YPT1_YEAST
ID YPT1_YEAST Reviewed; 206 AA.
AC P01123; D6VTJ2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=GTP-binding protein YPT1;
DE AltName: Full=Protein YP2;
DE AltName: Full=Rab GTPase YPT1;
DE AltName: Full=Transport GTPase YPT1;
GN Name=YPT1; Synonyms=YP2; OrderedLocusNames=YFL038C;
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=6318115; DOI=10.1038/306704a0;
RA Gallwitz D., Donath C., Sander C.;
RT "A yeast gene encoding a protein homologous to the human c-has/bas proto-
RT oncogene product.";
RL Nature 306:704-707(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 1-46; 49-55; 59-69; 72-79; 101-116 AND 130-167,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [6]
RP MUTAGENESIS OF SER-17; LYS-21; ALA-65 AND ASN-121.
RX PubMed=3311726; DOI=10.1002/j.1460-2075.1987.tb02514.x;
RA Wagner P., Molenaar C.M.T., Rauh A.J.G., Broekel R., Schmitt H.D.,
RA Gallwitz D.;
RT "Biochemical properties of the ras-related YPT protein in yeast: a
RT mutational analysis.";
RL EMBO J. 6:2373-2379(1987).
RN [7]
RP PALMITOYLATION AT CYS-23 AND CYS-123, AND MUTAGENESIS OF CYS-205 AND
RP CYS-206.
RX PubMed=3042385; DOI=10.1002/j.1460-2075.1988.tb02903.x;
RA Molenaar C.M.T., Prange R., Gallwitz D.;
RT "A carboxyl-terminal cysteine residue is required for palmitic acid binding
RT and biological activity of the ras-related yeast YPT1 protein.";
RL EMBO J. 7:971-976(1988).
RN [8]
RP MUTAGENESIS, AND POSSIBLE FUNCTION.
RX PubMed=3286011; DOI=10.1016/0092-8674(88)90579-x;
RA Schmitt H.D., Puzicha M., Gallwitz D.;
RT "Study of a temperature-sensitive mutant of the ras-related YPT1 gene
RT product in yeast suggests a role in the regulation of intracellular
RT calcium.";
RL Cell 53:635-647(1988).
RN [9]
RP MUTAGENESIS OF TYR-37; SER-39; THR-40; ILE-41; VAL-43 AND ASP-44.
RX PubMed=2009858; DOI=10.1002/j.1460-2075.1991.tb08010.x;
RA Becker J., Tan T.J., Trepte H.-H., Gallwitz D.;
RT "Mutational analysis of the putative effector domain of the GTP-binding
RT Ypt1 protein in yeast suggests specific regulation by a novel GAP
RT activity.";
RL EMBO J. 10:785-792(1991).
RN [10]
RP MUTAGENESIS OF ALA-136.
RX PubMed=7593181; DOI=10.1083/jcb.131.3.583;
RA Jedd G., Richardson C.J., Litt R.J., Segev N.;
RT "The Ypt1 GTPase is essential for the first two steps of the yeast
RT secretory pathway.";
RL J. Cell Biol. 131:583-590(1995).
RN [11]
RP INTERACTION WITH MRS6.
RX PubMed=8898359; DOI=10.1091/mbc.7.10.1521;
RA Bauer B.E., Lorenzetti S., Miaczynska M., Bui D.M., Schweyen R.J.,
RA Ragnini A.;
RT "Amino- and carboxy-terminal domains of the yeast Rab escort protein are
RT both required for binding of Ypt small G proteins.";
RL Mol. Biol. Cell 7:1521-1533(1996).
RN [12]
RP MUTAGENESIS OF GLN-67.
RX PubMed=9447979; DOI=10.1128/mcb.18.2.827;
RA Richardson C.J., Jones S., Litt R.J., Segev N.;
RT "GTP hydrolysis is not important for Ypt1 GTPase function in vesicular
RT transport.";
RL Mol. Cell. Biol. 18:827-838(1998).
RN [13]
RP ACTIVITY REGULATION.
