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Golgi SNAP receptor complex member 1 (Golgi SNARE protein 1) (Protein transport protein GOS1)

 GOSR1_YEAST             Reviewed;         223 AA.
P38736; D3DKT7;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
18-JUL-2018, entry version 133.
RecName: Full=Golgi SNAP receptor complex member 1;
AltName: Full=Golgi SNARE protein 1;
AltName: Full=Protein transport protein GOS1;
Name=GOS1; OrderedLocusNames=YHL031C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091229; DOI=10.1126/science.8091229;
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
VIII.";
Science 265:2077-2082(1994).
[2]
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).
[3]
INTERACTION WITH SED5.
PubMed=9211930; DOI=10.1074/jbc.272.28.17776;
McNew J.A., Soegaard M., Lampen N.M., Machida S., Ye R.R., Lacomis L.,
Tempst P., Rothman J.E., Soellner T.H.;
"Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi
transport.";
J. Biol. Chem. 272:17776-17783(1997).
[4]
FUNCTION, INTERACTION WITH SED5, DISRUPTION PHENOTYPE, AND SUBCELLULAR
LOCATION.
PubMed=9755865; DOI=10.1016/S0014-5793(98)01044-8;
McNew J.A., Coe J.G.S., Sogaard M., Zemelman B.V., Wimmer C., Hong W.,
Soellner T.H.;
"Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi
transport.";
FEBS Lett. 435:89-95(1998).
[5]
INTERACTION WITH SFT1; SED5; YKT6; BET1; BOS1; SEC22; PEP12 AND SELF.
PubMed=10591633;
Tsui M.M., Banfield D.K.;
"Yeast Golgi SNARE interactions are promiscuous.";
J. Cell Sci. 113:145-152(2000).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11160819; DOI=10.1091/mbc.12.1.13;
Bensen E.S., Yeung B.G., Payne G.S.;
"Ric1p and the Ypt6p GTPase function in a common pathway required for
localization of trans-Golgi network membrane proteins.";
Mol. Biol. Cell 12:13-26(2001).
[7]
DISRUPTION PHENOTYPE.
PubMed=11689439; DOI=10.1093/emboj/20.21.5991;
Siniossoglou S., Pelham H.R.B.;
"An effector of Ypt6p binds the SNARE Tlg1p and mediates selective
fusion of vesicles with late Golgi membranes.";
EMBO J. 20:5991-5998(2001).
[8]
DISRUPTION PHENOTYPE.
PubMed=12429822; DOI=10.1091/mbc.E02-06-0349;
Gillingham A.K., Pfeifer A.C., Munro S.;
"CASP, the alternatively spliced product of the gene encoding the
CCAAT-displacement protein transcription factor, is a Golgi membrane
protein related to giantin.";
Mol. Biol. Cell 13:3761-3774(2002).
[9]
FUNCTION, AND INTERACTION WITH SED5; YKT6 AND SFT1.
PubMed=11959998; DOI=10.1073/pnas.082100899;
Parlati F., Varlamov O., Paz K., McNew J.A., Hurtado D., Sollner T.H.,
Rothman J.E.;
"Distinct SNARE complexes mediating membrane fusion in Golgi transport
based on combinatorial specificity.";
Proc. Natl. Acad. Sci. U.S.A. 99:5424-5429(2002).
[10]
SUBCELLULAR LOCATION.
PubMed=16107716; DOI=10.1128/MCB.25.17.7696-7710.2005;
Inadome H., Noda Y., Adachi H., Yoda K.;
"Immunoisolaton of the yeast Golgi subcompartments and
characterization of a novel membrane protein, Svp26, discovered in the
Sed5-containing compartments.";
Mol. Cell. Biol. 25:7696-7710(2005).
[11]
SUBCELLULAR LOCATION.
PubMed=16699523; DOI=10.1038/nature04737;
Matsuura-Tokita K., Takeuchi M., Ichihara A., Mikuriya K., Nakano A.;
"Live imaging of yeast Golgi cisternal maturation.";
Nature 441:1007-1010(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, 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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Involved in transport from the ER to the Golgi apparatus
as well as in intra-Golgi transport. It belongs to a super-family
of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-
sensitive factor) attachment protein receptor. Rescues alpha-
factor maturation defects. {ECO:0000269|PubMed:11160819,
ECO:0000269|PubMed:11959998, ECO:0000269|PubMed:9755865}.
-!- SUBUNIT: Component of several multiprotein Golgi SNARE complexes.
Identified in a Golgi SNARE complex consisting of t-SNARES SED5,
YKT6, and the v-SNARE SFT1. Interacts with BET1. Interacts with
BOS1. Interacts with SEC22. Interacts with PEP12. Interacts with
self. {ECO:0000269|PubMed:10591633, ECO:0000269|PubMed:11959998,
ECO:0000269|PubMed:9211930, ECO:0000269|PubMed:9755865}.
