RAD2A_ARATH
ID RAD2A_ARATH Reviewed; 203 AA.
AC P28188; Q940Z7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ras-related protein RABD2a;
DE Short=AtRABD2a;
DE AltName: Full=Ras-related protein Ara-5;
DE AltName: Full=Ras-related protein Rab1B;
DE Short=AtRab1B;
GN Name=RABD2A; Synonyms=ARA-5, RAB1B; OrderedLocusNames=At1g02130;
GN ORFNames=T7I23.6;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 [MRNA] OF 9-203.
RC STRAIN=cv. Columbia, cv. En-1, cv. Est, cv. Landsberg erecta, and
RC cv. Lapalmam; TISSUE=Leaf;
RX PubMed=1748311; DOI=10.1016/0378-1119(91)90442-e;
RA Anai T., Hasegawa K., Watanabe Y., Uchimiya H., Ishizaki R., Matsui M.;
RT "Isolation and analysis of cDNAs encoding small GTP-binding proteins of
RT Arabidopsis thaliana.";
RL Gene 108:259-264(1991).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ASN-121.
RX PubMed=11090219; DOI=10.2307/3871115;
RA Batoko H., Zheng H.-Q., Hawes C., Moore I.;
RT "A rab1 GTPase is required for transport between the endoplasmic reticulum
RT and Golgi apparatus and for normal Golgi movement in plants.";
RL Plant Cell 12:2201-2218(2000).
RN [6]
RP FUNCTION.
RX PubMed=11874578; DOI=10.1046/j.0960-7412.2002.01252.x;
RA Saint-Jore C.M., Evins J., Batoko H., Brandizzi F., Moore I., Hawes C.;
RT "Redistribution of membrane proteins between the Golgi apparatus and
RT endoplasmic reticulum in plants is reversible and not dependent on
RT cytoskeletal networks.";
RL Plant J. 29:661-678(2002).
RN [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Protein transport. Regulator of membrane traffic from the
CC Golgi apparatus towards the endoplasmic reticulum (ER).
CC {ECO:0000269|PubMed:11090219, ECO:0000269|PubMed:11874578}.
CC -!- SUBUNIT: Does not interact with GC5.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24370.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U89959; AAC24370.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27387.1; -; Genomic_DNA.
DR EMBL; AY052333; AAK96526.1; -; mRNA.
DR EMBL; AY061905; AAL31232.1; -; mRNA.
DR EMBL; D01027; BAA00832.1; -; mRNA.
DR PIR; B86153; B86153.
DR PIR; PS0279; PS0279.
DR RefSeq; NP_171715.1; NM_100093.4.
DR AlphaFoldDB; P28188; -.
DR SMR; P28188; -.
DR BioGRID; 22265; 1.
DR IntAct; P28188; 1.
DR MINT; P28188; -.
DR STRING; 3702.AT1G02130.1; -.
DR iPTMnet; P28188; -.
DR PaxDb; P28188; -.
DR PRIDE; P28188; -.
DR ProteomicsDB; 236700; -.
DR EnsemblPlants; AT1G02130.1; AT1G02130.1; AT1G02130.
DR GeneID; 837023; -.
DR Gramene; AT1G02130.1; AT1G02130.1; AT1G02130.
DR KEGG; ath:AT1G02130; -.
DR Araport; AT1G02130; -.
DR TAIR; locus:2205603; AT1G02130.
DR eggNOG; KOG0084; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P28188; -.
DR OMA; DCTDLES; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; P28188; -.
DR PRO; PR:P28188; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P28188; baseline and differential.
DR Genevisible; P28188; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..203
FT /note="Ras-related protein RABD2a"
FT /id="PRO_0000121292"
FT REGION 176..203
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 LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 121
FT /note="N->I: Inhibits trafficking between the ER and
FT Golgi."
FT /evidence="ECO:0000269|PubMed:11090219"
SQ SEQUENCE 203 AA; 22648 MW; 85A2870837300B8D CRC64;
MNPEYDYLFK LLLIGDSGVG KSCLLLRFSD DSYVESYIST IGVDFKIRTV EQDGKTIKLQ
IWDTAGQERF RTITSSYYRG AHGIIIVYDV TDEESFNNVK QWLSEIDRYA SDNVNKLLVG
NKSDLTENRA IPYETAKAFA DEIGIPFMET SAKDATNVEQ AFMAMSASIK ERMASQPAGN
NARPPTVQIR GQPVAQKNGC CST
