RABA3_ARATH
ID RABA3_ARATH Reviewed; 237 AA.
AC Q9LNK1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ras-related protein RABA3;
DE Short=AtRABA3;
GN Name=RABA3; OrderedLocusNames=At1g01200; ORFNames=F6F3.1;
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 [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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) 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=18239134; DOI=10.1105/tpc.107.052001;
RA Chow C.M., Neto H., Foucart C., Moore I.;
RT "Rab-A2 and Rab-A3 GTPases define a trans-Golgi endosomal membrane domain
RT in Arabidopsis that contributes substantially to the cell plate.";
RL Plant Cell 20:101-123(2008).
CC -!- FUNCTION: Intracellular vesicle trafficking and protein transport.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:18239134}.
CC Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305|PubMed:18239134}; Lipid-anchor
CC {ECO:0000305|PubMed:18239134}. Note=During cytokinesis located to the
CC growing margins of the cell plate.
CC -!- TISSUE SPECIFICITY: Expressed in root tips.
CC {ECO:0000269|PubMed:18239134}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC023628; AAF97325.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27253.1; -; Genomic_DNA.
DR EMBL; BT010707; AAR20764.1; -; mRNA.
DR EMBL; BT010979; AAR24757.1; -; mRNA.
DR PIR; B86142; B86142.
DR RefSeq; NP_171628.2; NM_100002.4.
DR AlphaFoldDB; Q9LNK1; -.
DR SMR; Q9LNK1; -.
DR BioGRID; 24728; 3.
DR IntAct; Q9LNK1; 2.
DR STRING; 3702.AT1G01200.1; -.
DR iPTMnet; Q9LNK1; -.
DR PaxDb; Q9LNK1; -.
DR PRIDE; Q9LNK1; -.
DR ProteomicsDB; 236497; -.
DR EnsemblPlants; AT1G01200.1; AT1G01200.1; AT1G01200.
DR GeneID; 839493; -.
DR Gramene; AT1G01200.1; AT1G01200.1; AT1G01200.
DR KEGG; ath:AT1G01200; -.
DR Araport; AT1G01200; -.
DR TAIR; locus:2035302; AT1G01200.
DR eggNOG; KOG0087; Eukaryota.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; Q9LNK1; -.
DR OMA; ITSRFCD; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; Q9LNK1; -.
DR PRO; PR:Q9LNK1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNK1; baseline and differential.
DR Genevisible; Q9LNK1; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042546; P:cell wall biogenesis; IMP: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 2: Evidence at transcript level;
KW Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..237
FT /note="Ras-related protein RABA3"
FT /id="PRO_0000407343"
FT MOTIF 57..65
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 35..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 172..173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 237
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 235
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 237
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 237 AA; 26250 MW; 5C3A5AFE61E105FC CRC64;
MNEEMSGESP ENNKHVKKPT MPEKIDYVFK VVVIGDSAVG KTQLLSRFTH NEFCYDSKST
IGVEFQTRTI TLRGKLVKAQ IWDTAGQERY RAVTSAYYRG ALGAMVVYDI TKRLSFDHVA
RWVEELRAHA DDSAVIMLVG NKADLSVGKR AVPTEDAVEF AETQRLFFSE VSALSGGNVD
EAFFRLLEEI FSRVVVSRKA MESDGGATVK LDGSRIDVIS GSDLETSNIK EQASCSC
