ID RAF2B_ARATH Reviewed; 200 AA. AC Q9SN68; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 160. DE RecName: Full=Ras-related protein RABF2b {ECO:0000303|PubMed:12644670}; DE Short=AtRABF2b {ECO:0000303|PubMed:12644670}; DE AltName: Full=Ras-related protein Ara-7 {ECO:0000303|PubMed:11532937}; DE AltName: Full=Ras-related protein Rab5B {ECO:0000305|PubMed:12644670}; DE Short=AtRab5B {ECO:0000305|PubMed:12644670}; GN Name=RABF2B {ECO:0000303|PubMed:12644670}; GN Synonyms=ARA-7 {ECO:0000303|PubMed:11532937}, RAB5B GN {ECO:0000305|PubMed:12644670}; GN OrderedLocusNames=At4g19640 {ECO:0000312|Araport:AT4G19640}; GN ORFNames=F24J7.190 {ECO:0000312|EMBL:CAA16940.1}; 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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF GLN-69. RX PubMed=11532937; DOI=10.1093/emboj/20.17.4730; RA Ueda T., Yamaguchi M., Uchimiya H., Nakano A.; RT "Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic RT pathway of Arabidopsis thaliana."; RL EMBO J. 20:4730-4741(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). 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 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 SUBCELLULAR LOCATION. RX PubMed=15509844; DOI=10.1093/pcp/pch142; RA Lee G.J., Sohn E.J., Lee M.H., Hwang I.; RT "The Arabidopsis rab5 homologs rha1 and ara7 localize to the prevacuolar RT compartment."; RL Plant Cell Physiol. 45:1211-1220(2004). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=15608333; DOI=10.1105/tpc.104.027821; RA Haupt S., Cowan G.H., Ziegler A., Roberts A.G., Oparka K.J., Torrance L.; RT "Two plant-viral movement proteins traffic in the endocytic recycling RT pathway."; RL Plant Cell 17:164-181(2005). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16103374; DOI=10.1073/pnas.0502060102; RA Takano J., Miwa K., Yuan L., von Wiren N., Fujiwara T.; RT "Endocytosis and degradation of BOR1, a boron transporter of Arabidopsis RT thaliana, regulated by boron availability."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12276-12281(2005). RN [9] RP INTERACTION WITH VPS9A, AND INDUCTION. RX PubMed=18055610; DOI=10.1105/tpc.107.053876; RA Goh T., Uchida W., Arakawa S., Ito E., Dainobu T., Ebine K., Takeuchi M., RA Sato K., Ueda T., Nakano A.; RT "VPS9a, the common activator for two distinct types of Rab5 GTPases, is RT essential for the development of Arabidopsis thaliana."; RL Plant Cell 19:3504-3515(2007). RN [10] RP DEVELOPMENTAL STAGE. RX PubMed=18775970; DOI=10.1104/pp.108.126375; RA Wang Y., Zhang W.Z., Song L.F., Zou J.J., Su Z., Wu W.H.; RT "Transcriptome analyses show changes in gene expression to accompany pollen RT germination and tube growth in Arabidopsis."; RL Plant Physiol. 148:1201-1211(2008). RN [11] RP INTERACTION WITH TCTP1. RX PubMed=20736351; DOI=10.1073/pnas.1007926107; RA Brioudes F., Thierry A.M., Chambrier P., Mollereau B., Bendahmane M.; RT "Translationally controlled tumor protein is a conserved mitotic growth RT integrator in animals and plants."; RL Proc. Natl. Acad. Sci. U.S.A. 107:16384-16389(2010). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23682115; DOI=10.1093/jxb/ert125; RA Jia T., Gao C., Cui Y., Wang J., Ding Y., Cai Y., Ueda T., Nakano A., RA Jiang L.; RT "ARA7(Q69L) expression in transgenic Arabidopsis cells induces the RT formation of enlarged multivesicular bodies."; RL J. Exp. Bot. 64:2817-2829(2013). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=23482856; DOI=10.1105/tpc.112.108829; RA Zhou L.Z., Li S., Feng Q.N., Zhang Y.L., Zhao X., Zeng Y.L., Wang H., RA Jiang L., Zhang Y.; RT "Protein S-acyl transferase10 is critical for development and salt RT tolerance in Arabidopsis."; RL Plant Cell 25:1093-1107(2013). RN [14] RP FUNCTION, INTERACTION WITH MON1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP SER-24. 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 [15] RP FUNCTION, INTERACTION WITH EREX, AND MUTAGENESIS OF SER-24. RX PubMed=27288222; DOI=10.1105/tpc.16.00326; RA Sakurai H.T., Inoue T., Nakano A., Ueda T.; RT "ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an interacting partner of RAB5 RT GTPases, regulates membrane trafficking to protein storage vacuoles in RT Arabidopsis."; RL Plant Cell 28:1490-1503(2016). RN [16] RP SUBCELLULAR LOCATION, AND INTERACTION WITH VPS3. 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). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-179 IN COMPLEX WITH GDP, RP INTERACTION WITH VPS9A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-19; RP SER-24; VAL-36; THR-42; GLY-44; ALA-46; PHE-47; TRP-64; ALA-67; GLN-69; RP SER-74; LEU-75; MET-78; TYR-79 AND ASN-123. RX PubMed=20833725; DOI=10.1074/jbc.m110.152132; RA Uejima T., Ihara K., Goh T., Ito E., Sunada M., Ueda T., Nakano A., RA Wakatsuki S.; RT "GDP-bound and nucleotide-free intermediates of the guanine nucleotide RT exchange in the Rab5.Vps9 system."; RL J. Biol. Chem. 285:36689-36697(2010). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-179. RX PubMed=23519409; DOI=10.1107/s0907444912047294; RA Uejima T., Ihara K., Sunada M., Kawasaki M., Ueda T., Kato R., Nakano A., RA Wakatsuki S.; RT "Direct metal recognition by guanine nucleotide-exchange factor in the RT initial step of the exchange reaction."; RL Acta Crystallogr. D 69:345-351(2013). CC -!- FUNCTION: Endosomal protein that may be involved in endocytosis CC (PubMed:16103374). Involved in the trafficking of proteins from CC prevacuolar compartments (PVCs) to vacuoles (PubMed:23682115, CC PubMed:24824487). May activate the MON1-CCZ1 complex which acts as CC guanine nucleotide exchange factors (GEF) for Rab7 protein family, and CC serves as a link between Rab5 and Rab7 families in PVCs, and mediates CC PVC maturation (PubMed:24824487). Involved in vacuolar transport of CC storage proteins with EREX as effector. Regulates membrane trafficking CC to protein storage vacuoles (PSVs) (PubMed:27288222). CC {ECO:0000269|PubMed:16103374, ECO:0000269|PubMed:23682115, CC ECO:0000269|PubMed:24824487, ECO:0000269|PubMed:27288222}. CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) which promote the exchange of bound GDP for free GTP. CC {ECO:0000305|PubMed:24824487}. CC -!- SUBUNIT: Interacts with VPS9A homodimer (PubMed:18055610, CC PubMed:20833725). Interacts with TCTP1 (PubMed:20736351). Interacts CC with MON1 (PubMed:24824487). Interacts with EREX (via PX domain) CC (PubMed:27288222). Binds to VPS3 (PubMed:29463724). CC {ECO:0000269|PubMed:18055610, ECO:0000269|PubMed:20736351, CC ECO:0000269|PubMed:20833725, ECO:0000269|PubMed:24824487, CC ECO:0000269|PubMed:27288222, ECO:0000269|PubMed:29463724}. CC -!