RX PubMed=9819430; DOI=10.1128/mcb.18.12.7444;
RA Day G.-J., Mosteller R.D., Broek D.;
RT "Distinct subclasses of small GTPases interact with guanine nucleotide
RT exchange factors in a similar manner.";
RL Mol. Cell. Biol. 18:7444-7454(1998).
RN [14]
RP ISOPRENYLATION AT CYS-205 AND CYS-206, MUTAGENESIS OF CYS-205 AND CYS-206,
RP AND FUNCTION.
RX PubMed=10071213; DOI=10.1007/s004380050944;
RA Yoo J.S., Grabowski R., Xing L., Trepte H.H., Schmitt H.D., Gallwitz D.;
RT "Functional implications of genetic interactions between genes encoding
RT small GTPases involved in vesicular transport in yeast.";
RL Mol. Gen. Genet. 261:80-91(1999).
RN [15]
RP ACTIVITY REGULATION.
RX PubMed=11102533; DOI=10.1091/mbc.11.12.4403;
RA Jones S., Newman C., Liu F., Segev N.;
RT "The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32.";
RL Mol. Biol. Cell 11:4403-4411(2000).
RN [16]
RP ACTIVITY REGULATION.
RX PubMed=11359917; DOI=10.1091/mbc.12.5.1215;
RA Du L.-L., Novick P.;
RT "Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus
RT and is a negative regulator of Ypt1p.";
RL Mol. Biol. Cell 12:1215-1226(2001).
RN [17]
RP INTERACTION WITH YIP3.
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 [18]
RP FUNCTION.
RX PubMed=11879636; DOI=10.1016/s1534-5807(02)00133-8;
RA Morsomme P., Riezman H.;
RT "The Rab GTPase Ypt1p and tethering factors couple protein sorting at the
RT ER to vesicle targeting to the Golgi apparatus.";
RL Dev. Cell 2:307-317(2002).
RN [19]
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 [20]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=12189143; DOI=10.1074/jbc.m205783200;
RA De Antoni A., Schmitzova J., Trepte H.-H., Gallwitz D., Albert S.;
RT "Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to
RT Golgi transport revealed by the analysis of two novel Ypt1-GAPs.";
RL J. Biol. Chem. 277:41023-41031(2002).
RN [21]
RP FUNCTION, INTERACTION WITH YIP1, AND SUBCELLULAR LOCATION.
RX PubMed=12802060; DOI=10.1091/mbc.e02-11-0707;
RA Calero M., Chen C.Z., Zhu W., Winand N.J., Havas K.A., Gilbert P.M.,
RA Burd C.G., Collins R.N.;
RT "Dual prenylation is required for Rab protein localization and function.";
RL Mol. Biol. Cell 14:1852-1867(2003).
RN [22]
RP FUNCTION, AND MUTAGENESIS OF GLN-67.
RX PubMed=15082776; DOI=10.1128/mcb.24.9.3815-3826.2004;
RA Lafourcade C., Galan J.-M., Gloor Y., Haguenauer-Tsapis R., Peter M.;
RT "The GTPase-activating enzyme Gyp1p is required for recycling of
RT internalized membrane material by inactivation of the Rab/Ypt GTPase
RT Ypt1p.";
RL Mol. Cell. Biol. 24:3815-3826(2004).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [25]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20375281; DOI=10.1073/pnas.1000063107;
RA Lynch-Day M.A., Bhandari D., Menon S., Huang J., Cai H., Bartholomew C.R.,
RA Brumell J.H., Ferro-Novick S., Klionsky D.J.;
RT "Trs85 directs a Ypt1 GEF, TRAPPIII, to the phagophore to promote
RT autophagy.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7811-7816(2010).
RN [26]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-144, 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 [27]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH GDI1 AND GDP, AND
RP ISOPRENYLATION AT CYS-206.
