YPT7_YEAST
ID YPT7_YEAST Reviewed; 208 AA.
AC P32939; D6VZH4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Ypt/Rab-type GTPase YPT7;
DE AltName: Full=Vacuolar morphology protein 4 {ECO:0000303|PubMed:1526998};
GN Name=YPT7; Synonyms=VAM4 {ECO:0000303|PubMed:1526998};
GN OrderedLocusNames=YML001W {ECO:0000312|SGD:S000004460}; ORFNames=YM8270.02;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1473149; DOI=10.1016/s0092-8674(05)80062-5;
RA Wichmann H., Hengst L., Gallwitz D.;
RT "Endocytosis in yeast: evidence for the involvement of a small GTP-binding
RT protein (Ypt7p).";
RL Cell 71:1131-1142(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-22 AND GLN-68.
RC STRAIN=ATCC 26786 / X2180-1A;
RX DOI=10.1007/BF01281810;
RA Wada Y., Ohsumi Y., Kawai A., Ohsumi M.;
RT "Mutational analysis of Vam4/Ypt7p function in the vacuolar biogenesis and
RT morphogenesis in the yeast, Saccharomyces cerevisiae.";
RL Protoplasma 191:126-135(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP GENE FAMILY.
RX PubMed=1526998; DOI=10.1016/s0021-9258(19)37012-7;
RA Wada Y., Ohsumi Y., Anraku Y.;
RT "Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. I.
RT Isolation and characterization of two classes of vam mutants.";
RL J. Biol. Chem. 267:18665-18670(1992).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8308065; DOI=10.1242/jcs.106.3.823;
RA Schimmoeller F., Riezman H.;
RT "Involvement of Ypt7p, a small GTPase, in traffic from late endosome to the
RT vacuole in yeast.";
RL J. Cell Sci. 106:823-830(1993).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7489715; DOI=10.1002/j.1460-2075.1995.tb00210.x;
RA Haas A., Schegelmann D., Lazar T., Gallwitz D., Wickner W.;
RT "The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner
RT vacuoles for the homotypic fusion step of vacuole inheritance.";
RL EMBO J. 14:5258-5270(1995).
RN [8]
RP FUNCTION.
RX PubMed=11118206; DOI=10.1093/emboj/19.24.6713;
RA Eitzen G., Will E., Gallwitz D., Haas A., Wickner W.;
RT "Sequential action of two GTPases to promote vacuole docking and fusion.";
RL EMBO J. 19:6713-6720(2000).
RN [9]
RP FUNCTION.
RX PubMed=10725336; DOI=10.1083/jcb.148.6.1231;
RA Price A., Seals D., Wickner W., Ungermann C.;
RT "The docking stage of yeast vacuole fusion requires the transfer of
RT proteins from a cis-SNARE complex to a Rab/Ypt protein.";
RL J. Cell Biol. 148:1231-1238(2000).
RN [10]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11062257; DOI=10.1083/jcb.151.3.551;
RA Wurmser A.E., Sato T.K., Emr S.D.;
RT "New component of the vacuolar class C-Vps complex couples nucleotide
RT exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion.";
RL J. Cell Biol. 151:551-562(2000).
RN [11]
RP FUNCTION.
RX PubMed=10944212; DOI=10.1073/pnas.97.17.9402;
RA Seals D.F., Eitzen G., Margolis N., Wickner W.T., Price A.;
RT "A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required
RT for homotypic vacuole fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9402-9407(2000).
RN [12]
RP FUNCTION.
RX PubMed=11210571; DOI=10.1016/s0076-6879(01)29065-x;
RA Will E., Albert S., Gallwitz D.;
RT "Expression, purification, and biochemical properties of Ypt/Rab GTPase-
RT activating proteins of Gyp family.";
RL Methods Enzymol. 329:50-58(2001).
RN [13]
RP INTERACTION WITH GDI1.
RX PubMed=11785952; DOI=10.1006/bbrc.2001.6242;
RA Calero M., Collins R.N.;
RT "Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab
RT proteins.";
RL Biochem. Biophys. Res. Commun. 290:676-681(2002).
RN [14]
RP INTERACTION WITH IVY1.
