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 02-DEC-2020, entry version 141. 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}. 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; 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 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; DGDNCAC; -. 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; IDA:TAIR. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA: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 InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR Pfam; PF00071; Ras; 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 NP_BIND 15..23 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9SN68" FT NP_BIND 63..67 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9SN68" FT NP_BIND 125..128 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9SN68" FT NP_BIND 158..159 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9SN68" FT MOTIF 37..45 FT /note="Effector region" FT /evidence="ECO:0000250" 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 //