-!- INTERACTION:
Q8N6L0:CCDC155 (xeno); NbExp=3; IntAct=EBI-24365, EBI-749265;
Q96BA8:CREB3L1 (xeno); NbExp=3; IntAct=EBI-24365, EBI-6942903;
Q01590:SED5; NbExp=5; IntAct=EBI-24365, EBI-16930;
Q12846:STX4 (xeno); NbExp=3; IntAct=EBI-24365, EBI-744942;
Q8WW34-2:TMEM239 (xeno); NbExp=3; IntAct=EBI-24365, EBI-11528917;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:16699523,
ECO:0000269|PubMed:9755865}; Single-pass type IV membrane protein
{ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:16699523,
ECO:0000269|PubMed:9755865}. Note=Punctate localization pattern.
Localization affected by loss of SVP26, a membrane protein, and is
shifted to the ER.
-!- DISRUPTION PHENOTYPE: Lack of late Golgi SNARE proteins, TLG1 and
TLG2. Spores are temperature sensitive and fail to germinate at 37
degrees Celsius. 10 to 20% of cells possess a variety of aberrant
structures, including fragmentation of the vacuole, a common
occurrence in secretory defects, and substantial accumulation of
membranes in some cells. These structures are considered to be
abnormal Golgi remnants. Endoplasmic reticulum (ER) retention
defective, erd phenotype, which is characterized by hypersecretion
of ER-resident proteins. This results from a defect in retrograde
directed vesicles. Severely compromised viability when another
Golgi protein, COY1P is overexpressed. Incomplete maturation of
alpha-factor via defective localization of KEX2.
{ECO:0000269|PubMed:11160819, ECO:0000269|PubMed:11689439,
ECO:0000269|PubMed:12429822, ECO:0000269|PubMed:9755865}.
-!- SIMILARITY: Belongs to the GOSR1 family. {ECO:0000305}.
-!- CAUTION: Formerly referred to as a v-SNARE. {ECO:0000305}.
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EMBL; U11583; AAB65043.1; -; Genomic_DNA.
EMBL; BK006934; DAA06654.1; -; Genomic_DNA.
PIR; S48937; S48937.
RefSeq; NP_011832.1; NM_001179111.1.
ProteinModelPortal; P38736; -.
SMR; P38736; -.
BioGrid; 36391; 491.
ComplexPortal; CPX-1855; Golgi SNARE complex SED5-GOS1-YKT6-SFT1.
DIP; DIP-2490N; -.
IntAct; P38736; 13.
MINT; P38736; -.
STRING; 4932.YHL031C; -.
iPTMnet; P38736; -.
MaxQB; P38736; -.
PaxDb; P38736; -.
PRIDE; P38736; -.
EnsemblFungi; YHL031C; YHL031C; YHL031C.
GeneID; 856354; -.
KEGG; sce:YHL031C; -.
EuPathDB; FungiDB:YHL031C; -.
SGD; S000001023; GOS1.
GeneTree; ENSGT00390000008688; -.
HOGENOM; HOG000207760; -.
InParanoid; P38736; -.
KO; K08495; -.
OMA; INDKMAE; -.
OrthoDB; EOG092C5G0E; -.
BioCyc; YEAST:G3O-31051-MONOMER; -.
Reactome; R-SCE-6811438; Intra-Golgi traffic.
PRO; PR:P38736; -.
Proteomes; UP000002311; Chromosome VIII.
GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
GO; GO:0005797; C:Golgi medial cisterna; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; ISS:SGD.
GO; GO:0031201; C:SNARE complex; IDA:SGD.
GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0048193; P:Golgi vesicle transport; IMP:SGD.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0048209; P:regulation of vesicle targeting, to, from or within Golgi; IBA:GO_Central.
GO; GO:0006906; P:vesicle fusion; IDA:SGD.
InterPro; IPR023601; Golgi_SNAP_su1.
PANTHER; PTHR21094; PTHR21094; 1.
PIRSF; PIRSF027109; Golgi_SNARE; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; ER-Golgi transport; Golgi apparatus;
Membrane; Phosphoprotein; Protein transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 223 Golgi SNAP receptor complex member 1.
/FTId=PRO_0000212557.
TOPO_DOM 2 204 Cytoplasmic. {ECO:0000255}.
TRANSMEM 205 222 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 223 223 Vesicular. {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
SEQUENCE 223 AA; 25395 MW; 1E833249CCC306C2 CRC64;
MSSQPSFVTI RGKAISLETQ TESLLSKYST FAQTTSSEQT GQEKKIDKQL EGILGQRQDV
IDSLTQICDS NPAISASKLS QLHRHKEILQ DHWKSFRNIR SSIQQERNRL NLLFSVKNDI
ANSTTDAPAP IGDADEYIQN ETRRIDQSNN VVDRLISQAW ETRSQFHSQS NVLNTANNKV
LQTLQRIPGV NQLIMKINTR RKKNAFVLAT ITTLCILFLF FTW


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