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 08-MAY-2019, entry version 131. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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 RT reference 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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., RA Berne-Dedieu A., 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 RP OF 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., RA Jiang L.; RT "Activation of the Rab7 GTPase by the MON1-CCZ1 complex is essential RT for 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 RT GTPases 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 CC to vacuoles. Involved in the trafficking of newly synthesized CC protein to vacuoles. Essential for plant growth (PubMed:24824487). CC Participates in the recruitment of the core retromer components to CC the endosomal membrane by interacting with VPS35A CC (PubMed:23362252). {ECO:0000269|PubMed:23362252, CC ECO:0000269|PubMed:24824487}. CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange CC factors (GEFs) which promote the exchange of bound GDP for free CC GTP. Regulated by the MON1-CCZ1 complex which serves as a link CC between Rab5 and Rab7 protein families in PVCs and mediates PVC CC maturation. {ECO:0000269|PubMed:24824487}. CC -!- SUBUNIT: Interacts with VPS35A. {ECO:0000269|PubMed:23362252}. CC -!- SUBCELLULAR LOCATION: Endosome membrane CC {ECO:0000269|PubMed:23362252, ECO:0000269|PubMed:24824487}; Lipid- CC anchor {ECO:0000305}. Vacuole membrane CC {ECO:0000269|PubMed:24824487, ECO:0000269|PubMed:29463724}; Lipid- CC 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 CC cytoplasmic punctate structures, and with VPS39 at subdomains of CC the vacuolar membrane. Co-localizes with VPS18. CC {ECO:0000269|PubMed:29463724}. CC -!- MISCELLANEOUS: Over-expression of a dominant negative form of CC RABG3F (Asn-22) inhibits degradation of storage proteins in the CC protein 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 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 eggNOG; ENOG410XNZV; LUCA. DR HOGENOM; HOG000233968; -. DR InParanoid; Q9LS94; -. DR KO; K07897; -. DR OMA; DVTMPNT; -. 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: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; IBA:GO_Central. 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:0032482; P:Rab protein signal transduction; IBA:GO_Central. 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 Complete proteome; Endosome; GTP-binding; Lipoprotein; Membrane; KW Methylation; Nucleotide-binding; Prenylation; Protein transport; KW Reference proteome; Transport; Vacuole. FT CHAIN 1 206 Ras-related protein RABG3f. FT /FTId=PRO_0000407366. FT NP_BIND 15 23 GTP. {ECO:0000250|UniProtKB:Q9SN68}. FT NP_BIND 63 67 GTP. {ECO:0000250|UniProtKB:Q9SN68}. FT NP_BIND 125 128 GTP. {ECO:0000250|UniProtKB:Q9SN68}. FT NP_BIND 158 159 GTP. {ECO:0000250|UniProtKB:Q9SN68}. FT MOTIF 37 45 Effector region. {ECO:0000250}. FT MOD_RES 206 206 Cysteine methyl ester. {ECO:0000250}. FT LIPID 204 204 S-geranylgeranyl cysteine. {ECO:0000250}. FT LIPID 206 206 S-geranylgeranyl cysteine. {ECO:0000250}. FT MUTAGEN 22 22 T->N: Dominant negative (GDP-bound form); FT loss of targeting to the prevacuolar FT compartments and tonoplast. Inhibits FT vacuolar trafficking and forms enlarged FT prevacuolar compartments. Inhibits FT degradation of storage proteins in the FT protein storage vacuole resulting in FT seedling death. FT {ECO:0000269|PubMed:24824487}. FT MUTAGEN 67 67 Q->L: Constitutively active form (GTP- FT bound form); targets almost exclusively FT to tonoplast. FT {ECO:0000269|PubMed:24824487}. FT CONFLICT 102 102 W -> R (in Ref. 5; AAM60858). FT {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 //