RX PubMed=12553664; DOI=10.1078/0171-9335-00290;
RA Lazar T., Scheglmann D., Gallwitz D.;
RT "A novel phospholipid-binding protein from the yeast Saccharomyces
RT cerevisiae with dual binding specificities for the transport GTPase Ypt7p
RT and the Sec1-related Vps33p.";
RL Eur. J. Cell Biol. 81:635-646(2002).
RN [15]
RP INTERACTION WITH YIF1; YIP4 AND YIP5.
RX PubMed=11943201; DOI=10.1016/s0014-5793(02)02442-0;
RA Calero M., Winand N.J., Collins R.N.;
RT "Identification of the novel proteins Yip4p and Yip5p as Rab GTPase
RT interacting factors.";
RL FEBS Lett. 515:89-98(2002).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP FUNCTION.
RX PubMed=19386605; DOI=10.1074/jbc.m109.000737;
RA Hickey C.M., Stroupe C., Wickner W.;
RT "The major role of the Rab Ypt7p in vacuole fusion is supporting HOPS
RT membrane association.";
RL J. Biol. Chem. 284:16118-16125(2009).
RN [18]
RP ACTIVITY REGULATION.
RX PubMed=20797862; DOI=10.1016/j.cub.2010.08.002;
RA Nordmann M., Cabrera M., Perz A., Broecker C., Ostrowicz C.,
RA Engelbrecht-Vandre S., Ungermann C.;
RT "The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog
RT Ypt7.";
RL Curr. Biol. 20:1654-1659(2010).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21062894; DOI=10.1242/jcs.071977;
RA Balderhaar H.J., Arlt H., Ostrowicz C., Broecker C., Suendermann F.,
RA Brandt R., Babst M., Ungermann C.;
RT "The Rab GTPase Ypt7 is linked to retromer-mediated receptor recycling and
RT fusion at the yeast late endosome.";
RL J. Cell Sci. 123:4085-4094(2010).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22593205; DOI=10.1091/mbc.e11-11-0915;
RA Liu T.T., Gomez T.S., Sackey B.K., Billadeau D.D., Burd C.G.;
RT "Rab GTPase regulation of retromer-mediated cargo export during endosome
RT maturation.";
RL Mol. Biol. Cell 23:2505-2515(2012).
RN [21]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-147, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [22]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VPS39.
RX PubMed=25026035; DOI=10.1016/j.devcel.2014.06.006;
RA Hoenscher C., Mari M., Auffarth K., Bohnert M., Griffith J., Geerts W.,
RA van der Laan M., Cabrera M., Reggiori F., Ungermann C.;
RT "Cellular metabolism regulates contact sites between vacuoles and
RT mitochondria.";
RL Dev. Cell 30:86-94(2014).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-182 IN COMPLEX WITH GTP.
RX PubMed=11937061; DOI=10.1016/s0969-2126(02)00737-2;
RA Constantinescu A.T., Rak A., Alexandrov K., Esters H., Goody R.S.,
RA Scheidig A.J.;
RT "Rab-subfamily-specific regions of Ypt7p are structurally different from
RT other RabGTPases.";
RL Structure 10:569-579(2002).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-182 IN COMPLEX WITH GTP.
RX PubMed=26178622; DOI=10.1038/ncomms8773;
RA Wiegandt D., Vieweg S., Hofmann F., Koch D., Li F., Wu Y.W., Itzen A.,
RA Mueller M.P., Goody R.S.;
RT "Locking GTPases covalently in their functional states.";
RL Nat. Commun. 6:7773-7773(2015).
CC -!- FUNCTION: Ypt/Rab-type GTPases are key regulators of membrane
CC trafficking and intracellular vesicular transport. They act as
CC molecular switches that convert between GTP-bound and GDP-bound states,
CC and regulate virtually all steps of membrane traffic from the formation
CC of the transport vesicle at the donor membrane to its fusion at the
CC target membrane. In the GDP-bound state, Ypt proteins are predominantly
CC cytosolic, solubilized through the interaction with a GDP dissociation
CC inhibitor (GDI). In the GTP-bound state, the proteins are membrane
CC bound and interact with specific effector proteins that select cargo,
CC promote vesicle movement, or verify the correct site of fusion
CC (Probable). YPT7 is involved in regulation of vesicular protein
CC transport in exo- and endocytosis (PubMed:8308065). Involved in
CC homotypic vacuole fusion, the last step in the vacuole inheritance
CC process, by interacting in its GTP-bound state on the donor membrane
CC with the large multiprotein tethering complex termed HOPS on the
CC acceptor membrane (PubMed:7489715, PubMed:11118206, PubMed:10725336,
CC PubMed:10944212, PubMed:11210571, PubMed:19386605). Involved in the
CC regulation of transport steps from late endosomes to the vacuole,
CC mediated by interaction in its GTP-bound state on the donor membrane
CC with the large multiprotein tethering complex termed class C-Vps
CC complex on the acceptor membrane (PubMed:8308065, PubMed:11062257,
CC PubMed:21062894). Involved in retromer assembly and cargo export,
CC recognizing the cargo selection complex (CSC). GTP-bound YPT7 recruits
CC CSC to vacuolar membranes via retromer subunit VPS35 (PubMed:22593205).
