RAG3F_ARATH
ID RAG3F_ARATH Reviewed; 206 AA.
AC Q9LS94; Q8LGH5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ras-related protein RABG3f;
DE Short=AtRABG3f;
DE AltName: Full=Ras-related protein Rab71;
DE Short=AtRab71;
DE AltName: Full=Ras-related protein Rab7B;
DE Short=AtRab7B;
GN Name=RABG3F; Synonyms=RAB71, RAB7B; OrderedLocusNames=At3g18820;
GN ORFNames=MVE11.21;
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].
RA Ueda T., Wada Y., Nakano A.;
RT "Rab7 homologs in Arabidopsis thaliana.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 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 FUNCTION, INTERACTION WITH VPS35A, AND SUBCELLULAR LOCATION.
RX PubMed=23362252; DOI=10.1074/jbc.m112.440503;
RA Zelazny E., Santambrogio M., Pourcher M., Chambrier P., Berne-Dedieu A.,
RA Fobis-Loisy I., Miege C., Jaillais Y., Gaude T.;
RT "Mechanisms governing the endosomal membrane recruitment of the core
RT retromer in Arabidopsis.";
RL J. Biol. Chem. 288:8815-8825(2013).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-22 AND GLN-67.
RX PubMed=24824487; DOI=10.1105/tpc.114.123141;
RA Cui Y., Zhao Q., Gao C., Ding Y., Zeng Y., Ueda T., Nakano A., Jiang L.;
RT "Activation of the Rab7 GTPase by the MON1-CCZ1 complex is essential for
RT PVC-to-vacuole trafficking and plant growth in Arabidopsis.";
RL Plant Cell 26:2080-2097(2014).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=29463724; DOI=10.1073/pnas.1717839115;
RA Takemoto K., Ebine K., Askani J.C., Krueger F., Gonzalez Z.A., Ito E.,
RA Goh T., Schumacher K., Nakano A., Ueda T.;
RT "Distinct sets of tethering complexes, SNARE complexes, and Rab GTPases
RT mediate membrane fusion at the vacuole in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2457-E2466(2018).
CC -!- FUNCTION: Essential for trafficking from prevacuolar compartments to
CC vacuoles. Involved in the trafficking of newly synthesized protein to
CC vacuoles. Essential for plant growth (PubMed:24824487). Participates in
CC the recruitment of the core retromer components to the endosomal
CC membrane by interacting with VPS35A (PubMed:23362252).
CC {ECO:0000269|PubMed:23362252, ECO:0000269|PubMed:24824487}.
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP. Regulated
CC by the MON1-CCZ1 complex which serves as a link between Rab5 and Rab7
CC protein families in PVCs and mediates PVC maturation.
CC {ECO:0000269|PubMed:24824487}.
CC -!- SUBUNIT: Interacts with VPS35A. {ECO:0000269|PubMed:23362252}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:23362252,
CC ECO:0000269|PubMed:24824487}; Lipid-anchor {ECO:0000305}. Vacuole
CC membrane {ECO:0000269|PubMed:24824487, ECO:0000269|PubMed:29463724};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Prevacuolar
CC compartment membrane {ECO:0000269|PubMed:24824487}; Lipid-anchor
CC {ECO:0000305}. Note=Partial co-localization with VPS3 at cytoplasmic
CC punctate structures, and with VPS39 at subdomains of the vacuolar
CC membrane. Co-localizes with VPS18. {ECO:0000269|PubMed:29463724}.
CC -!- MISCELLANEOUS: Over-expression of a dominant negative form of RABG3F
CC (Asn-22) inhibits degradation of storage proteins in the protein
CC storage vacuole and results in seedling death.
CC {ECO:0000269|PubMed:24824487}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB071846; BAB68371.1; -; mRNA.
DR EMBL; AB026654; BAB01810.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76152.1; -; Genomic_DNA.
DR EMBL; AY035137; AAK59641.1; -; mRNA.
DR EMBL; AY059072; AAL15178.1; -; mRNA.
DR EMBL; AY084266; AAM60858.1; -; mRNA.
DR RefSeq; NP_188512.1; NM_112768.3.
DR AlphaFoldDB; Q9LS94; -.
DR SMR; Q9LS94; -.
DR STRING; 3702.AT3G18820.1; -.
DR PaxDb; Q9LS94; -.
DR PRIDE; Q9LS94; -.
DR ProteomicsDB; 236405; -.
DR EnsemblPlants; AT3G18820.1; AT3G18820.1; AT3G18820.
DR GeneID; 821415; -.
DR Gramene; AT3G18820.1; AT3G18820.1; AT3G18820.
DR KEGG; ath:AT3G18820; -.
DR Araport; AT3G18820; -.
DR TAIR; locus:2094029; AT3G18820.
DR eggNOG; KOG0394; Eukaryota.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q9LS94; -.
DR OMA; KAMQHET; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; Q9LS94; -.
DR PRO; PR:Q9LS94; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LS94; baseline and differential.
DR Genevisible; Q9LS94; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB.
DR GO; GO:0007033; P:vacuole organization; IMP:UniProtKB.
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 Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..206
FT /note="Ras-related protein RABG3f"
FT /id="PRO_0000407366"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9SN68"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9SN68"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9SN68"
FT BINDING 158..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9SN68"
FT MOD_RES 206
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 22
FT /note="T->N: Dominant negative (GDP-bound form); loss of
FT targeting to the prevacuolar compartments and tonoplast.
FT Inhibits vacuolar trafficking and forms enlarged
FT prevacuolar compartments. Inhibits degradation of storage
FT proteins in the protein storage vacuole resulting in
FT seedling death."
FT /evidence="ECO:0000269|PubMed:24824487"
FT MUTAGEN 67
FT /note="Q->L: Constitutively active form (GTP-bound form);
FT targets almost exclusively to tonoplast."
FT /evidence="ECO:0000269|PubMed:24824487"
FT CONFLICT 102
FT /note="W -> R (in Ref. 5; AAM60858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 23102 MW; 30D5020AEF6E44D0 CRC64;
MPSRRRTLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV QFEDRLFTLQ
IWDTAGQERF QSLGVAFYRG ADCCVLVYDV NSMKSFENLN NWREEFLIQA SPSDPENFPF
VLIGNKVDVD DGNSRVVSEK KAKAWCASKG NIPYFETSAK VGTNVEEAFQ CIAKDALKSG
EEEELYLPDT IDVGTSNQQR STGCEC
