RAB1B_ARATH
ID RAB1B_ARATH Reviewed; 211 AA.
AC Q38922; A8MRA2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ras-related protein RABB1b;
DE Short=AtRABB1b;
DE AltName: Full=Ras-related protein GB2;
DE Short=AtGB2;
DE AltName: Full=Ras-related protein Rab2C;
DE Short=AtRab2C;
GN Name=RABB1B; Synonyms=GB2, RAB2C; OrderedLocusNames=At4g35860;
GN ORFNames=F4B14.130;
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] (ISOFORM 1).
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] (ISOFORM 1).
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] (ISOFORM 1).
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).
CC -!- FUNCTION: Intracellular vesicle trafficking and protein transport.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q38922-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q38922-3; Sequence=VSP_040946;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; U46925; AAA87883.1; -; mRNA.
DR EMBL; AL031986; CAA21472.1; -; Genomic_DNA.
DR EMBL; AL161588; CAB81495.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86581.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86582.1; -; Genomic_DNA.
DR EMBL; AY065262; AAL38738.1; -; mRNA.
DR EMBL; AY117348; AAM51423.1; -; mRNA.
DR EMBL; AY085750; AAM62968.1; -; mRNA.
DR PIR; S71585; S71585.
DR RefSeq; NP_001078499.1; NM_001085030.1. [Q38922-3]
DR RefSeq; NP_195311.1; NM_119752.4. [Q38922-1]
DR AlphaFoldDB; Q38922; -.
DR SMR; Q38922; -.
DR BioGRID; 15022; 13.
DR IntAct; Q38922; 12.
DR STRING; 3702.AT4G35860.1; -.
DR PaxDb; Q38922; -.
DR PRIDE; Q38922; -.
DR ProteomicsDB; 225938; -. [Q38922-1]
DR EnsemblPlants; AT4G35860.1; AT4G35860.1; AT4G35860. [Q38922-1]
DR EnsemblPlants; AT4G35860.2; AT4G35860.2; AT4G35860. [Q38922-3]
DR GeneID; 829740; -.
DR Gramene; AT4G35860.1; AT4G35860.1; AT4G35860. [Q38922-1]
DR Gramene; AT4G35860.2; AT4G35860.2; AT4G35860. [Q38922-3]
DR KEGG; ath:AT4G35860; -.
DR Araport; AT4G35860; -.
DR TAIR; locus:2125384; AT4G35860.
DR eggNOG; KOG0098; Eukaryota.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q38922; -.
DR OMA; HITTING; -.
DR OrthoDB; 1271975at2759; -.
DR PhylomeDB; Q38922; -.
DR PRO; PR:Q38922; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38922; baseline and differential.
DR Genevisible; Q38922; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IDA:TAIR.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated 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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..211
FT /note="Ras-related protein RABB1b"
FT /id="PRO_0000407355"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 149..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 209
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 210
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040946"
SQ SEQUENCE 211 AA; 23175 MW; 71B5036D4B9A158E CRC64;
MSYDYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMVTV DGRPIKLQIW
DTAGQESFRS ITRSYYRGAA GALLVYDITR RETFNHLASW LEDARQHANP NMSIMLIGNK
CDLAHKRAVS KEEGQQFAKE HGLLFLEASA RTAQNVEEAF IETAAKILQN IQDGVFDVSN
ESSGIKIGYG RTQGAAGGRD GTISQGGGCC G
