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GTP-binding protein YPT1 (Protein YP2) (Rab GTPase YPT1) (Transport GTPase YPT1)

 YPT1_YEAST              Reviewed;         206 AA.
P01123; D6VTJ2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
25-OCT-2017, entry version 196.
RecName: Full=GTP-binding protein YPT1;
AltName: Full=Protein YP2;
AltName: Full=Rab GTPase YPT1;
AltName: Full=Transport GTPase YPT1;
Name=YPT1; Synonyms=YP2; OrderedLocusNames=YFL038C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6318115; DOI=10.1038/306704a0;
Gallwitz D., Donath C., Sander C.;
"A yeast gene encoding a protein homologous to the human c-has/bas
proto-oncogene product.";
Nature 306:704-707(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7670463; DOI=10.1038/ng0795-261;
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M.,
Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
Yamazaki M., Tashiro H., Eki T.;
"Analysis of the nucleotide sequence of chromosome VI from
Saccharomyces cerevisiae.";
Nat. Genet. 10:261-268(1995).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 1-46; 49-55; 59-69; 72-79; 101-116 AND 130-167,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1, AND
IDENTIFICATION BY MASS SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (MAY-2005) to UniProtKB.
[6]
MUTAGENESIS OF SER-17; LYS-21; ALA-65 AND ASN-121.
PubMed=3311726;
Wagner P., Molenaar C.M.T., Rauh A.J.G., Broekel R., Schmitt H.D.,
Gallwitz D.;
"Biochemical properties of the ras-related YPT protein in yeast: a
mutational analysis.";
EMBO J. 6:2373-2379(1987).
[7]
PALMITOYLATION AT CYS-23 AND CYS-123, AND MUTAGENESIS OF CYS-205 AND
CYS-206.
PubMed=3042385;
Molenaar C.M.T., Prange R., Gallwitz D.;
"A carboxyl-terminal cysteine residue is required for palmitic acid
binding and biological activity of the ras-related yeast YPT1
protein.";
EMBO J. 7:971-976(1988).
[8]
MUTAGENESIS, AND POSSIBLE FUNCTION.
PubMed=3286011; DOI=10.1016/0092-8674(88)90579-X;
Schmitt H.D., Puzicha M., Gallwitz D.;
"Study of a temperature-sensitive mutant of the ras-related YPT1 gene
product in yeast suggests a role in the regulation of intracellular
calcium.";
Cell 53:635-647(1988).
[9]
MUTAGENESIS OF TYR-37; SER-39; THR-40; ILE-41; VAL-43 AND ASP-44.
PubMed=2009858;
Becker J., Tan T.J., Trepte H.-H., Gallwitz D.;
"Mutational analysis of the putative effector domain of the GTP-
binding Ypt1 protein in yeast suggests specific regulation by a novel
GAP activity.";
EMBO J. 10:785-792(1991).
[10]
MUTAGENESIS OF ALA-136.
PubMed=7593181; DOI=10.1083/jcb.131.3.583;
Jedd G., Richardson C.J., Litt R.J., Segev N.;
"The Ypt1 GTPase is essential for the first two steps of the yeast
secretory pathway.";
J. Cell Biol. 131:583-590(1995).
[11]
INTERACTION WITH MRS6.
PubMed=8898359; DOI=10.1091/mbc.7.10.1521;
Bauer B.E., Lorenzetti S., Miaczynska M., Bui D.M., Schweyen R.J.,
Ragnini A.;
"Amino- and carboxy-terminal domains of the yeast Rab escort protein
are both required for binding of Ypt small G proteins.";
Mol. Biol. Cell 7:1521-1533(1996).
[12]
MUTAGENESIS OF GLN-67.
PubMed=9447979; DOI=10.1128/MCB.18.2.827;
Richardson C.J., Jones S., Litt R.J., Segev N.;
"GTP hydrolysis is not important for Ypt1 GTPase function in vesicular
transport.";
Mol. Cell. Biol. 18:827-838(1998).
[13]
ENZYME REGULATION.
