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RAA1D_ARATH
ID   RAA1D_ARATH             Reviewed;         214 AA.
AC   Q9SN35;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Ras-related protein RABA1d;
DE            Short=AtRABA1d;
DE   AltName: Full=Ras-related protein Rab11B;
DE            Short=AtRab11B;
DE   AltName: Full=Ras-related protein SGBP;
DE            Short=AthSGBP;
GN   Name=RABA1D; Synonyms=RAB11B, SGBP; OrderedLocusNames=At4g18800;
GN   ORFNames=F28A21.210;
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=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].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20841426; DOI=10.1105/tpc.109.069880;
RA   Ovecka M., Berson T., Beck M., Derksen J., Samaj J., Baluska F.,
RA   Lichtscheidl I.K.;
RT   "Structural sterols are involved in both the initiation and tip growth of
RT   root hairs in Arabidopsis thaliana.";
RL   Plant Cell 22:2999-3019(2010).
CC   -!- FUNCTION: Intracellular vesicle trafficking and protein transport.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9SN35; Q8LA96: At4g17720; NbExp=4; IntAct=EBI-4454333, EBI-4425250;
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000269|PubMed:20841426}. Golgi apparatus, trans-Golgi network
CC       membrane {ECO:0000305|PubMed:20841426}; Lipid-anchor
CC       {ECO:0000305|PubMed:20841426}.
CC   -!- TISSUE SPECIFICITY: Expressed in the vesicle-rich apical dome of
CC       growing root hairs. {ECO:0000269|PubMed:20841426}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AL035526; CAB37465.1; -; Genomic_DNA.
DR   EMBL; AL161549; CAB78882.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84091.1; -; Genomic_DNA.
DR   EMBL; BT003901; AAO41949.1; -; mRNA.
DR   EMBL; BT004936; AAO50469.1; -; mRNA.
DR   EMBL; AK228509; BAF00433.1; -; mRNA.
DR   PIR; T04872; T04872.
DR   RefSeq; NP_193615.1; NM_117996.6.
DR   AlphaFoldDB; Q9SN35; -.
DR   SMR; Q9SN35; -.
DR   BioGRID; 12907; 4.
DR   IntAct; Q9SN35; 2.
DR   STRING; 3702.AT4G18800.1; -.
DR   iPTMnet; Q9SN35; -.
DR   PaxDb; Q9SN35; -.
DR   PRIDE; Q9SN35; -.
DR   ProteomicsDB; 226097; -.
DR   EnsemblPlants; AT4G18800.1; AT4G18800.1; AT4G18800.
DR   GeneID; 827614; -.
DR   Gramene; AT4G18800.1; AT4G18800.1; AT4G18800.
DR   KEGG; ath:AT4G18800; -.
DR   Araport; AT4G18800; -.
DR   TAIR; locus:2124092; AT4G18800.
DR   eggNOG; KOG0087; Eukaryota.
DR   HOGENOM; CLU_041217_23_0_1; -.
DR   InParanoid; Q9SN35; -.
DR   OMA; NIRAQIW; -.
DR   OrthoDB; 1133775at2759; -.
DR   PhylomeDB; Q9SN35; -.
DR   PRO; PR:Q9SN35; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SN35; baseline and differential.
DR   Genevisible; Q9SN35; AT.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0042546; P:cell wall biogenesis; IMP: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; 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   Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..214
FT                   /note="Ras-related protein RABA1d"
FT                   /id="PRO_0000407335"
FT   MOTIF           42..50
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         68..72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           211
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           212
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   214 AA;  23870 MW;  FF5EE36FDD333560 CRC64;
     MAGYRADDDY DYLFKVVLIG DSGVGKSNLL SRFTRNEFSL ESKSTIGVEF ATRSLNVNEK
     VIKAQIWDTA GQERYRAITS AYYRGAVGAL LVYDVTRHST FENVERWLRE LRDHTDPNIV
     VMLVGNKSDL RHLVAVQTED AKSFAENESL YFMETSALES TNVENAFSEV LTQIYHVVSK
     KAMEAGEDSG NVPSKGEKID VDVSAVKKTG CCSN
 
 
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