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 02-SEP-2026, entry version 220. DE RecName: Full=Ypt/Rab-type GTPase YPT7; DE Short=Ypt7p {ECO:0000305}; 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}; GN 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; DOI=10.1038/387s090; 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, INTERACTION WITH CCZ1, MUTAGENESIS OF LYS-127; ASP-129; THR-157 RP AND ALA-159, AND CHARACTERIZATION OF THR-22 AND GLN-68. RX PubMed=11590240; DOI=10.1242/jcs.114.17.3137; RA Kucharczyk R., Kierzek A.M., Slonimski P.P., Rytka J.; RT "The Ccz1 protein interacts with Ypt7 GTPase during fusion of multiple RT transport intermediates with the vacuole in S. cerevisiae."; RL J. Cell Sci. 114:3137-3145(2001). RN [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] RP SUBCELLULAR LOCATION. RX PubMed=32391792; DOI=10.7554/elife.56090; RA Langemeyer L., Borchers A.C., Herrmann E., Fuellbrunn N., Han Y., Perz A., RA Auffarth K., Kuemmel D., Ungermann C.; RT "A conserved and regulated mechanism drives endosomal Rab transition."; RL Elife 9:0-0(2020). RN [25] RP SUBCELLULAR LOCATION. RX PubMed=37463208; DOI=10.1073/pnas.2303750120; RA Borchers A.C., Janz M., Schaefer J.H., Moeller A., Kuemmel D., Paululat A., RA Ungermann C., Langemeyer L.; RT "Regulatory sites in the Mon1-Ccz1 complex control Rab5 to Rab7 transition RT and endosome maturation."; RL Proc. Natl. Acad. Sci. U.S.A. 120:e2303750120-e2303750120(2023). RN [26] 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 [27] 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). Involved in regulation of vesicular protein transport in CC exo- and endocytosis (PubMed:8308065). Involved in regulation of late CC endosome to vacuole trafficking and homotypic vacuole fusion, by CC interacting in its GTP-bound state on the donor membrane with the large CC multiprotein HOPS/class C-Vps tethering complex on the acceptor CC membrane (PubMed:10725336, PubMed:10944212, PubMed:11062257, CC PubMed:11118206, PubMed:11210571, PubMed:11590240, PubMed:19386605, CC PubMed:21062894, PubMed:7489715, PubMed:8308065). Involved in retromer CC assembly and cargo export, recognizing the cargo selection complex CC (CSC). GTP-bound YPT7 recruits CSC to vacuolar membranes via retromer CC subunit VPS35 (PubMed:22593205). Interacts with the HOPS complex CC subunit VPS39 independent of the HOPS complex at mitochondria-vacuole CC contact sites (vCLAMPs), providing a physical and metabolic CC interconnection between the endocytic pathway and mitochondria CC (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:11590240, ECO:0000269|PubMed:19386605, CC ECO:0000269|PubMed:21062894, ECO:0000269|PubMed:22593205, CC ECO:0000269|PubMed:25026035, ECO:0000269|PubMed:7489715, CC 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 Interacts with CCZ1 (PubMed:11590240). {ECO:0000269|PubMed:10944212, CC ECO:0000269|PubMed:11062257, ECO:0000269|PubMed:11118206, CC ECO:0000269|PubMed:11590240, 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=4; 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:32391792, ECO:0000269|PubMed:37463208, CC ECO:0000269|PubMed:7489715}; Lipid-anchor {ECO:0000305}; Cytoplasmic CC side {ECO:0000305}. Note=Localizes to sites of contact between the CC vacuole and mitochondria (vCLAMPs). Vacuolar membrane localization CC requires the action of small GTPase Rab5 homologs such as YPT52, YPT10 CC or VPS21 (PubMed:32391792). {ECO:0000269|PubMed:25026035, CC ECO:0000269|PubMed:32391792}. 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}. 