- SUBCELLULAR LOCATION: Early endosome membrane CC {ECO:0000269|PubMed:11532937, ECO:0000269|PubMed:23482856}; Lipid- CC anchor {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:15608333, CC ECO:0000269|PubMed:16103374, ECO:0000269|PubMed:24824487}; Lipid-anchor CC {ECO:0000305}. Prevacuolar compartment membrane CC {ECO:0000269|PubMed:15509844, ECO:0000269|PubMed:24824487}; Lipid- CC anchor {ECO:0000305}. Endosome, multivesicular body membrane CC {ECO:0000269|PubMed:23682115}; Lipid-anchor {ECO:0000305}. Cell CC membrane {ECO:0000305|PubMed:23519409}; Lipid-anchor {ECO:0000305}. CC Cytoplasm {ECO:0000269|PubMed:29463724}. Note=Strong co-localization CC with VPS3 and VPS18 in cytoplasmic puncta. CC {ECO:0000269|PubMed:29463724}. CC -!- TISSUE SPECIFICITY: Expressed in roots and actively dividing cells. CC {ECO:0000269|PubMed:11532937}. CC -!- DEVELOPMENTAL STAGE: Expressed during pollen germination and pollen CC tube growth. {ECO:0000269|PubMed:18775970}. CC -!- INDUCTION: Activated by VPS9A. {ECO:0000269|PubMed:18055610}. CC -!- MISCELLANEOUS: Over-expression of the constitutively active GTP-bound CC mutant of Leu-69 induces the formation of large ring-like structures of CC 1-2 micrometers in diameter. {ECO:0000269|PubMed:23682115}. 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; AB038491; BAB32669.1; -; mRNA. DR EMBL; AL021768; CAA16940.1; -; Genomic_DNA. DR EMBL; AL161551; CAB78966.1; -; Genomic_DNA. DR EMBL; CP002687; AEE84207.1; -; Genomic_DNA. DR EMBL; AF370309; AAK44124.1; -; mRNA. DR EMBL; AY052670; AAK96574.1; -; mRNA. DR EMBL; AY063095; AAL34269.1; -; mRNA. DR PIR; T06157; T06157. DR RefSeq; NP_193699.1; NM_118084.5. DR PDB; 2EFC; X-ray; 2.09 A; B/D=1-179. DR PDB; 2EFD; X-ray; 3.00 A; B/D=1-179. DR PDB; 2EFE; X-ray; 2.08 A; B/D=1-179. DR PDB; 2EFH; X-ray; 2.10 A; B/D=1-179. DR PDB; 4G01; X-ray; 2.20 A; B=1-179. DR PDBsum; 2EFC; -. DR PDBsum; 2EFD; -. DR PDBsum; 2EFE; -. DR PDBsum; 2EFH; -. DR PDBsum; 4G01; -. DR AlphaFoldDB; Q9SN68; -. DR SMR; Q9SN68; -. DR BioGRID; 12999; 1. DR IntAct; Q9SN68; 2. DR STRING; 3702.Q9SN68; -. DR PaxDb; 3702-AT4G19640-1; -. DR ProteomicsDB; 225957; -. DR EnsemblPlants; AT4G19640.1; AT4G19640.1; AT4G19640. DR GeneID; 827706; -. DR Gramene; AT4G19640.1; AT4G19640.1; AT4G19640. DR KEGG; ath:AT4G19640; -. DR Araport; AT4G19640; -. DR TAIR; AT4G19640; ARA7. DR eggNOG; KOG0092; Eukaryota. DR HOGENOM; CLU_041217_10_2_1; -. DR InParanoid; Q9SN68; -. DR OMA; QSTRACC; -. DR OrthoDB; 5483572at2759; -. DR PhylomeDB; Q9SN68; -. DR EvolutionaryTrace; Q9SN68; -. DR PRO; PR:Q9SN68; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q9SN68; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR. DR GO; GO:0005768; C:endosome; IDA:TAIR. DR GO; GO:0043229; C:intracellular organelle; IDA:TAIR. DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0140313; F:molecular sequestering activity; EXP:DisProt. DR GO; GO:0036094; F:small molecule binding; EXP:DisProt. 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 CDD; cd01860; Rab5_related; 1. DR DisProt; DP02962; -. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47978; -; 1. DR PANTHER; PTHR47978:SF47; RAB FAMILY GTPASE; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. DR Genevisible; Q9SN68; AT. