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GTP-binding protein YPT32/YPT11 (Rab GTPase YPT32)

 YPT32_YEAST             Reviewed;         222 AA.
P51996; D6VTU5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 163.
RecName: Full=GTP-binding protein YPT32/YPT11;
AltName: Full=Rab GTPase YPT32;
Name=YPT32; Synonyms=YPT11; OrderedLocusNames=YGL210W;
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], AND FUNCTION.
STRAIN=DUR;
PubMed=8978673;
Benli M., Doering F., Robinson D.G., Yang X., Gallwitz D.;
"Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi
function in yeast.";
EMBO J. 15:6460-6475(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8813766;
DOI=10.1002/(SICI)1097-0061(19960630)12:8<799::AID-YEA965>3.0.CO;2-U;
Kail M., Juettner E., Vaux D.;
"Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces
cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and
containing three novel transcribed open reading frames.";
Yeast 12:799-807(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9153757;
DOI=10.1002/(SICI)1097-0061(199704)13:5<475::AID-YEA101>3.0.CO;2-0;
Feuermann M., Simeonava L., Souciet J.-L., Potier S.;
"Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII
reveals 11 open reading frames: two correspond to new genes.";
Yeast 13:475-477(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[5]
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).
[6]
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).
[7]
FUNCTION, MUTAGENESIS OF ALA-141, AND SUBCELLULAR LOCATION.
PubMed=9151665; DOI=10.1083/jcb.137.3.563;
Jedd G., Mulholland J., Segev N.;
"Two new Ypt GTPases are required for exit from the yeast trans-Golgi
compartment.";
J. Cell Biol. 137:563-580(1997).
[8]
ENZYME REGULATION.
PubMed=10559187; DOI=10.1074/jbc.274.47.33186;
Albert S., Gallwitz D.;
"Two new members of a family of Ypt/Rab GTPase activating proteins.
Promiscuity of substrate recognition.";
J. Biol. Chem. 274:33186-33189(1999).
[9]
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).
[10]
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).
[11]
FUNCTION, AND INTERACTION WITH TRS130.
PubMed=12478387; DOI=10.1007/s00294-002-0336-5;
Yamamoto K., Jigami Y.;
"Mutation of TRS130, which encodes a component of the TRAPP II
complex, activates transcription of OCH1 in Saccharomyces
cerevisiae.";
Curr. Genet. 42:85-93(2002).
[12]
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).
[13]
FUNCTION, INTERACTION WITH SEC2, AND MUTAGENESIS OF SER-27; GLU-49;
GLN-72 AND ASN-126.
PubMed=12045183; DOI=10.1083/jcb.200201003;
Ortiz D., Medkova M., Walch-Solimena C., Novick P.J.;
"Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p,
to secretory vesicles; evidence for a Rab cascade in yeast.";
J. Cell Biol. 157:1005-1015(2002).
[14]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[15]
FUNCTION.
PubMed=23078654; DOI=10.1111/tra.12024;
Zou S., Chen Y., Liu Y., Segev N., Yu S., Liu Y., Min G., Ye M.,
Zeng Y., Zhu X., Hong B., Bjorn L.O., Liang Y., Li S., Xie Z.;
"Trs130 participates in autophagy through GTPases Ypt31/32 in
Saccharomyces cerevisiae.";
Traffic 14:233-246(2013).
-!- FUNCTION: Required for protein transport through the secretory
pathway. Probably involved in regulation of secretory vesicle
formation at the trans-Golgi compartment. Mediates the proper
polarized localization of SEC2, a GEF for SEC4, but does not alter
the exchange activity of SEC2 on SEC4. Plays a role in autophagy.
{ECO:0000269|PubMed:12045183, ECO:0000269|PubMed:12478387,
ECO:0000269|PubMed:23078654, ECO:0000269|PubMed:8978673,
ECO:0000269|PubMed:9151665}.
-!- ENZYME REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by the guanine
nucleotide-exchange factor (GEF) TRAPP complex, and inactivated by
GTPase-activating protein (GAP) GYP3.
{ECO:0000269|PubMed:10559187, ECO:0000269|PubMed:11102533}.
-!- SUBUNIT: Interacts with YIF1, YIP3, YIP4 and YIP5. Interacts with
the GEF SEC2. Interacts with TRS130. {ECO:0000269|PubMed:11785952,
ECO:0000269|PubMed:11943201, ECO:0000269|PubMed:12045183,
ECO:0000269|PubMed:12478387}.
-!- INTERACTION:
P39958:GDI1; NbExp=3; IntAct=EBI-29384, EBI-7517;
Q08484:GYP1; NbExp=3; IntAct=EBI-29384, EBI-8005;
P53845:YIF1; NbExp=2; IntAct=EBI-29384, EBI-28230;
P53633:YIP3; NbExp=2; IntAct=EBI-29384, EBI-25301;
P53093:YIP4; NbExp=2; IntAct=EBI-29384, EBI-24124;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:9151665}; Lipid-anchor
{ECO:0000269|PubMed:9151665}.
