RAC2A_ARATH
ID RAC2A_ARATH Reviewed; 210 AA.
AC O49841;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ras-related protein RABC2a;
DE Short=AtRABC2a;
DE AltName: Full=Ras-related protein Rab18B;
DE Short=AtRab18B;
GN Name=RABC2A; Synonyms=RAB18B; OrderedLocusNames=At5g03530;
GN ORFNames=F12E4.310;
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].
RX PubMed=9396626; DOI=10.1016/s0167-4781(97)00130-9;
RA Mikami K., Ichimura K., Iuch S., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Molecular characterization of a cDNA encoding a novel small GTP-binding
RT protein from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1354:99-104(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH XI-2/MYA2, AND SUBCELLULAR LOCATION.
RX PubMed=18703495; DOI=10.1093/jxb/ern202;
RA Hashimoto K., Igarashi H., Mano S., Takenaka C., Shiina T., Yamaguchi M.,
RA Demura T., Nishimura M., Shimmen T., Yokota E.;
RT "An isoform of Arabidopsis myosin XI interacts with small GTPases in its C-
RT terminal tail region.";
RL J. Exp. Bot. 59:3523-3531(2008).
CC -!- FUNCTION: Intracellular vesicle trafficking and protein transport.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with XI-2/MYA2. {ECO:0000269|PubMed:18703495}.
CC -!- INTERACTION:
CC O49841; Q9LKB9: XI-2; NbExp=3; IntAct=EBI-2009559, EBI-2009528;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:18703495}. Note=Colocalizes with peroxisome.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; D89824; BAA24074.1; -; mRNA.
DR EMBL; AL162751; CAB83314.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90619.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70568.1; -; Genomic_DNA.
DR EMBL; AK119027; BAC43603.1; -; mRNA.
DR EMBL; BT006101; AAP04086.1; -; mRNA.
DR PIR; T48379; T48379.
DR RefSeq; NP_001332165.1; NM_001342711.1.
DR RefSeq; NP_568121.1; NM_120433.3.
DR AlphaFoldDB; O49841; -.
DR SMR; O49841; -.
DR BioGRID; 17086; 1.
DR IntAct; O49841; 1.
DR STRING; 3702.AT5G03530.1; -.
DR iPTMnet; O49841; -.
DR PaxDb; O49841; -.
DR PRIDE; O49841; -.
DR ProteomicsDB; 236389; -.
DR EnsemblPlants; AT5G03530.1; AT5G03530.1; AT5G03530.
DR EnsemblPlants; AT5G03530.2; AT5G03530.2; AT5G03530.
DR GeneID; 831810; -.
DR Gramene; AT5G03530.1; AT5G03530.1; AT5G03530.
DR Gramene; AT5G03530.2; AT5G03530.2; AT5G03530.
DR KEGG; ath:AT5G03530; -.
DR Araport; AT5G03530; -.
DR TAIR; locus:2831859; AT5G03530.
DR eggNOG; KOG0080; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; O49841; -.
DR OMA; VYDVSCQ; -.
DR OrthoDB; 1247169at2759; -.
DR PhylomeDB; O49841; -.
DR PRO; PR:O49841; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O49841; baseline and differential.
DR Genevisible; O49841; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:TAIR.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0080115; F:myosin XI tail binding; IPI:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..210
FT /note="Ras-related protein RABC2a"
FT /id="PRO_0000407358"
FT MOTIF 41..49
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 157..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 209
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 23306 MW; 551337D936809B5B CRC64;
MGSSSGQSGY DLSFKILLIG DSGVGKSSLL VSFISSSVED LAPTIGVDFK IKQLTVGGKR
LKLTIWDTAG QERFRTLTSS YYRGAQGIIL VYDVTRRETF TNLVDVWGKE IELYSTNQEC
VRMLVGNKVD RESERGVSRE EGIALAKELN CMFLECSART RQNVEQCFEE LALKIMEVPS
LLEEGSSAVK RNILKQKPEH QTNTQSGCCS
