation: AEE84413.1.
CP002687 Genomic DNA. Translation: AEE84414.1.
AY062549 mRNA. Translation: AAL32627.1.
BT008822 mRNA. Translation: AAP68261.1.
AY088434 mRNA. Translation: AAM65970.1.
AK229406 mRNA. Translation: BAF01268.1.
PIRiT04947.
RefSeqiNP_567620.1. NM_118235.3.
NP_849416.1. NM_179085.2.
NP_974581.1. NM_202852.2.
NP_974582.1. NM_202853.2.
UniGeneiAt.75195.

Genome annotation databases

EnsemblPlantsiAT4G21160.1; AT4G21160.1; AT4G21160.
AT4G21160.2; AT4G21160.2; AT4G21160.
AT4G21160.3; AT4G21160.3; AT4G21160.
AT4G21160.4; AT4G21160.4; AT4G21160.
GeneIDi827864.
GrameneiAT4G21160.1; AT4G21160.1; AT4G21160.
AT4G21160.2; AT4G21160.2; AT4G21160.
AT4G21160.3; AT4G21160.3; AT4G21160.
AT4G21160.4; AT4G21160.4; AT4G21160.
KEGGiath:AT4G21160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177381 mRNA. Translation: AAG09280.1.
AL021960 Genomic DNA. Translation: CAA17535.1. Sequence problems.
AL161554 Genomic DNA. Translation: CAB79116.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84411.1.
CP002687 Genomic DNA. Translation: AEE84412.1.
CP002687 Genomic DNA. Translation: AEE84413.1.
CP002687 Genomic DNA. Translation: AEE84414.1.
AY062549 mRNA. Translation: AAL32627.1.
BT008822 mRNA. Translation: AAP68261.1.
AY088434 mRNA. Translation: AAM65970.1.
AK229406 mRNA. Translation: BAF01268.1.
PIRiT04947.
RefSeqiNP_567620.1. NM_118235.3.
NP_849416.1. NM_179085.2.
NP_974581.1. NM_202852.2.
NP_974582.1. NM_202853.2.
UniGeneiAt.75195.

3D structure databases

ProteinModelPortaliQ9FVJ3.
SMRiQ9FVJ3. Positions 18-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13155. 1 interaction.
IntActiQ9FVJ3. 1 interaction.
STRINGi3702.AT4G21160.1.

PTM databases

iPTMnetiQ9FVJ3.

Proteomic databases

PaxDbiQ9FVJ3.
PRIDEiQ9FVJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G21160.1; AT4G21160.1; AT4G21160.
AT4G21160.2; AT4G21160.2; AT4G21160.
AT4G21160.3; AT4G21160.3; AT4G21160.
AT4G21160.4; AT4G21160.4; AT4G21160.
GeneIDi827864.
GrameneiAT4G21160.1; AT4G21160.1; AT4G21160.
AT4G21160.2; AT4G21160.2; AT4G21160.
AT4G21160.3; AT4G21160.3; AT4G21160.
AT4G21160.4; AT4G21160.4; AT4G21160.
KEGGiath:AT4G21160.

Organism-specific databases

TAIRiAT4G21160.

Phylogenomic databases

eggNOGiKOG0703. Eukaryota.
KOG1030. Eukaryota.
COG5347. LUCA.
HOGENOMiHOG000238659.
InParanoidiQ9FVJ3.
KOiK12486.
OMAiSEGMVEF.
PhylomeDBiQ9FVJ3.

Miscellaneous databases

PROiQ9FVJ3.

Gene expression databases

GenevisibleiQ9FVJ3. AT.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR001164. ArfGAP.
IPR000008. C2_dom.
[Graphical view]
PfamiPF01412. ArfGap. 1 hit.
PF00168. C2. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00105. ArfGap. 1 hit.
SM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50115. ARFGAP. 1 hit.
PS50004. C2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Promiscuous and specific phospholipid binding by domains in ZAC, a membrane-associated Arabidopsis protein with an ARF GAP zinc finger and a C2 domain."
    Jensen R.B., Lykke-Andersen K., Frandsen G.I., Nielsen H.B., Haseloff J., Jespersen H.M., Mundy J., Skriver K.
    Plant Mol. Biol. 44:799-814(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-33, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    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.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Analysis of the small GTPase gene superfamily of Arabidopsis."
    Vernoud V., Horton A.C., Yang Z., Nielsen E.
    Plant Physiol. 131:1191-1208(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  8. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAGD12_ARATH
AccessioniPrimary (citable) accession number: Q9FVJ3
Secondary accession number(s): O49557, Q0WNN1, Q8L9H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: March 1, 2001
Last modified: February 17, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.