-!- MISCELLANEOUS: Present with 4298 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X72834; CAA51355.1; -; Genomic_DNA.
EMBL; U33754; AAC49495.1; -; Genomic_DNA.
EMBL; Z72732; CAA96926.1; -; Genomic_DNA.
EMBL; AY558506; AAS56832.1; -; Genomic_DNA.
EMBL; BK006941; DAA07906.1; -; Genomic_DNA.
PIR; S58514; S58514.
RefSeq; NP_011305.1; NM_001181075.1.
PDB; 3RWM; X-ray; 2.00 A; B=7-188.
PDB; 3RWO; X-ray; 1.70 A; A/B=7-188.
PDBsum; 3RWM; -.
PDBsum; 3RWO; -.
ProteinModelPortal; P51996; -.
SMR; P51996; -.
BioGrid; 33046; 91.
DIP; DIP-6597N; -.
IntAct; P51996; 7.
MINT; MINT-703976; -.
STRING; 4932.YGL210W; -.
iPTMnet; P51996; -.
MaxQB; P51996; -.
PRIDE; P51996; -.
EnsemblFungi; YGL210W; YGL210W; YGL210W.
GeneID; 852662; -.
KEGG; sce:YGL210W; -.
EuPathDB; FungiDB:YGL210W; -.
SGD; S000003178; YPT32.
GeneTree; ENSGT00760000118841; -.
HOGENOM; HOG000233968; -.
InParanoid; P51996; -.
KO; K07905; -.
OMA; ANSTACK; -.
OrthoDB; EOG092C5MDH; -.
BioCyc; YEAST:G3O-30687-MONOMER; -.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-8854214; TBC/RABGAPs.
Reactome; R-SCE-8873719; RAB geranylgeranylation.
PRO; PR:P51996; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005768; C:endosome; IDA:SGD.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:SGD.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0034498; P:early endosome to Golgi transport; IGI:SGD.
GO; GO:0006887; P:exocytosis; IMP:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0016192; P:vesicle-mediated transport; 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; Exocytosis;
Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
Nucleotide-binding; Prenylation; Protein transport;
Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P38555}.
CHAIN 2 222 GTP-binding protein YPT32/YPT11.
/FTId=PRO_0000121324.
NP_BIND 20 27 GTP. {ECO:0000250}.
NP_BIND 68 72 GTP. {ECO:0000250}.
NP_BIND 126 129 GTP. {ECO:0000250}.
MOTIF 42 50 Effector region. {ECO:0000305}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P38555}.
LIPID 221 221 S-geranylgeranyl cysteine. {ECO:0000250}.
LIPID 222 222 S-geranylgeranyl cysteine. {ECO:0000250}.
MUTAGEN 27 27 S->N: Binds preferentially GDP.
{ECO:0000269|PubMed:12045183}.
MUTAGEN 49 49 E->Q: Cold sensitive.
{ECO:0000269|PubMed:12045183}.
MUTAGEN 72 72 Q->L: Reduces GTPase activity.
{ECO:0000269|PubMed:12045183}.
MUTAGEN 126 126 N->I: Blocks nucleotide binding.
{ECO:0000269|PubMed:12045183}.
MUTAGEN 141 141 A->D: Loss of function at 37 degrees
Celsius. {ECO:0000269|PubMed:9151665}.
STRAND 11 19 {ECO:0000244|PDB:3RWO}.
HELIX 26 35 {ECO:0000244|PDB:3RWO}.
STRAND 47 57 {ECO:0000244|PDB:3RWO}.
STRAND 60 71 {ECO:0000244|PDB:3RWO}.
HELIX 76 83 {ECO:0000244|PDB:3RWO}.
STRAND 88 94 {ECO:0000244|PDB:3RWO}.
HELIX 98 102 {ECO:0000244|PDB:3RWO}.
HELIX 104 114 {ECO:0000244|PDB:3RWO}.
STRAND 120 126 {ECO:0000244|PDB:3RWO}.
HELIX 128 133 {ECO:0000244|PDB:3RWO}.
HELIX 138 147 {ECO:0000244|PDB:3RWO}.
STRAND 151 154 {ECO:0000244|PDB:3RWO}.
TURN 157 159 {ECO:0000244|PDB:3RWO}.
HELIX 163 177 {ECO:0000244|PDB:3RWO}.
SEQUENCE 222 AA; 24520 MW; 621217A296161964 CRC64;
MSNEDYGYDY DYLFKIVLIG DSGVGKSNLL SRFTTDEFNI ESKSTIGVEF ATRTIEVENK
KIKAQIWDTA GQERYRAITS AYYRGAVGAL IVYDISKSSS YENCNHWLTE LRENADDNVA
VGLIGNKSDL AHLRAVPTDE AKNFAMENQM LFTETSALNS DNVDKAFREL IVAIFQMVSK
HQVDLSGSGT NNMGSNGAPK GPTISLTPAP KEDKKKKSSN CC


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