GAP22_ARATH
ID GAP22_ARATH Reviewed; 550 AA.
AC Q94BY9; Q56WX5; Q9FJC7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Rab GTPase-activating protein 22 {ECO:0000303|PubMed:16332933};
GN Name=RABGAP22 {ECO:0000303|PubMed:16332933};
GN OrderedLocusNames=At5g53570 {ECO:0000312|Araport:AT5G53570};
GN ORFNames=MNC6.11 {ECO:0000312|EMBL:BAB09733.1};
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 {ECO:0000312|EMBL:AAK62601.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 237-550.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16332933; DOI=10.1152/physiolgenomics.00210.2005;
RA Jiang S.Y., Ramachandran S.;
RT "Comparative and evolutionary analysis of genes encoding small GTPases and
RT their activating proteins in eukaryotic genomes.";
RL Physiol. Genomics 24:235-251(2006).
RN [6]
RP FUNCTION, INTERACTION WITH AGT1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24505423; DOI=10.1371/journal.pone.0088187;
RA Roos J., Bejai S., Oide S., Dixelius C.;
RT "RabGAP22 is required for defense to the vascular pathogen Verticillium
RT longisporum and contributes to stomata immunity.";
RL PLoS ONE 9:E88187-E88187(2014).
CC -!- FUNCTION: Involved in defense response against fungal and bacterial
CC pathogens (PubMed:24505423). Acts as negative regulator of jasmonate
CC (JA) responses during infection by the soil-born fungal pathogen
CC Verticillium longisporum (PubMed:24505423). Involved in abscisic acid-
CC dependent stomata closure in response to infection by V. longisporum
CC and Pseudomonas syringae (PubMed:24505423). May be a downstream
CC component of brassinosteroid-mediated signaling (PubMed:24505423).
CC {ECO:0000269|PubMed:24505423}.
CC -!- SUBUNIT: Interacts with AGT1 in peroxisome under biotic stress
CC conditions. {ECO:0000269|PubMed:24505423}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24505423}. Peroxisome
CC {ECO:0000269|PubMed:24505423}. Note=Localizes to peroxisome under
CC biotic stress conditions. {ECO:0000269|PubMed:24505423}.
CC -!- TISSUE SPECIFICITY: Expressed in root meristems, vascular tissues,
CC guard cells, trichomes, styles and receptacles.
CC {ECO:0000269|PubMed:24505423}.
CC -!- INDUCTION: Induced by infection with the soil-born fungal pathogen
CC Verticillium longisporum. {ECO:0000269|PubMed:24505423}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit increased susceptibility to the
CC soil-born fungal pathogen Verticillium longisporum.
CC {ECO:0000269|PubMed:24505423}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09733.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB015476; BAB09733.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96378.1; -; Genomic_DNA.
DR EMBL; AY039546; AAK62601.1; -; mRNA.
DR EMBL; AY102156; AAM26723.1; -; mRNA.
DR EMBL; AK221904; BAD94281.1; -; mRNA.
DR RefSeq; NP_200169.1; NM_124737.3.
DR AlphaFoldDB; Q94BY9; -.
DR SMR; Q94BY9; -.
DR PRIDE; Q94BY9; -.
DR ProteomicsDB; 177131; -.
DR EnsemblPlants; AT5G53570.1; AT5G53570.1; AT5G53570.
DR GeneID; 835439; -.
DR Gramene; AT5G53570.1; AT5G53570.1; AT5G53570.
DR KEGG; ath:AT5G53570; -.
DR Araport; AT5G53570; -.
DR HOGENOM; CLU_004457_5_0_1; -.
DR PhylomeDB; Q94BY9; -.
DR PRO; PR:Q94BY9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BY9; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Nucleus; Peroxisome; Plant defense; Reference proteome.
FT CHAIN 1..550
FT /note="Rab GTPase-activating protein 22"
FT /id="PRO_0000449824"
FT DOMAIN 126..460
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 61916 MW; AB5631C2DD1F723F CRC64;
MKALRRSYTS TSSGNSSSSS SLPSSSSSSL PSSSSSSPPS SNSNSYSNSN SSSSSSSWIH
LRSVLFVANL SSPSSVTSSD RRRKSPWSRR KRKWALTPHQ WRSLFTPEGK LRDGGVGFLK
KVRSRGVDPS IRAEVWLFLL GVYDLNSTSE EREAVKTQKR KEYEKLQRRC QMLLKCGNGS
TDNLEELPSD EANSQCVRFV DDYKITGPMT SQDVVSALNT DSSDTDSCED NEDVLLLSSF
AHSDEKKPEE DNSNNNSEEN SSLLVAAASE VQVEVAVHED FSTWQRIIRL DALRADSEWA
NYSPYSTAIT ESKARRLAES VGLKDYDHLE SCRLYHAARL VAILEAYAMY DPEIGYCQGM
SDLLSPILAV ISEDHEAFWC FVGFMKKARH NFRLDEAGIQ RQLSIVSKII KNKDSQLYKH
LENLQAEDCS FVYRMVLVMF RRELSFEQTL CLWEVMWADQ AAIRAGVGKS PWSRIRQQAP
PTDDLLLYAI AALVLRRKLI IQKYSSMDEI VEECNSMAGQ LNVWKLLDDA HHLVVTLHDK
IETLSQSQSI