PubMed=9819430; DOI=10.1128/MCB.18.12.7444;
Day G.-J., Mosteller R.D., Broek D.;
"Distinct subclasses of small GTPases interact with guanine nucleotide
exchange factors in a similar manner.";
Mol. Cell. Biol. 18:7444-7454(1998).
[14]
ISOPRENYLATION AT CYS-205 AND CYS-206, MUTAGENESIS OF CYS-205 AND
CYS-206, AND FUNCTION.
PubMed=10071213; DOI=10.1007/s004380050944;
Yoo J.S., Grabowski R., Xing L., Trepte H.H., Schmitt H.D.,
Gallwitz D.;
"Functional implications of genetic interactions between genes
encoding small GTPases involved in vesicular transport in yeast.";
Mol. Gen. Genet. 261:80-91(1999).
[15]
ENZYME REGULATION.
PubMed=11102533; DOI=10.1091/mbc.11.12.4403;
Jones S., Newman C., Liu F., Segev N.;
"The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32.";
Mol. Biol. Cell 11:4403-4411(2000).
[16]
ENZYME REGULATION.
PubMed=11359917; DOI=10.1091/mbc.12.5.1215;
Du L.-L., Novick P.;
"Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi
apparatus and is a negative regulator of Ypt1p.";
Mol. Biol. Cell 12:1215-1226(2001).
[17]
INTERACTION WITH YIP3.
PubMed=11785952; DOI=10.1006/bbrc.2001.6242;
Calero M., Collins R.N.;
"Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab
proteins.";
Biochem. Biophys. Res. Commun. 290:676-681(2002).
[18]
FUNCTION.
PubMed=11879636; DOI=10.1016/S1534-5807(02)00133-8;
Morsomme P., Riezman H.;
"The Rab GTPase Ypt1p and tethering factors couple protein sorting at
the ER to vesicle targeting to the Golgi apparatus.";
Dev. Cell 2:307-317(2002).
[19]
INTERACTION WITH YIF1; YIP4 AND YIP5.
PubMed=11943201; DOI=10.1016/S0014-5793(02)02442-0;
Calero M., Winand N.J., Collins R.N.;
"Identification of the novel proteins Yip4p and Yip5p as Rab GTPase
interacting factors.";
FEBS Lett. 515:89-98(2002).
[20]
FUNCTION, AND ENZYME REGULATION.
PubMed=12189143; DOI=10.1074/jbc.M205783200;
De Antoni A., Schmitzova J., Trepte H.-H., Gallwitz D., Albert S.;
"Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic
reticulum to Golgi transport revealed by the analysis of two novel
Ypt1-GAPs.";
J. Biol. Chem. 277:41023-41031(2002).
[21]
FUNCTION, INTERACTION WITH YIP1, AND SUBCELLULAR LOCATION.
PubMed=12802060; DOI=10.1091/mbc.E02-11-0707;
Calero M., Chen C.Z., Zhu W., Winand N.J., Havas K.A., Gilbert P.M.,
Burd C.G., Collins R.N.;
"Dual prenylation is required for Rab protein localization and
function.";
Mol. Biol. Cell 14:1852-1867(2003).
[22]
FUNCTION, AND MUTAGENESIS OF GLN-67.
PubMed=15082776; DOI=10.1128/MCB.24.9.3815-3826.2004;
Lafourcade C., Galan J.-M., Gloor Y., Haguenauer-Tsapis R., Peter M.;
"The GTPase-activating enzyme Gyp1p is required for recycling of
internalized membrane material by inactivation of the Rab/Ypt GTPase
Ypt1p.";
Mol. Cell. Biol. 24:3815-3826(2004).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[25]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20375281; DOI=10.1073/pnas.1000063107;
Lynch-Day M.A., Bhandari D., Menon S., Huang J., Cai H.,
Bartholomew C.R., Brumell J.H., Ferro-Novick S., Klionsky D.J.;
"Trs85 directs a Ypt1 GEF, TRAPPIII, to the phagophore to promote
autophagy.";
Proc. Natl. Acad. Sci. U.S.A. 107:7811-7816(2010).
[26]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-144, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[27]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH GDI1.
