RABD1_ARATH
ID RABD1_ARATH Reviewed; 205 AA.
AC Q9ZRE2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ras-related protein RABD1;
DE Short=AtRABD1;
DE AltName: Full=Ras-related protein ATFP8;
GN Name=RABD1; Synonyms=ATFP8; OrderedLocusNames=At3g11730; ORFNames=F26K24.2;
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 [MRNA], AND ISOPRENYLATION.
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 GC5.
RX PubMed=18182439; DOI=10.1093/jxb/erm304;
RA Latijnhouwers M., Gillespie T., Boevink P., Kriechbaumer V., Hawes C.,
RA Carvalho C.M.;
RT "Localization and domain characterization of Arabidopsis golgin
RT candidates.";
RL J. Exp. Bot. 58:4373-4386(2007).
RN [8]
RP INTERACTION WITH XI-2/MYA2.
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).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-22; GLN-67 AND ASN-121.
RX PubMed=19789181; DOI=10.1242/jcs.050625;
RA Pinheiro H., Samalova M., Geldner N., Chory J., Martinez A., Moore I.;
RT "Genetic evidence that the higher plant Rab-D1 and Rab-D2 GTPases exhibit
RT distinct but overlapping interactions in the early secretory pathway.";
RL J. Cell Sci. 122:3749-3758(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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: Protein transport. Regulator of membrane traffic from the
CC Golgi apparatus towards the endoplasmic reticulum (ER).
CC -!- SUBUNIT: Does not interact with GC5. Interacts with XI-2/MYA2.
CC {ECO:0000269|PubMed:18182439, ECO:0000269|PubMed:18703495}.
CC -!- INTERACTION:
CC Q9ZRE2; Q9LKB9: XI-2; NbExp=3; IntAct=EBI-2009542, EBI-2009528;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:19789181}. Golgi apparatus membrane
CC {ECO:0000305|PubMed:19789181}; Lipid-anchor
CC {ECO:0000305|PubMed:19789181}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; U64911; AAD00111.1; -; mRNA.
DR EMBL; AC016795; AAF23189.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75090.1; -; Genomic_DNA.
DR EMBL; AK118150; BAC42775.1; -; mRNA.
DR EMBL; BT005576; AAO63996.1; -; mRNA.
DR RefSeq; NP_187779.1; NM_112005.4.
DR AlphaFoldDB; Q9ZRE2; -.
DR SMR; Q9ZRE2; -.
DR BioGRID; 5679; 10.
DR IntAct; Q9ZRE2; 10.
DR STRING; 3702.AT3G11730.1; -.
DR iPTMnet; Q9ZRE2; -.
DR SwissPalm; Q9ZRE2; -.
DR PaxDb; Q9ZRE2; -.
DR PRIDE; Q9ZRE2; -.
DR ProteomicsDB; 236556; -.
DR EnsemblPlants; AT3G11730.1; AT3G11730.1; AT3G11730.
DR GeneID; 820345; -.
DR Gramene; AT3G11730.1; AT3G11730.1; AT3G11730.
DR KEGG; ath:AT3G11730; -.
DR Araport; AT3G11730; -.
DR TAIR; locus:2081486; AT3G11730.
DR eggNOG; KOG0084; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q9ZRE2; -.
DR OMA; KMGSQTN; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; Q9ZRE2; -.
DR PRO; PR:Q9ZRE2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZRE2; baseline and differential.
DR Genevisible; Q9ZRE2; AT.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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: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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
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 Acetylation; ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..205
FT /note="Ras-related protein RABD1"
FT /id="PRO_0000348544"
FT REGION 174..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 151..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT LIPID 202
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 203
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 22
FT /note="S->N: Dominant negative (GDP-bound form); no effect
FT on trafficking between the ER and Golgi."
FT /evidence="ECO:0000269|PubMed:19789181"
FT MUTAGEN 67
FT /note="Q->L: No effect on trafficking between the ER and
FT Golgi."
FT /evidence="ECO:0000269|PubMed:19789181"
FT MUTAGEN 121
FT /note="N->I: Inhibits trafficking between the ER and Golgi.
FT Causes severe dwarfism and seedlings death."
FT /evidence="ECO:0000269|PubMed:19789181"
SQ SEQUENCE 205 AA; 22725 MW; 8842C2B074B71AAD CRC64;
MSNEYDYLFK LLLIGDSSVG KSCLLLRFAD DAYIDSYIST IGVDFKIRTI EQDGKTIKLQ
IWDTAGQERF RTITSSYYRG AHGIIIVYDC TEMESFNNVK QWLSEIDRYA NESVCKLLIG
NKNDMVESKV VSTETGRALA DELGIPFLET SAKDSINVEQ AFLTIAGEIK KKMGSQTNAN
KTSGPGTVQM KGQPIQQNNG GCCGQ