CC Interacts with the HOPS complex subunit VPS39 independent of the HOPS
CC complex at mitochondria-vacuole contact sites (vCLAMPs), providing a
CC physical and metabolic interconnection between the endocytic pathway
CC and mitochondria (PubMed:25026035). {ECO:0000269|PubMed:10725336,
CC ECO:0000269|PubMed:10944212, ECO:0000269|PubMed:11062257,
CC ECO:0000269|PubMed:11118206, ECO:0000269|PubMed:11210571,
CC ECO:0000269|PubMed:19386605, ECO:0000269|PubMed:21062894,
CC ECO:0000269|PubMed:22593205, ECO:0000269|PubMed:25026035,
CC ECO:0000269|PubMed:7489715, ECO:0000269|PubMed:8308065, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). YPT7 is
CC activated by GEFs MON1-CCZ1 complex (MC1) and VAM6/VPS39, and
CC inactivated by GAPs GYP7 and GYP1. {ECO:0000269|PubMed:11062257,
CC ECO:0000269|PubMed:11210571, ECO:0000269|PubMed:19386605,
CC ECO:0000269|PubMed:20797862, ECO:0000269|PubMed:22593205}.
CC -!- SUBUNIT: Interacts with IVY1 (PubMed:12553664). Interacts with YIF1,
CC YIP4 and YIP5 (PubMed:11943201). Interacts with the HOPS complex
CC (PubMed:10944212, PubMed:19386605). Interacts with the class C-Vps
CC complex (PubMed:11062257). Interacts with VPS35 (PubMed:22593205).
CC Interacts with VPS39 (PubMed:25026035). Interacts with the GDP
CC dissociation inhibitor GDI1 (PubMed:11118206, PubMed:11785952).
CC {ECO:0000269|PubMed:10944212, ECO:0000269|PubMed:11062257,
CC ECO:0000269|PubMed:11118206, ECO:0000269|PubMed:11785952,
CC ECO:0000269|PubMed:11943201, ECO:0000269|PubMed:12553664,
CC ECO:0000269|PubMed:19386605, ECO:0000269|PubMed:22593205,
CC ECO:0000269|PubMed:25026035}.
CC -!- INTERACTION:
CC P32939; P39958: GDI1; NbExp=3; IntAct=EBI-29509, EBI-7517;
CC P32939; Q04934: IVY1; NbExp=3; IntAct=EBI-29509, EBI-35255;
CC P32939; P53845: YIF1; NbExp=2; IntAct=EBI-29509, EBI-28230;
CC P32939; P53093: YIP4; NbExp=2; IntAct=EBI-29509, EBI-24124;
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:21062894}.
CC Vacuole membrane {ECO:0000269|PubMed:22593205,
CC ECO:0000269|PubMed:7489715}. Note=Localizes to sites of contact between
CC the vacuole and mitochondria (vCLAMPs). {ECO:0000269|PubMed:25026035}.
CC -!- DISRUPTION PHENOTYPE: Endocytosed alpha-factor accumulates in late
CC endosomes. {ECO:0000269|PubMed:8308065}.
CC -!- MISCELLANEOUS: Present with 5530 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X68144; CAA48244.1; -; Genomic_DNA.
DR EMBL; D64114; BAA10973.1; -; Genomic_DNA.
DR EMBL; Z48613; CAA88515.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09898.1; -; Genomic_DNA.
DR PIR; A44334; A44334.
DR RefSeq; NP_013713.1; NM_001182356.1.
