RAF2B_ARATH
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 03-AUG-2022, entry version 153.
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},
GN RAB5B {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}.
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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.AT4G19640.1; -.
DR PaxDb; Q9SN68; -.
DR PRIDE; Q9SN68; -.
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; locus:2123010; AT4G19640.
DR eggNOG; KOG0092; Eukaryota.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q9SN68; -.
DR OMA; YVKGQFF; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q9SN68; -.
DR EvolutionaryTrace; Q9SN68; -.
DR PRO; PR:Q9SN68; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SN68; baseline and differential.
DR Genevisible; Q9SN68; AT.
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:0030139; C:endocytic vesicle; IBA:GO_Central.
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; 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:0007033; P:vacuole organization; IMP:UniProtKB.
DR DisProt; DP02962; -.
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 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
