RAE1E_ARATH
ID RAE1E_ARATH Reviewed; 218 AA.
AC Q9SF91;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ras-related protein RABE1e;
DE Short=AtRABE1e;
DE AltName: Full=Ras-related protein Rab8E;
DE Short=AtRab8E;
GN Name=RABE1E; Synonyms=RAB8E; OrderedLocusNames=At3g09900; ORFNames=F8A24.5;
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=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 [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., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [7]
RP INTERACTION WITH PI5K2.
RX PubMed=19903693; DOI=10.1242/jcs.053488;
RA Camacho L., Smertenko A.P., Perez-Gomez J., Hussey P.J., Moore I.;
RT "Arabidopsis Rab-E GTPases exhibit a novel interaction with a plasma-
RT membrane phosphatidylinositol-4-phosphate 5-kinase.";
RL J. Cell Sci. 122:4383-4392(2009).
CC -!- FUNCTION: Involved in membrane trafficking from the Golgi to the plasma
CC membrane. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PI5K2. {ECO:0000269|PubMed:19903693}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane. Cell membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AC015985; AAF23246.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74828.1; -; Genomic_DNA.
DR EMBL; BT024925; ABD94081.1; -; mRNA.
DR EMBL; AK229294; BAF01157.1; -; mRNA.
DR EMBL; AY084345; AAM60928.1; -; mRNA.
DR RefSeq; NP_187601.1; NM_111825.4.
DR AlphaFoldDB; Q9SF91; -.
DR SMR; Q9SF91; -.
DR STRING; 3702.AT3G09900.1; -.
DR iPTMnet; Q9SF91; -.
DR PaxDb; Q9SF91; -.
DR PRIDE; Q9SF91; -.
DR ProteomicsDB; 236560; -.
DR EnsemblPlants; AT3G09900.1; AT3G09900.1; AT3G09900.
DR GeneID; 820148; -.
DR Gramene; AT3G09900.1; AT3G09900.1; AT3G09900.
DR KEGG; ath:AT3G09900; -.
DR Araport; AT3G09900; -.
DR TAIR; locus:2085089; AT3G09900.
DR eggNOG; KOG0078; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q9SF91; -.
DR OMA; NEKSACC; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; Q9SF91; -.
DR PRO; PR:Q9SF91; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF91; baseline and differential.
DR Genevisible; Q9SF91; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; 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 Cell membrane; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..218
FT /note="Ras-related protein RABE1e"
FT /id="PRO_0000407369"
FT REGION 182..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..52
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 197..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 159..160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 24295 MW; E4C701A49AE426A1 CRC64;
MAVAPARARS DYDYLIKLLL IGDSGVGKSC LLLRFSDDTF TTSFITTIGI DFKIRTVELD
GKRIKLQIWD TAGQERFRTI TTAYYRGAMG ILLVYDVTDE SSFNNIRNWM KNIEQHASDS
VNKILVGNKA DMDESKRAVP TSKGQALADE YGIKFFETSA KTNQNVEQVF LSIAKDIKQR
LTESDTKAEP QGIKITKQDA NKASSSSTNE KSACCSYV