PubMed=14576435; DOI=10.1126/science.1087761;
Rak A., Pylypenko O., Durek T., Watzke A., Kushnir S., Brunsveld L.,
Waldmann H., Goody R.S., Alexandrov K.;
"Structure of Rab GDP-dissociation inhibitor in complex with
prenylated YPT1 GTPase.";
Science 302:646-650(2003).
-!- FUNCTION: The small GTPases Rab are key regulators of
intracellular membrane trafficking, from the formation of
transport vesicles to their fusion with membranes. Rabs cycle
between an inactive GDP-bound form and an active GTP-bound form
that is able to recruit to membranes different set of downstream
effectors directly responsible for vesicle formation, movement,
tethering and fusion. YPT1 regulates the trafficking of secretory
vesicles from the endoplasmic reticulum (ER) to the Golgi.
Vesicular transport depends on shuttling of YPT1 between membrane
and cytosol by GDI1, probably by recycling it to its membrane of
origin after a vesicle fusion event. Plays a role in the initial
events of the autophagic vacuole development which take place at
specialized regions of the endoplasmic reticulum. Also involved in
the recycling of membrane proteins. {ECO:0000269|PubMed:10071213,
ECO:0000269|PubMed:11879636, ECO:0000269|PubMed:12189143,
ECO:0000269|PubMed:12802060, ECO:0000269|PubMed:15082776,
ECO:0000269|PubMed:20375281}.
-!- ENZYME REGULATION: Rab activation is generally mediated by a
guanine exchange factor (GEF), while inactivation through
hydrolysis of bound GTP is catalyzed by a GTPase activating
protein (GAP). YPT1 is activated by the GEFs DSS4 and TRAPP
complex, and inactivated by GAPs GYP1, GYP5 and GYP8.
{ECO:0000269|PubMed:11102533, ECO:0000269|PubMed:11359917,
ECO:0000269|PubMed:12189143, ECO:0000269|PubMed:9819430}.
-!- SUBUNIT: Forms a complex with the Rab escort protein (REP) MRS6,
which is recognized by Rab geranylgeranyltransferase BET2-BET4.
Interacts with the Rab GDP dissociation inhibitor GDI1, which can
retrieve from and deliver to membranes the GDP-bound and
prenylated form of YPT1. Interacts with YIP1, which is required
for proper membrane targeting of prenylated YPT1. Interacts with
YIF1, YIP3, YIP4 and YIP5. {ECO:0000269|PubMed:11785952,
ECO:0000269|PubMed:11943201, ECO:0000269|PubMed:12802060,
ECO:0000269|PubMed:14576435, ECO:0000269|PubMed:8898359}.
-!- INTERACTION:
P39958:GDI1; NbExp=6; IntAct=EBI-29496, EBI-7517;
P22214:SEC22; NbExp=2; IntAct=EBI-29496, EBI-16577;
Q01590:SED5; NbExp=3; IntAct=EBI-29496, EBI-16930;
P53845:YIF1; NbExp=3; IntAct=EBI-29496, EBI-28230;
P53633:YIP3; NbExp=2; IntAct=EBI-29496, EBI-25301;
P53093:YIP4; NbExp=2; IntAct=EBI-29496, EBI-24124;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12802060}; Peripheral membrane protein
{ECO:0000269|PubMed:12802060}. Golgi apparatus membrane
{ECO:0000269|PubMed:12802060}; Peripheral membrane protein
{ECO:0000269|PubMed:12802060}. Cytoplasm
{ECO:0000269|PubMed:12802060}. Preautophagosomal structure
membrane {ECO:0000269|PubMed:20375281}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=ER and Golgi
when GTP-bound. Cytoplasmic when bound to GDI1.
-!- PTM: Prenylation is required for interaction with GDI1 and YIP1.
{ECO:0000269|PubMed:10071213}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
-!- CAUTION: In PubMed:3042385 the location of any palmitoylation was
not determined. Mutagenesis of either Cys-205 or Cys-206 would
disrupt normal geranylgeranylation, and there would be no primary
membrane association for secondary S-palmitoylation to occur at
some other position, for example Cys-23. Mutagenesis of both Cys-
205 and Cys-206 is lethal, so protein production could not have
been observed. {ECO:0000305}.