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; 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 AlphaFoldDB; P32939; -. DR SMR; P32939; -. DR BioGRID; 35170; 509. DR DIP; DIP-1735N; -. DR FunCoup; P32939; 1188. DR IntAct; P32939; 25. 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 PaxDb; 4932-YML001W; -. DR PeptideAtlas; P32939; -. DR TopDownProteomics; P32939; -. DR EnsemblFungi; YML001W_mRNA; YML001W; YML001W. DR GeneID; 855012; -. DR KEGG; sce:YML001W; -. DR AGR; SGD:S000004460; -. DR SGD; S000004460; YPT7. DR VEuPathDB; FungiDB:YML001W; -. DR eggNOG; KOG0394; Eukaryota. DR HOGENOM; CLU_041217_10_6_1; -. DR InParanoid; P32939; -. DR OMA; TSWKDEF; -. DR OrthoDB; 9989112at2759; -. DR BioCyc; YEAST:G3O-32607-MONOMER; -. 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-9013406; RHOQ GTPase cycle. DR BioGRID-ORCS; 855012; 1 hit in 10 CRISPR screens. 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; EXP:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005771; C:multivesicular body; IDA:SGD. DR GO; GO:0045335; C:phagocytic vesicle; IBA:GO_Central. DR GO; GO:0005774; C:vacuolar membrane; EXP:UniProtKB. 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:InterPro. 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 targeting 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 CDD; cd01862; Rab7; 1. DR FunFam; 3.40.50.300:FF:000086; Ras-related small GTPase; 1. 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. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47981; RAB FAMILY; 1. DR PANTHER; PTHR47981:SF20; RAS-RELATED PROTEIN RAB-7A; 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 PDBsum; 1KY2; -. DR PDBsum; 1KY3; -. DR PDBsum; 4PHF; -. DR PDBsum; 4PHG; -. DR PDBsum; 4PHH; -. 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. Does FT not suppress the zinc, caffeine and calcium sensitivity of FT CCZ1 mutants." FT /evidence="ECO:0000269|PubMed:11590240, ECO:0000269|Ref.2" FT MUTAGEN 68 FT /note="Q->L: GTP-bound stabilized constitutively active FT mutant. Complements the fragmented vacuolar morphology of FT YPT7 null mutant cells. Does not suppress the zinc, FT caffeine and calcium sensitivity of CCZ1 mutants." FT /evidence="ECO:0000269|PubMed:11590240, ECO:0000269|Ref.2" FT MUTAGEN 127 FT /note="K->E: Reduced nucleotide affinity leading to FT increased turnover between GDP- and GTP-bound states FT without the need of a guanine nucleotide-exchange factor. FT Suppresses the zinc, caffeine and calcium sensitivity of FT CCZ1 mutants." FT /evidence="ECO:0000269|PubMed:11590240" FT MUTAGEN 129 FT /note="D->G,N,A: Reduced nucleotide affinity leading to FT increased turnover between GDP- and GTP-bound states FT without the need of a guanine nucleotide-exchange factor. FT Suppresses the zinc, caffeine and calcium sensitivity of FT CCZ1 mutants." FT /evidence="ECO:0000269|PubMed:11590240" FT MUTAGEN 157 FT /note="T->P: Reduced nucleotide affinity leading to FT increased turnover between GDP- and GTP-bound states FT without the need of a guanine nucleotide-exchange factor. FT Suppresses the zinc, caffeine and calcium sensitivity of FT CCZ1 mutants." FT /evidence="ECO:0000269|PubMed:11590240" FT MUTAGEN 159 FT /note="A->P: Reduced nucleotide affinity leading to FT increased turnover between GDP- and GTP-bound states FT without the need of a guanine nucleotide-exchange factor. FT Suppresses the zinc, caffeine and calcium sensitivity of FT CCZ1 mutants." FT /evidence="ECO:0000269|PubMed:11590240" FT STRAND 8..14 FT /evidence="ECO:0007829|PDB:1KY3" FT HELIX 21..30 FT /evidence="ECO:0007829|PDB:1KY3" FT HELIX 37..40 FT /evidence="ECO:0007829|PDB:1KY2" FT STRAND 46..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 //