RX PubMed=14576435; DOI=10.1126/science.1087761;
RA Rak A., Pylypenko O., Durek T., Watzke A., Kushnir S., Brunsveld L.,
RA Waldmann H., Goody R.S., Alexandrov K.;
RT "Structure of Rab GDP-dissociation inhibitor in complex with prenylated
RT YPT1 GTPase.";
RL Science 302:646-650(2003).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 3-172 IN COMPLEX WITH GTP.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH GDI1 AND GDP, AND
RP ISOPRENYLATION AT CYS-205 AND CYS-206.
RX PubMed=16395334; DOI=10.1038/sj.emboj.7600921;
RA Pylypenko O., Rak A., Durek T., Kushnir S., Dursina B.E., Thomae N.H.,
RA Constantinescu A.T., Brunsveld L., Watzke A., Waldmann H., Goody R.S.,
RA Alexandrov K.;
RT "Structure of doubly prenylated Ypt1:GDI complex and the mechanism of GDI-
RT mediated Rab recycling.";
RL EMBO J. 25:13-23(2006).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS).
RX PubMed=18585354; DOI=10.1016/j.cell.2008.04.049;
RA Cai Y., Chin H.F., Lazarova D., Menon S., Fu C., Cai H., Sclafani A.,
RA Rodgers D.W., De La Cruz E.M., Ferro-Novick S., Reinisch K.M.;
RT "The structural basis for activation of the Rab Ypt1p by the TRAPP
RT membrane-tethering complexes.";
RL Cell 133:1202-1213(2008).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. YPT1 regulates the
CC trafficking of secretory vesicles from the endoplasmic reticulum (ER)
CC to the Golgi. Vesicular transport depends on shuttling of YPT1 between
CC membrane and cytosol by GDI1, probably by recycling it to its membrane
CC of origin after a vesicle fusion event. Plays a role in the initial
CC events of the autophagic vacuole development which take place at
CC specialized regions of the endoplasmic reticulum. Also involved in the
CC recycling of membrane proteins. {ECO:0000269|PubMed:10071213,
CC ECO:0000269|PubMed:11879636, ECO:0000269|PubMed:12189143,
CC ECO:0000269|PubMed:12802060, ECO:0000269|PubMed:15082776,
CC ECO:0000269|PubMed:20375281}.
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). YPT1 is
CC activated by the GEFs DSS4 and TRAPP complex, and inactivated by GAPs
CC GYP1, GYP5 and GYP8. {ECO:0000269|PubMed:11102533,
CC ECO:0000269|PubMed:11359917, ECO:0000269|PubMed:12189143,
CC ECO:0000269|PubMed:9819430}.
CC -!- SUBUNIT: Forms a complex with the Rab escort protein (REP) MRS6, which
CC is recognized by Rab geranylgeranyltransferase BET2-BET4. Interacts
CC with the Rab GDP dissociation inhibitor GDI1, which can retrieve from
CC and deliver to membranes the GDP-bound and prenylated form of YPT1.
CC Interacts with YIP1, which is required for proper membrane targeting of
CC prenylated YPT1. Interacts with YIF1, YIP3, YIP4 and YIP5.
CC {ECO:0000269|PubMed:11785952, ECO:0000269|PubMed:11943201,
CC ECO:0000269|PubMed:12802060, ECO:0000269|PubMed:14576435,
CC ECO:0000269|PubMed:8898359}.
CC -!- INTERACTION:
CC P01123; P39958: GDI1; NbExp=6; IntAct=EBI-29496, EBI-7517;
CC P01123; P22214: SEC22; NbExp=2; IntAct=EBI-29496, EBI-16577;
CC P01123; Q01590: SED5; NbExp=3; IntAct=EBI-29496, EBI-16930;
CC P01123; P53845: YIF1; NbExp=3; IntAct=EBI-29496, EBI-28230;
CC P01123; P53633: YIP3; NbExp=2; IntAct=EBI-29496, EBI-25301;
CC P01123; P53093: YIP4; NbExp=2; IntAct=EBI-29496, EBI-24124;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12802060}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12802060}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12802060}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12802060}. Cytoplasm {ECO:0000269|PubMed:12802060}.