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EMBL; X00209; CAA25036.1; -; Genomic_DNA.
EMBL; D50617; BAA09201.1; -; Genomic_DNA.
EMBL; AY558467; AAS56793.1; -; Genomic_DNA.
EMBL; BK006940; DAA12402.1; -; Genomic_DNA.
PIR; S56216; TVBYQ2.
RefSeq; NP_116615.1; NM_001179928.1.
PDB; 1UKV; X-ray; 1.50 A; Y=1-206.
PDB; 1YZN; X-ray; 2.06 A; A=3-172.
PDB; 2BCG; X-ray; 1.48 A; Y=1-206.
PDB; 3CUE; X-ray; 3.70 A; F/L/R/X=1-206.
PDBsum; 1UKV; -.
PDBsum; 1YZN; -.
PDBsum; 2BCG; -.
PDBsum; 3CUE; -.
ProteinModelPortal; P01123; -.
SMR; P01123; -.
BioGrid; 31108; 401.
DIP; DIP-2019N; -.
IntAct; P01123; 34.
MINT; MINT-389361; -.
STRING; 4932.YFL038C; -.
iPTMnet; P01123; -.
MaxQB; P01123; -.
PRIDE; P01123; -.
EnsemblFungi; BAA09201; BAA09201; BAA09201.
EnsemblFungi; YFL038C; YFL038C; YFL038C.
GeneID; 850505; -.
KEGG; sce:YFL038C; -.
EuPathDB; FungiDB:YFL038C; -.
SGD; S000001856; YPT1.
GeneTree; ENSGT00900000140786; -.
HOGENOM; HOG000233968; -.
InParanoid; P01123; -.
KO; K07874; -.
OMA; VTDNDTF; -.
OrthoDB; EOG092C5MDH; -.
BioCyc; YEAST:G3O-30424-MONOMER; -.
Reactome; R-SCE-114608; Platelet degranulation.
Reactome; R-SCE-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-SCE-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-SCE-8854214; TBC/RABGAPs.
Reactome; R-SCE-8873719; RAB geranylgeranylation.
EvolutionaryTrace; P01123; -.
PRO; PR:P01123; -.
Proteomes; UP000002311; Chromosome VI.
GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:SGD.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IDA:SGD.
GO; GO:0005795; C:Golgi stack; IDA:SGD.
GO; GO:0000407; C:pre-autophagosomal structure; IDA:SGD.
GO; GO:0034045; C:pre-autophagosomal structure membrane; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:SGD.
GO; GO:0000149; F:SNARE binding; IDA:SGD.
GO; GO:0090114; P:COPII-coated vesicle budding; IMP:SGD.
GO; GO:0034498; P:early endosome to Golgi transport; IMP:SGD.
GO; GO:0032456; P:endocytic recycling; IMP:SGD.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:SGD.
GO; GO:0048194; P:Golgi vesicle budding; IGI:SGD.
GO; GO:0048211; P:Golgi vesicle docking; IMP:SGD.
GO; GO:0016236; P:macroautophagy; IMP:SGD.
GO; GO:1990261; P:pre-mRNA catabolic process; IMP:SGD.
GO; GO:0032258; P:protein localization by the Cvt pathway; IMP:SGD.
GO; GO:0034497; P:protein localization to pre-autophagosomal structure; IMP:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:SGD.
GO; GO:0043549; P:regulation of kinase activity; IMP:SGD.
GO; GO:0061709; P:reticulophagy; IMP:SGD.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:SGD.
GO; GO:0035493; P:SNARE complex assembly; IDA:SGD.
GO; GO:0035494; P:SNARE complex disassembly; IMP:SGD.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Autophagy; Complete proteome; Cytoplasm;
Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
Golgi apparatus; GTP-binding; Isopeptide bond; Lipoprotein; Membrane;
Nucleotide-binding; Palmitate; Phosphoprotein; Prenylation;
Protein transport; Reference proteome; Transport; Ubl conjugation.
CHAIN 1 206 GTP-binding protein YPT1.
/FTId=PRO_0000121318.
NP_BIND 15 23 GTP. {ECO:0000250|UniProtKB:P62820}.