DR PDB; 1KY2; X-ray; 1.60 A; A=1-182.
DR PDB; 1KY3; X-ray; 1.35 A; A=1-182.
DR PDB; 4PHF; X-ray; 1.95 A; A=1-182.
DR PDB; 4PHG; X-ray; 1.90 A; A=1-182.
DR PDB; 4PHH; X-ray; 2.35 A; A/B/C/D=1-182.
DR PDBsum; 1KY2; -.
DR PDBsum; 1KY3; -.
DR PDBsum; 4PHF; -.
DR PDBsum; 4PHG; -.
DR PDBsum; 4PHH; -.
DR AlphaFoldDB; P32939; -.
DR SMR; P32939; -.
DR BioGRID; 35170; 488.
DR DIP; DIP-1735N; -.
DR IntAct; P32939; 19.
DR MINT; P32939; -.
DR STRING; 4932.YML001W; -.
DR TCDB; 9.A.63.1.1; the retromer-dependent vacuolar protein sorting (r-vps) family.
DR iPTMnet; P32939; -.
DR MaxQB; P32939; -.
DR PaxDb; P32939; -.
DR PRIDE; P32939; -.
DR TopDownProteomics; P32939; -.
DR EnsemblFungi; YML001W_mRNA; YML001W; YML001W.
DR GeneID; 855012; -.
DR KEGG; sce:YML001W; -.
DR SGD; S000004460; YPT7.
DR VEuPathDB; FungiDB:YML001W; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000166196; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; P32939; -.
DR OMA; IQACPRD; -.
DR BioCyc; YEAST:G3O-32607-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8854214; TBC/RABGAPs.
DR Reactome; R-SCE-8873719; RAB geranylgeranylation.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR EvolutionaryTrace; P32939; -.
DR PRO; PR:P32939; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32939; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0045335; C:phagocytic vesicle; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0072665; P:protein localization to vacuole; IMP:SGD.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IDA:SGD.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IMP:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IPI:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IDA:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:SGD.
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; Endosome; GTP-binding; Isopeptide bond; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport; Ubl conjugation; Vacuole.
FT CHAIN 1..208
FT /note="Ypt/Rab-type GTPase YPT7"
FT /id="PRO_0000121320"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 17..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1KY2, ECO:0007744|PDB:1KY3,
FT ECO:0007744|PDB:4PHF, ECO:0007744|PDB:4PHG"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1KY2, ECO:0007744|PDB:1KY3,
FT ECO:0007744|PDB:4PHF, ECO:0007744|PDB:4PHG"
FT BINDING 67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1KY2, ECO:0007744|PDB:4PHG"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1KY2, ECO:0007744|PDB:1KY3,
FT ECO:0007744|PDB:4PHF, ECO:0007744|PDB:4PHG"
FT BINDING 158..160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1KY2, ECO:0007744|PDB:1KY3,
FT ECO:0007744|PDB:4PHF, ECO:0007744|PDB:4PHG"
FT MOD_RES 208
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P36586"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P36586"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P36586"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 22
FT /note="T->N: Constitutively in the GDP-bound conformation.
FT Causes loss of function during vacuolar morphogenesis."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 68
FT /note="Q->L: Constitutively in the GTP-bound conformation.
FT Complements the fragmented vacuolar morphology of ypt7 null
FT mutant cells."
FT /evidence="ECO:0000269|Ref.2"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:1KY3"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1KY3"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1KY3"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1KY3"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1KY3"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1KY2"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:1KY2"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1KY2"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1KY3"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:1KY3"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1KY3"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1KY3"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1KY3"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1KY3"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:1KY3"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1KY3"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:1KY3"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:1KY3"
SQ SEQUENCE 208 AA; 23043 MW; 0E2B72BDA7F7CEE5 CRC64;
MSSRKKNILK VIILGDSGVG KTSLMHRYVN DKYSQQYKAT IGADFLTKEV TVDGDKVATM
QVWDTAGQER FQSLGVAFYR GADCCVLVYD VTNASSFENI KSWRDEFLVH ANVNSPETFP
FVILGNKIDA EESKKIVSEK SAQELAKSLG DIPLFLTSAK NAINVDTAFE EIARSALQQN
QADTEAFEDD YNDAINIRLD GENNSCSC