CC Preautophagosomal structure membrane {ECO:0000269|PubMed:20375281};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=ER and
CC Golgi when GTP-bound. Cytoplasmic when bound to GDI1.
CC -!- PTM: Prenylation is required for interaction with GDI1 and YIP1.
CC {ECO:0000269|PubMed:10071213}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- CAUTION: In PubMed:3042385 the location of any palmitoylation was not
CC determined. Mutagenesis of either Cys-205 or Cys-206 would disrupt
CC normal geranylgeranylation, and there would be no primary membrane
CC association for secondary S-palmitoylation to occur at some other
CC position, for example Cys-23. Mutagenesis of both Cys-205 and Cys-206
CC is lethal, so protein production could not have been observed.
CC {ECO:0000305}.
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DR EMBL; X00209; CAA25036.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09201.1; -; Genomic_DNA.
DR EMBL; AY558467; AAS56793.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12402.1; -; Genomic_DNA.
DR PIR; S56216; TVBYQ2.
DR RefSeq; NP_116615.1; NM_001179928.1.
DR PDB; 1UKV; X-ray; 1.50 A; Y=1-206.
DR PDB; 1YZN; X-ray; 2.06 A; A=3-172.
DR PDB; 2BCG; X-ray; 1.48 A; Y=1-206.
DR PDB; 3CUE; X-ray; 3.70 A; F/L/R/X=1-206.
DR PDB; 7KMT; EM; 3.70 A; A=1-206.
DR PDBsum; 1UKV; -.
DR PDBsum; 1YZN; -.
DR PDBsum; 2BCG; -.
DR PDBsum; 3CUE; -.
DR PDBsum; 7KMT; -.
DR AlphaFoldDB; P01123; -.
DR SMR; P01123; -.
DR BioGRID; 31108; 435.
DR DIP; DIP-2019N; -.
DR IntAct; P01123; 34.
DR MINT; P01123; -.
DR STRING; 4932.YFL038C; -.
DR iPTMnet; P01123; -.
DR MaxQB; P01123; -.
DR PaxDb; P01123; -.
DR PRIDE; P01123; -.
DR EnsemblFungi; YFL038C_mRNA; YFL038C; YFL038C.
DR GeneID; 850505; -.
DR KEGG; sce:YFL038C; -.
DR SGD; S000001856; YPT1.
DR VEuPathDB; FungiDB:YFL038C; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00940000175199; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P01123; -.
DR OMA; KERMGNT; -.
DR BioCyc; YEAST:G3O-30424-MON; -.
DR Reactome; R-SCE-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-SCE-8873719; RAB geranylgeranylation.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR EvolutionaryTrace; P01123; -.
DR PRO; PR:P01123; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P01123; protein.
DR GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0005795; C:Golgi stack; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:SGD.
DR GO; GO:0032456; P:endocytic recycling; IMP:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0048194; P:Golgi vesicle budding; IGI:SGD.
DR GO; GO:0048211; P:Golgi vesicle docking; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:1990261; P:pre-mRNA catabolic process; IMP:SGD.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:SGD.
DR GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0043549; P:regulation of kinase activity; IMP:SGD.
DR GO; GO:0061709; P:reticulophagy; IMP:SGD.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:SGD.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:SGD.
