RGAP2_ARATH
ID RGAP2_ARATH Reviewed; 430 AA.
AC F4JI46; Q9ZNR7;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Rho GTPase-activating protein 2;
DE AltName: Full=Rho-type GTPase-activating protein 2;
GN Name=ROPGAP2; OrderedLocusNames=At4g03100; ORFNames=F4C21.2, T4I9.2;
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=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 [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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP SUBUNIT, AND MUTAGENESIS OF HIS-88; HIS-91 AND ARG-165.
RX PubMed=21294109; DOI=10.1002/bip.21601;
RA Schaefer A., Hoehner K., Berken A., Wittinghofer A.;
RT "The unique plant RhoGAPs are dimeric and contain a CRIB motif required for
RT affinity and specificity towards cognate small G proteins.";
RL Biopolymers 95:420-433(2011).
CC -!- FUNCTION: Acts as a GTPase activator for the Rac-type GTPase by
CC converting it to an inactive GDP-bound state. {ECO:0000250}.
CC -!- SUBUNIT: Homodimerizes via its Rho-GAP domain and forms a tetrameric
CC complex (2:2) with ARAC1/ROP3, ARAC2/ROP7, ARAC4/ROP2, ARAC5/ROP4,
CC ARAC7/ROP9 or ARAC11/ROP1. {ECO:0000269|PubMed:21294109}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79102.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD14438.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB77795.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005275; AAD14438.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF069442; AAC79102.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161496; CAB77795.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE82271.1; -; Genomic_DNA.
DR EMBL; BX826644; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T01383; T01383.
DR RefSeq; NP_192219.2; NM_116544.4.
DR AlphaFoldDB; F4JI46; -.
DR SMR; F4JI46; -.
DR BioGRID; 13383; 1.
DR STRING; 3702.AT4G03100.1; -.
DR iPTMnet; F4JI46; -.
DR PaxDb; F4JI46; -.
DR PRIDE; F4JI46; -.
DR ProteomicsDB; 236167; -.
DR EnsemblPlants; AT4G03100.1; AT4G03100.1; AT4G03100.
DR GeneID; 828092; -.
DR Gramene; AT4G03100.1; AT4G03100.1; AT4G03100.
DR KEGG; ath:AT4G03100; -.
DR Araport; AT4G03100; -.
DR TAIR; locus:2139330; AT4G03100.
DR eggNOG; KOG4270; Eukaryota.
DR HOGENOM; CLU_031591_0_1_1; -.
DR InParanoid; F4JI46; -.
DR OMA; DMDRSCE; -.
DR OrthoDB; 1093913at2759; -.
DR PRO; PR:F4JI46; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JI46; baseline and differential.
DR Genevisible; F4JI46; AT.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR044785; RopGAP1-5.
DR PANTHER; PTHR23177; PTHR23177; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Reference proteome.
FT CHAIN 1..430
FT /note="Rho GTPase-activating protein 2"
FT /id="PRO_0000422717"
FT DOMAIN 80..93
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 125..310
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 88
FT /note="H->A: Reduces binding affinity with ARAC3/ROP7 10-
FT fold."
FT /evidence="ECO:0000269|PubMed:21294109"
FT MUTAGEN 91
FT /note="H->A: Reduces binding affinity with ARAC3/ROP7 10-
FT fold."
FT /evidence="ECO:0000269|PubMed:21294109"
FT MUTAGEN 165
FT /note="R->A: No effect on homodimerization and complex
FT formation."
FT /evidence="ECO:0000269|PubMed:21294109"
FT CONFLICT 120..122
FT /note="VSV -> FSF (in Ref. 3; BX826644)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="S -> R (in Ref. 3; BX826644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47299 MW; 870152C85E46FB97 CRC64;
MTGLVMMTKG GGCGGGGKGG RRKSTAEEEE EEEQNQQQLS LVEFLLTALR KSVVSCRVDN
RQDDGGVGGG ISSAVHHMEI GWPTNVRHIT HVTFDRFHGF LGLPHELQVE IPCRVPSASV
SVFGVSAESM QCSYDEKGNS VPTILLLMQE RLYSQQGLKA EGIFRINPEN SQEEHVRDQL
NRGIVPENID VHCLAGLIKA WFRELPSGVL DGLSPEEVLN CNTEDESVEL IKQLKPTESA
LLNWAVDLMA DVVEEEESNK MNARNIAMVF APNMTQMTDP LTALMHAVQV MNLLKTLITK
TLAEREENAT GSEGYSPSHS SNSQTDSDSD NAQDMEVSCE SQATDSECGE EEEVEEVEQH
QEHLSRHSTH EDETDIGSLC SIEKCFLNQL NNNAARVSNT SISEDWSPKA FPLVSFTENK
SNTLSSSTSD