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cytoplasm; Endosome; GTP-binding; Lipoprotein; KW Membrane; Nucleotide-binding; Prenylation; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..200 FT /note="Ras-related protein RABF2b" FT /id="PRO_0000406605" FT MOTIF 39..47 FT /note="Effector region" FT /evidence="ECO:0000250" FT BINDING 17..25 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20833725, FT ECO:0007744|PDB:2EFC, ECO:0007744|PDB:2EFH" FT BINDING 65..69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20833725, FT ECO:0007744|PDB:2EFC, ECO:0007744|PDB:2EFH" FT BINDING 123..126 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20833725, FT ECO:0007744|PDB:2EFC, ECO:0007744|PDB:2EFH" FT BINDING 153..154 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20833725, FT ECO:0007744|PDB:2EFC, ECO:0007744|PDB:2EFH" FT LIPID 198 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT LIPID 199 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT MUTAGEN 19 FT /note="V->T: Loss of interaction with VPS9A. Loss of FT interaction with MON1. Loss of interaction with EREX." FT /evidence="ECO:0000269|PubMed:20833725, FT ECO:0000269|PubMed:24824487, ECO:0000269|PubMed:27288222" FT MUTAGEN 24 FT /note="S->N: Dominant negative (GDP-bound form); no effect FT on the interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 36 FT /note="V->P: No effect on the interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 42 FT /note="T->A: No effect on the interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 44 FT /note="G->P: No effect on the interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 46 FT /note="A->D: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 47 FT /note="F->A: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 64 FT /note="W->A: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 67 FT /note="A->G: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 69 FT /note="Q->E: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:11532937, FT ECO:0000269|PubMed:20833725" FT MUTAGEN 69 FT /note="Q->L: Constitutively active (GTP-bound form); loss FT of targeting to plasma membrane and interaction with FT VPS9A." FT /evidence="ECO:0000269|PubMed:11532937, FT ECO:0000269|PubMed:20833725" FT MUTAGEN 74 FT /note="S->A: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 75 FT /note="L->A: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 78 FT /note="M->A: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 79 FT /note="Y->A: Loss of interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT MUTAGEN 123 FT /note="N->I: Blocks nucleotide binding; no effect on the FT interaction with VPS9A." FT /evidence="ECO:0000269|PubMed:20833725" FT STRAND 9..16 FT /evidence="ECO:0007829|PDB:2EFE" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:2EFE" FT TURN 36..38 FT /evidence="ECO:0007829|PDB:2EFE" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:4G01" FT STRAND 46..54 FT /evidence="ECO:0007829|PDB:2EFE" FT STRAND 57..65 FT /evidence="ECO:0007829|PDB:2EFE" FT HELIX 70..76 FT /evidence="ECO:0007829|PDB:2EFE" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:2EFE" FT STRAND 84..91 FT /evidence="ECO:0007829|PDB:2EFE" FT HELIX 95..111 FT /evidence="ECO:0007829|PDB:2EFE" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:2EFE" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:2EFE" FT HELIX 135..144 FT /evidence="ECO:0007829|PDB:2EFE" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:2EFE" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:2EFE" FT HELIX 160..169 FT /evidence="ECO:0007829|PDB:2EFE" SQ SEQUENCE 200 AA; 21873 MW; 769F75CFC708C6D0 CRC64; MAAAGNKSIN AKLVLLGDVG AGKSSLVLRF VKDQFVEFQE STIGAAFFSQ TLAVNDATVK FEIWDTAGQE RYHSLAPMYY RGAAAAIIVF DVTNQASFER AKKWVQELQA QGNPNMVMAL AGNKSDLLDA RKVTAEDAQT YAQENGLFFM ETSAKTATNV KEIFYEIARR LPRVQPTENP TGMVLPDRAM DRAVSSSCCA //