RAA4B_ARATH
ID RAA4B_ARATH Reviewed; 224 AA.
AC Q9SMQ6; Q38923; Q8L958;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ras-related protein RABA4b {ECO:0000303|PubMed:12644670};
DE Short=AtRABA4b {ECO:0000303|PubMed:12644670};
DE AltName: Full=Ras-related protein GB3 {ECO:0000303|PubMed:8843944};
DE Short=AtGB3 {ECO:0000303|PubMed:8843944};
DE AltName: Full=Ras-related protein Rab11G {ECO:0000305|PubMed:12644670};
DE Short=AtRab11G {ECO:0000305|PubMed:12644670};
GN Name=RABA4B {ECO:0000303|PubMed:12644670};
GN Synonyms=GB3 {ECO:0000303|PubMed:8843944},
GN RAB11G {ECO:0000305|PubMed:12644670};
GN OrderedLocusNames=At4g39990 {ECO:0000312|Araport:AT4G39990};
GN ORFNames=T5J17.160 {ECO:0000312|EMBL:CAB38912.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8843944; DOI=10.1007/bf00040720;
RA Biermann B.J., Randall S.K., Crowell D.N.;
RT "Identification and isoprenylation of plant GTP-binding proteins.";
RL Plant Mol. Biol. 31:1021-1028(1996).
RN [2]
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 [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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 TISSUE SPECIFICITY.
RX PubMed=15155878; DOI=10.1105/tpc.021634;
RA Preuss M.L., Serna J., Falbel T.G., Bednarek S.Y., Nielsen E.;
RT "The Arabidopsis Rab GTPase RabA4b localizes to the tips of growing root
RT hair cells.";
RL Plant Cell 16:1589-1603(2004).
RN [8]
RP INTERACTION WITH TCTP1.
RX PubMed=20736351; DOI=10.1073/pnas.1007926107;
RA Brioudes F., Thierry A.M., Chambrier P., Mollereau B., Bendahmane M.;
RT "Translationally controlled tumor protein is a conserved mitotic growth
RT integrator in animals and plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16384-16389(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21134079; DOI=10.1111/j.1600-0854.2010.01146.x;
RA Kang B.H., Nielsen E., Preuss M.L., Mastronarde D., Staehelin L.A.;
RT "Electron tomography of RabA4b- and PI-4Kbeta1-labeled trans Golgi network
RT compartments in Arabidopsis.";
RL Traffic 12:313-329(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Regulator of membrane trafficking. May be required for
CC secretion of cell wall components in cells.
CC -!- SUBUNIT: Interacts with TCTP1. {ECO:0000269|PubMed:20736351}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:21134079}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000305|PubMed:21134079}; Lipid-anchor
CC {ECO:0000305|PubMed:21134079}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
CC Expressed in tips of growing root hair cells.
CC {ECO:0000269|PubMed:15155878}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; U46926; AAA87884.1; -; mRNA.
DR EMBL; AL035708; CAB38912.1; -; Genomic_DNA.
DR EMBL; AL161596; CAB80662.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87150.1; -; Genomic_DNA.
DR EMBL; AY072448; AAL62440.1; -; mRNA.
DR EMBL; AY128914; AAM91314.1; -; mRNA.
DR EMBL; AY088624; AAM66946.1; -; mRNA.
DR PIR; T06105; T06105.
DR RefSeq; NP_195709.1; NM_120163.4.
DR AlphaFoldDB; Q9SMQ6; -.
DR SMR; Q9SMQ6; -.
DR BioGRID; 15440; 2.
DR IntAct; Q9SMQ6; 1.
DR MINT; Q9SMQ6; -.
DR STRING; 3702.AT4G39990.1; -.
DR iPTMnet; Q9SMQ6; -.
DR PaxDb; Q9SMQ6; -.
DR PRIDE; Q9SMQ6; -.
DR ProteomicsDB; 225903; -.
DR EnsemblPlants; AT4G39990.1; AT4G39990.1; AT4G39990.
DR GeneID; 830160; -.
DR Gramene; AT4G39990.1; AT4G39990.1; AT4G39990.
DR KEGG; ath:AT4G39990; -.
DR Araport; AT4G39990; -.
DR TAIR; locus:2140079; AT4G39990.
DR eggNOG; KOG0087; Eukaryota.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; Q9SMQ6; -.
DR OMA; LMMEIFN; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; Q9SMQ6; -.
DR PRO; PR:Q9SMQ6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SMQ6; baseline and differential.
DR Genevisible; Q9SMQ6; AT.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0090404; C:pollen tube tip; IDA:TAIR.
DR GO; GO:0035619; C:root hair tip; IDA:TAIR.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
DR GO; GO:0032456; P:endocytic recycling; IDA:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
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.
PE 1: Evidence at protein level;
KW Acetylation; Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..224
FT /note="Ras-related protein RABA4b"
FT /id="PRO_0000407345"
FT MOTIF 46..54
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 72..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 160..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT LIPID 220
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 221
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 191
FT /note="G -> C (in Ref. 1; AAA87884)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="G -> A (in Ref. 5; AAM66946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24407 MW; FA2C5E5A0DC2025B CRC64;
MAGGGGYGGA SGKVDYVFKV VLIGDSAVGK SQLLARFARD EFSMDSKATI GVEFQTRTLS
IEQKSIKAQI WDTAGQERYR AVTSAYYRGA VGAMLVYDMT KRETFEHIPR WLEELRAHAD
KNIVIILIGN KSDLEDQRAV PTEDAKEFAE KEGLFFLETS ALNATNVENS FNTLMTQIYN
TVNKKNLASE GDSNNPGSLA GKKILIPGSG QEIPAKTSTC CTSS
