RAE1D_ARATH
ID RAE1D_ARATH Reviewed; 216 AA.
AC Q9LZD4; Q2V3A4; Q8LBQ4;
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 RABE1d;
DE Short=AtRABE1d;
DE AltName: Full=Ras-related protein Rab8C;
DE Short=AtRab8C;
GN Name=RABE1D; Synonyms=RAB8C; OrderedLocusNames=At5g03520;
GN ORFNames=F12E4.300;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [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 INTERACTION WITH PI5K2, AND MUTAGENESIS OF SER-29 AND GLN-74.
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 Q9LZD4; Q8LA96: At4g17720; NbExp=3; IntAct=EBI-25518674, EBI-4425250;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane. Cell membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LZD4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LZD4-2; Sequence=VSP_040949;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AL162751; CAB83313.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90617.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90618.1; -; Genomic_DNA.
DR EMBL; AY035124; AAK59629.1; -; mRNA.
DR EMBL; AY056351; AAL07200.1; -; mRNA.
DR EMBL; AY087058; AAM64619.1; -; mRNA.
DR PIR; T48378; T48378.
DR RefSeq; NP_001031827.1; NM_001036750.1. [Q9LZD4-2]
DR RefSeq; NP_195972.1; NM_120432.5. [Q9LZD4-1]
DR AlphaFoldDB; Q9LZD4; -.
DR SMR; Q9LZD4; -.
DR BioGRID; 17093; 2.
DR IntAct; Q9LZD4; 1.
DR STRING; 3702.AT5G03520.1; -.
DR iPTMnet; Q9LZD4; -.
DR PaxDb; Q9LZD4; -.
DR PRIDE; Q9LZD4; -.
DR ProteomicsDB; 236559; -. [Q9LZD4-1]
DR EnsemblPlants; AT5G03520.1; AT5G03520.1; AT5G03520. [Q9LZD4-1]
DR EnsemblPlants; AT5G03520.2; AT5G03520.2; AT5G03520. [Q9LZD4-2]
DR GeneID; 831817; -.
DR Gramene; AT5G03520.1; AT5G03520.1; AT5G03520. [Q9LZD4-1]
DR Gramene; AT5G03520.2; AT5G03520.2; AT5G03520. [Q9LZD4-2]
DR KEGG; ath:AT5G03520; -.
DR Araport; AT5G03520; -.
DR TAIR; locus:2142684; AT5G03520.
DR eggNOG; KOG0078; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q9LZD4; -.
DR OMA; LINIRNW; -.
DR PhylomeDB; Q9LZD4; -.
DR PRO; PR:Q9LZD4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZD4; baseline and differential.
DR Genevisible; Q9LZD4; AT.
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; HDA:TAIR.
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 Alternative splicing; Cell membrane; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..216
FT /note="Ras-related protein RABE1d"
FT /id="PRO_0000407368"
FT REGION 196..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 2..49
FT /note="AVAPARARSDYDYLIKLLLIGDSGVGKSCLLLRFSDDTFTTSFITTIG ->
FT ITSSSFFSSAIAVWGRVVCYFDSQMILSLQVSLLPLGI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040949"
FT MUTAGEN 29
FT /note="S->N: Loss of binding to PI5K2."
FT /evidence="ECO:0000269|PubMed:19903693"
FT MUTAGEN 74
FT /note="Q->L: Increases binding efficiency to PI5K2."
FT /evidence="ECO:0000269|PubMed:19903693"
FT CONFLICT 121
FT /note="V -> F (in Ref. 4; AAM64619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24037 MW; 50C7D3AF4DC86F67 CRC64;
MAVAPARARS DYDYLIKLLL IGDSGVGKSC LLLRFSDDTF TTSFITTIGI DFKIRTVELD
GKRIKLQIWD TAGQERFRTI TTAYYRGAMG ILLVYDVTDE SSFNNIRNWM KNIEQHASDN
VNKILVGNKA DMDESKRAVP TAKGQALADE YGIKFFETSA KTNLNVENVF MSIAKDIKQR
LTETDTKAEP QGIKITKQDT AASSSTAEKS ACCSYV