DR GO; GO:0035494; P:SNARE complex disassembly; IMP: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; Acetylation; Autophagy; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Isopeptide bond; Lipoprotein; Membrane; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..206
FT /note="GTP-binding protein YPT1"
FT /id="PRO_0000121318"
FT REGION 63..80
FT /note="Interaction with GDI1"
FT /evidence="ECO:0000269|PubMed:14576435"
FT REGION 173..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..195
FT /note="Interaction with GDI1"
FT /evidence="ECO:0000269|PubMed:14576435"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14576435,
FT ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16395334,
FT ECO:0007744|PDB:1UKV, ECO:0007744|PDB:1YZN,
FT ECO:0007744|PDB:2BCG"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14576435,
FT ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16395334,
FT ECO:0007744|PDB:1UKV, ECO:0007744|PDB:1YZN,
FT ECO:0007744|PDB:2BCG"
FT BINDING 66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16034420,
FT ECO:0007744|PDB:1YZN"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14576435,
FT ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16395334,
FT ECO:0007744|PDB:1UKV, ECO:0007744|PDB:1YZN,
FT ECO:0007744|PDB:2BCG"
FT BINDING 152..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:14576435,
FT ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16395334,
FT ECO:0007744|PDB:1UKV, ECO:0007744|PDB:1YZN,
FT ECO:0007744|PDB:2BCG"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.5"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT LIPID 23
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 123
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:10071213,
FT ECO:0000269|PubMed:16395334"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:10071213,
FT ECO:0000269|PubMed:14576435, ECO:0000269|PubMed:16395334,
FT ECO:0007744|PDB:1UKV"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 17
FT /note="S->G: Decreases GTP binding and increases GTP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:3311726"
FT MUTAGEN 21
FT /note="K->M: Abolishes GTP binding."
FT /evidence="ECO:0000269|PubMed:3311726"
FT MUTAGEN 37
FT /note="Y->F: No change."
FT /evidence="ECO:0000269|PubMed:2009858"
FT MUTAGEN 39
FT /note="S->A: No change."
FT /evidence="ECO:0000269|PubMed:2009858"
FT MUTAGEN 40
FT /note="T->S: No change."
FT /evidence="ECO:0000269|PubMed:2009858"
FT MUTAGEN 41
FT /note="I->M: Lethal."
FT /evidence="ECO:0000269|PubMed:2009858"
FT MUTAGEN 43
FT /note="V->E: No change."
FT /evidence="ECO:0000269|PubMed:2009858"
FT MUTAGEN 44
FT /note="D->N: Temperature-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:2009858"
FT MUTAGEN 65
FT /note="A->T: Decreases GTP binding and GTP hydrolysis."
FT /evidence="ECO:0000269|PubMed:3311726"
FT MUTAGEN 67
FT /note="Q->L: Locks YPT1 in the GTP-bound form by reducing
FT GTP hydrolysis rate 40-fold."
FT /evidence="ECO:0000269|PubMed:15082776,
FT ECO:0000269|PubMed:9447979"
FT MUTAGEN 121
FT /note="N->I: Abolishes GTP binding."
FT /evidence="ECO:0000269|PubMed:3311726"
FT MUTAGEN 136
FT /note="A->D: Loss of function at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:7593181"
FT MUTAGEN 205
FT /note="C->S: Abolishes membrane association. Lethal; when
FT associated with S-206."
FT /evidence="ECO:0000269|PubMed:10071213,
FT ECO:0000269|PubMed:3042385"
FT MUTAGEN 206
FT /note="C->S: Abolishes membrane association. Lethal; when
FT associated with S-205."
FT /evidence="ECO:0000269|PubMed:10071213,
FT ECO:0000269|PubMed:3042385"
FT STRAND 6..16
FT /evidence="ECO:0007829|PDB:2BCG"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:2BCG"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2BCG"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:2BCG"
FT TURN 65..71
FT /evidence="ECO:0007829|PDB:2BCG"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2BCG"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2BCG"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:2BCG"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:2BCG"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2BCG"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:2BCG"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2BCG"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2BCG"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:2BCG"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:2BCG"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2BCG"
SQ SEQUENCE 206 AA; 23214 MW; F8C704F6BF2D227B CRC64;
MNSEYDYLFK LLLIGNSGVG KSCLLLRFSD DTYTNDYIST IGVDFKIKTV ELDGKTVKLQ
IWDTAGQERF RTITSSYYRG SHGIIIVYDV TDQESFNGVK MWLQEIDRYA TSTVLKLLVG
NKCDLKDKRV VEYDVAKEFA DANKMPFLET SALDSTNVED AFLTMARQIK ESMSQQNLNE
TTQKKEDKGN VNLKGQSLTN TGGGCC