NP_BIND 33 40 GTP. {ECO:0000250|UniProtKB:P62820}.
NP_BIND 63 67 GTP. {ECO:0000250|UniProtKB:P62820}.
NP_BIND 121 124 GTP. {ECO:0000250|UniProtKB:P62820}.
NP_BIND 151 153 GTP. {ECO:0000250|UniProtKB:P62820}.
REGION 63 80 Interaction with GDI1.
REGION 189 195 Interaction with GDI1.
MOTIF 37 45 Effector region. {ECO:0000305}.
MOD_RES 1 1 N-acetylmethionine. {ECO:0000269|Ref.5}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
LIPID 23 23 S-palmitoyl cysteine. {ECO:0000255}.
LIPID 123 123 S-palmitoyl cysteine. {ECO:0000255}.
LIPID 205 205 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:10071213}.
LIPID 206 206 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:10071213}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 17 17 S->G: Decreases GTP binding and increases
GTP hydrolysis.
{ECO:0000269|PubMed:3311726}.
MUTAGEN 21 21 K->M: Abolishes GTP binding.
{ECO:0000269|PubMed:3311726}.
MUTAGEN 37 37 Y->F: No change.
{ECO:0000269|PubMed:2009858}.
MUTAGEN 39 39 S->A: No change.
{ECO:0000269|PubMed:2009858}.
MUTAGEN 40 40 T->S: No change.
{ECO:0000269|PubMed:2009858}.
MUTAGEN 41 41 I->M: Lethal.
{ECO:0000269|PubMed:2009858}.
MUTAGEN 43 43 V->E: No change.
{ECO:0000269|PubMed:2009858}.
MUTAGEN 44 44 D->N: Temperature-sensitive phenotype.
{ECO:0000269|PubMed:2009858}.
MUTAGEN 65 65 A->T: Decreases GTP binding and GTP
hydrolysis. {ECO:0000269|PubMed:3311726}.
MUTAGEN 67 67 Q->L: Locks YPT1 in the GTP-bound form by
reducing GTP hydrolysis rate 40-fold.
{ECO:0000269|PubMed:15082776,
ECO:0000269|PubMed:9447979}.
MUTAGEN 121 121 N->I: Abolishes GTP binding.
{ECO:0000269|PubMed:3311726}.
MUTAGEN 136 136 A->D: Loss of function at 37 degrees
Celsius. {ECO:0000269|PubMed:7593181}.
MUTAGEN 205 205 C->S: Abolishes membrane association.
Lethal; when associated with S-206.
{ECO:0000269|PubMed:10071213,
ECO:0000269|PubMed:3042385}.
MUTAGEN 206 206 C->S: Abolishes membrane association.
Lethal; when associated with S-205.
{ECO:0000269|PubMed:10071213,
ECO:0000269|PubMed:3042385}.
CONFLICT 171 171 E -> Q (in Ref. 1; CAA25036).
{ECO:0000305}.
STRAND 6 16 {ECO:0000244|PDB:2BCG}.
HELIX 21 30 {ECO:0000244|PDB:2BCG}.
STRAND 45 52 {ECO:0000244|PDB:2BCG}.
STRAND 55 62 {ECO:0000244|PDB:2BCG}.
TURN 65 71 {ECO:0000244|PDB:2BCG}.
HELIX 75 78 {ECO:0000244|PDB:2BCG}.
STRAND 82 89 {ECO:0000244|PDB:2BCG}.
HELIX 93 109 {ECO:0000244|PDB:2BCG}.
STRAND 115 121 {ECO:0000244|PDB:2BCG}.
TURN 126 128 {ECO:0000244|PDB:2BCG}.
HELIX 133 142 {ECO:0000244|PDB:2BCG}.
STRAND 147 149 {ECO:0000244|PDB:2BCG}.
TURN 152 154 {ECO:0000244|PDB:2BCG}.
HELIX 158 172 {ECO:0000244|PDB:2BCG}.
HELIX 175 179 {ECO:0000244|PDB:2BCG}.
HELIX 183 185 {ECO:0000244|PDB:2BCG}.
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


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