RAE1C_ARATH
ID RAE1C_ARATH Reviewed; 216 AA.
AC P28186;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ras-related protein RABE1c;
DE Short=AtRABE1c;
DE AltName: Full=Ras-related protein Ara-3;
DE AltName: Full=Ras-related protein Rab8A;
DE Short=AtRab8A;
GN Name=RABE1C; Synonyms=ARA-3, RAB8A; OrderedLocusNames=At3g46060;
GN ORFNames=F12M12.30;
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].
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 [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=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 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 INDUCTION BY ETHYLENE.
RX PubMed=12692329; DOI=10.1104/pp.014035;
RA Moshkov I.E., Mur L.A., Novikova G.V., Smith A.R., Hall M.A.;
RT "Ethylene regulates monomeric GTP-binding protein gene expression and
RT activity in Arabidopsis.";
RL Plant Physiol. 131:1705-1717(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [8]
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 -!- INTERACTION:
CC P28186; Q8LA96: At4g17720; NbExp=4; IntAct=EBI-4433523, EBI-4425250;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane. Cell membrane
CC {ECO:0000269|PubMed:15060130}; Lipid-anchor {ECO:0000305}.
CC -!- INDUCTION: By ethylene. {ECO:0000269|PubMed:12692329}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; D01025; BAA00830.1; -; mRNA.
DR EMBL; AL355775; CAB90933.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78106.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78107.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78108.1; -; Genomic_DNA.
DR EMBL; AY035132; AAK59637.1; -; mRNA.
DR EMBL; AY042795; AAK68735.1; -; mRNA.
DR EMBL; BT001952; AAN71951.1; -; mRNA.
DR EMBL; BT002186; AAN72197.1; -; mRNA.
DR PIR; JS0640; JS0640.
DR RefSeq; NP_001078248.1; NM_001084779.1.
DR RefSeq; NP_001118780.1; NM_001125308.1.
DR RefSeq; NP_190192.1; NM_114475.4.
DR AlphaFoldDB; P28186; -.
DR SMR; P28186; -.
DR BioGRID; 9069; 11.
DR IntAct; P28186; 10.
DR STRING; 3702.AT3G46060.2; -.
DR iPTMnet; P28186; -.
DR PaxDb; P28186; -.
DR PRIDE; P28186; -.
DR ProteomicsDB; 236626; -.
DR EnsemblPlants; AT3G46060.1; AT3G46060.1; AT3G46060.
DR EnsemblPlants; AT3G46060.2; AT3G46060.2; AT3G46060.
DR EnsemblPlants; AT3G46060.3; AT3G46060.3; AT3G46060.
DR GeneID; 823749; -.
DR Gramene; AT3G46060.1; AT3G46060.1; AT3G46060.
DR Gramene; AT3G46060.2; AT3G46060.2; AT3G46060.
DR Gramene; AT3G46060.3; AT3G46060.3; AT3G46060.
DR KEGG; ath:AT3G46060; -.
DR Araport; AT3G46060; -.
DR TAIR; locus:2075251; AT3G46060.
DR eggNOG; KOG0078; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P28186; -.
DR OMA; SKMEQNE; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P28186; -.
DR PRO; PR:P28186; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P28186; baseline and differential.
DR Genevisible; P28186; 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:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:1901527; P:abscisic acid-activated signaling pathway involved in stomatal movement; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEP:TAIR.
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..216
FT /note="Ras-related protein RABE1c"
FT /id="PRO_0000121289"
FT MOTIF 44..52
FT /note="Effector region"
FT /evidence="ECO:0000250"
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 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 23835 MW; 09E9C19A7A44E705 CRC64;
MAAPPARARA DYDYLIKLLL IGDSGVGKSC LLLRFSDGSF TTSFITTIGI DFKIRTIELD
GKRIKLQIWD TAGQERFRTI TTAYYRGAMG ILLVYDVTDE SSFNNIRNWI RNIEQHASDN
VNKILVGNKA DMDESKRAVP TAKGQALADE YGIKFFETSA KTNLNVEEVF FSIGRDIKQR
LSDTDSRAEP ATIKISQTDQ AAGAGQATQK SACCGT
