REP_ARATH
ID REP_ARATH Reviewed; 563 AA.
AC Q8LLD4; Q8LPP8; Q9C8Z5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Rab escort protein 1 {ECO:0000305};
DE Short=AthREP {ECO:0000303|PubMed:15854662};
GN Name=REP {ECO:0000303|PubMed:15854662};
GN OrderedLocusNames=At3g06540 {ECO:0000312|Araport:AT3G06540};
GN ORFNames=F5E6.13 {ECO:0000312|EMBL:AAG51329.1};
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15854662; DOI=10.1016/j.jmb.2005.02.002;
RA Hala M., Elias M., Zarsky V.;
RT "A specific feature of the angiosperm Rab escort protein (REP) and
RT evolution of the REP/GDI superfamily.";
RL J. Mol. Biol. 348:1299-1313(2005).
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17140818; DOI=10.1016/j.cellbi.2006.04.011;
RA Wojtas M., Swiezewski S., Sarnowski T.J., Plochocka D., Chelstowska A.,
RA Tolmachova T., Swiezewska E.;
RT "Cloning and characterization of Rab escort protein (REP) from Arabidopsis
RT thaliana.";
RL Cell Biol. Int. 31:246-251(2007).
RN [6]
RP SUBUNIT.
RX PubMed=26589801; DOI=10.1074/jbc.m115.673491;
RA Shi W., Zeng Q., Kunkel B.N., Running M.P.;
RT "Arabidopsis Rab geranylgeranyltransferases demonstrate redundancy and
RT broad substrate specificity in vitro.";
RL J. Biol. Chem. 291:1398-1410(2016).
CC -!- FUNCTION: Substrate-binding subunit of the Rab
CC geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC proteins and presents the substrate peptide to the catalytic component
CC composed of the alpha subunit RGTA and the beta subunit RGTB
CC (Probable). Preferentially binds the GDP-bound form of Rab and
CC stimulates geranylgeranylation of various Rab GTPases in vitro
CC (PubMed:15854662). {ECO:0000269|PubMed:15854662,
CC ECO:0000305|PubMed:15854662, ECO:0000305|PubMed:17140818}.
CC -!- SUBUNIT: Heterotrimer composed of the alpha subunit RGTA, the beta
CC subunit RGTB and REP; within this trimer, RGTA and RGTB form the
CC catalytic component, while REP mediates peptide substrate binding.
CC {ECO:0000269|PubMed:26589801}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15854662}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:17140818}.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51329.1; Type=Erroneous gene model prediction; Evidence={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; AF409086; AAN03631.2; -; mRNA.
DR EMBL; AC020580; AAG51329.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74410.1; -; Genomic_DNA.
DR EMBL; AY094486; AAM19852.1; -; mRNA.
DR EMBL; BT000837; AAN33212.1; -; mRNA.
DR RefSeq; NP_187306.2; NM_111530.4.
DR AlphaFoldDB; Q8LLD4; -.
DR SMR; Q8LLD4; -.
DR IntAct; Q8LLD4; 6.
DR STRING; 3702.AT3G06540.1; -.
DR PaxDb; Q8LLD4; -.
DR PRIDE; Q8LLD4; -.
DR ProteomicsDB; 236874; -.
DR EnsemblPlants; AT3G06540.1; AT3G06540.1; AT3G06540.
DR GeneID; 819832; -.
DR Gramene; AT3G06540.1; AT3G06540.1; AT3G06540.
DR KEGG; ath:AT3G06540; -.
DR Araport; AT3G06540; -.
DR TAIR; locus:2084289; AT3G06540.
DR eggNOG; KOG4405; Eukaryota.
DR HOGENOM; CLU_021695_4_3_1; -.
DR InParanoid; Q8LLD4; -.
DR OMA; QMYPNEE; -.
DR OrthoDB; 1017439at2759; -.
DR PhylomeDB; Q8LLD4; -.
DR PRO; PR:Q8LLD4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LLD4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IMP:TAIR.
DR GO; GO:0031267; F:small GTPase binding; IDA:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0010152; P:pollen maturation; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:2000541; P:positive regulation of protein geranylgeranylation; IDA:TAIR.
DR GO; GO:0018344; P:protein geranylgeranylation; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR017230; Mrs6.
DR InterPro; IPR001738; Rab_escort.
DR PANTHER; PTHR11787; PTHR11787; 1.
DR Pfam; PF00996; GDI; 2.
DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR PRINTS; PR00891; RABGDIREP.
DR PRINTS; PR00894; YEASTMRS6P.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..563
FT /note="Rab escort protein 1"
FT /id="PRO_0000436613"
FT REGION 538..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 372
FT /note="S -> N (in Ref. 4; AAM19852/AAN33212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 61511 MW; 7CD780D3E3AC3A8D CRC64;
MIDIPPYPPL DPSNYDLIVV GTGVSESVLA AAASSSGSSV LHLDPNPFYG SHFASLSLPD
LTSFLHSNSV SPPPSPSSPP LPPSNNHDFI SVDLVNRSLY SSVEISSFES EILEEHSRRF
NVDLAGPRVV FCADESINLM LKSGANNYVE FKSIDASFVG DSSGELRNVP DSRAAIFKDK
SLTLLEKNQL MKFFKLVQSH LASSTEKDDS TTVKISEEDM ESPFVDFLSK MRLPPKIKSI
ILYAIAMLDY DQDNTETCRH LLKTKEGIDR LALYITSMGR FSNALGALIY PIYGQGELPQ
AFCRRAAVKG CIYVLRMPIT ALLLDKETGG YKGVRLASGQ EIFSQKLILD PCVTVGLESL
SSLTDQQNET LSVLVPKSMI NKEKIARGVC VIRGSVKANV SNALVVYPPK SLFPEQLTAI
RVLQLGSGLA VCPADMHVLY LSTLCDNDDQ GIKALLSAMS NLISLPVPEN RQSDSVVEND
TSETKPILLW RALYVQELVK GEFGGTISSM PSPDGNLNYN EIVESAVKLY EKLMGSEELF
KEETSPAENT TEEENDGGVE IED
