GOSR1_YEAST
ID GOSR1_YEAST Reviewed; 223 AA.
AC P38736; D3DKT7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Golgi SNAP receptor complex member 1;
DE AltName: Full=Golgi SNARE protein 1;
DE AltName: Full=Protein transport protein GOS1;
GN Name=GOS1; OrderedLocusNames=YHL031C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP INTERACTION WITH SED5.
RX PubMed=9211930; DOI=10.1074/jbc.272.28.17776;
RA McNew J.A., Soegaard M., Lampen N.M., Machida S., Ye R.R., Lacomis L.,
RA Tempst P., Rothman J.E., Soellner T.H.;
RT "Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi
RT transport.";
RL J. Biol. Chem. 272:17776-17783(1997).
RN [4]
RP FUNCTION, INTERACTION WITH SED5, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9755865; DOI=10.1016/s0014-5793(98)01044-8;
RA McNew J.A., Coe J.G.S., Sogaard M., Zemelman B.V., Wimmer C., Hong W.,
RA Soellner T.H.;
RT "Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi
RT transport.";
RL FEBS Lett. 435:89-95(1998).
RN [5]
RP INTERACTION WITH SFT1; SED5; YKT6; BET1; BOS1; SEC22; PEP12 AND SELF.
RX PubMed=10591633; DOI=10.1242/jcs.113.1.145;
RA Tsui M.M., Banfield D.K.;
RT "Yeast Golgi SNARE interactions are promiscuous.";
RL J. Cell Sci. 113:145-152(2000).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11160819; DOI=10.1091/mbc.12.1.13;
RA Bensen E.S., Yeung B.G., Payne G.S.;
RT "Ric1p and the Ypt6p GTPase function in a common pathway required for
RT localization of trans-Golgi network membrane proteins.";
RL Mol. Biol. Cell 12:13-26(2001).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=11689439; DOI=10.1093/emboj/20.21.5991;
RA Siniossoglou S., Pelham H.R.B.;
RT "An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion
RT of vesicles with late Golgi membranes.";
RL EMBO J. 20:5991-5998(2001).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=12429822; DOI=10.1091/mbc.e02-06-0349;
RA Gillingham A.K., Pfeifer A.C., Munro S.;
RT "CASP, the alternatively spliced product of the gene encoding the CCAAT-
RT displacement protein transcription factor, is a Golgi membrane protein
RT related to giantin.";
RL Mol. Biol. Cell 13:3761-3774(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH SED5; YKT6 AND SFT1.
RX PubMed=11959998; DOI=10.1073/pnas.082100899;
RA Parlati F., Varlamov O., Paz K., McNew J.A., Hurtado D., Sollner T.H.,
RA Rothman J.E.;
RT "Distinct SNARE complexes mediating membrane fusion in Golgi transport
RT based on combinatorial specificity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5424-5429(2002).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005;
RA Inadome H., Noda Y., Adachi H., Yoda K.;
RT "Immunoisolation of the yeast Golgi subcompartments and characterization of
RT a novel membrane protein, Svp26, discovered in the Sed5-containing
RT compartments.";
RL Mol. Cell. Biol. 25:7696-7710(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=16699523; DOI=10.1038/nature04737;
RA Matsuura-Tokita K., Takeuchi M., Ichihara A., Mikuriya K., Nakano A.;
RT "Live imaging of yeast Golgi cisternal maturation.";
RL Nature 441:1007-1010(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in transport from the ER to the Golgi apparatus as
CC well as in intra-Golgi transport. It belongs to a super-family of
CC proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive
CC factor) attachment protein receptor. Rescues alpha-factor maturation
CC defects. {ECO:0000269|PubMed:11160819, ECO:0000269|PubMed:11959998,
CC ECO:0000269|PubMed:9755865}.
CC -!- SUBUNIT: Component of several multiprotein Golgi SNARE complexes.
CC Identified in a Golgi SNARE complex consisting of t-SNARES SED5, YKT6,
CC and the v-SNARE SFT1. Interacts with BET1. Interacts with BOS1.
CC Interacts with SEC22. Interacts with PEP12. Interacts with self.
CC {ECO:0000269|PubMed:10591633, ECO:0000269|PubMed:11959998,
CC ECO:0000269|PubMed:9211930, ECO:0000269|PubMed:9755865}.
CC -!- INTERACTION:
CC P38736; Q01590: SED5; NbExp=6; IntAct=EBI-24365, EBI-16930;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:16699523,
CC ECO:0000269|PubMed:9755865}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:16699523,
CC ECO:0000269|PubMed:9755865}. Note=Punctate localization pattern.
CC Localization affected by loss of SVP26, a membrane protein, and is
CC shifted to the ER.
CC -!- DISRUPTION PHENOTYPE: Lack of late Golgi SNARE proteins, TLG1 and TLG2.
CC Spores are temperature sensitive and fail to germinate at 37 degrees
CC Celsius. 10 to 20% of cells possess a variety of aberrant structures,
CC including fragmentation of the vacuole, a common occurrence in
CC secretory defects, and substantial accumulation of membranes in some
CC cells. These structures are considered to be abnormal Golgi remnants.
CC Endoplasmic reticulum (ER) retention defective, erd phenotype, which is
CC characterized by hypersecretion of ER-resident proteins. This results
CC from a defect in retrograde directed vesicles. Severely compromised
CC viability when another Golgi protein, COY1P is overexpressed.
CC Incomplete maturation of alpha-factor via defective localization of
CC KEX2. {ECO:0000269|PubMed:11160819, ECO:0000269|PubMed:11689439,
CC ECO:0000269|PubMed:12429822, ECO:0000269|PubMed:9755865}.
CC -!- SIMILARITY: Belongs to the GOSR1 family. {ECO:0000305}.
CC -!- CAUTION: Formerly referred to as a v-SNARE. {ECO:0000305}.
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DR EMBL; U11583; AAB65043.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06654.1; -; Genomic_DNA.
DR PIR; S48937; S48937.
DR RefSeq; NP_011832.1; NM_001179111.1.
DR AlphaFoldDB; P38736; -.
DR SMR; P38736; -.
DR BioGRID; 36391; 497.
DR ComplexPortal; CPX-1855; Golgi SNARE complex SED5-GOS1-SFT1-YKT6.
DR DIP; DIP-2490N; -.
DR IntAct; P38736; 9.
DR MINT; P38736; -.
DR STRING; 4932.YHL031C; -.
DR iPTMnet; P38736; -.
DR MaxQB; P38736; -.
DR PaxDb; P38736; -.
DR PRIDE; P38736; -.
DR EnsemblFungi; YHL031C_mRNA; YHL031C; YHL031C.
DR GeneID; 856354; -.
DR KEGG; sce:YHL031C; -.
DR SGD; S000001023; GOS1.
DR VEuPathDB; FungiDB:YHL031C; -.
DR eggNOG; KOG3208; Eukaryota.
DR GeneTree; ENSGT00390000008688; -.
DR HOGENOM; CLU_078034_1_1_1; -.
DR InParanoid; P38736; -.
DR OMA; QAYAVND; -.
DR BioCyc; YEAST:G3O-31051-MON; -.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811438; Intra-Golgi traffic.
DR PRO; PR:P38736; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38736; protein.
DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:1990674; C:Golgi cis cisterna membrane; IC:ComplexPortal.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR GO; GO:0048193; P:Golgi vesicle transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IDA:ComplexPortal.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IC:ComplexPortal.
DR InterPro; IPR023601; Golgi_SNAP_su1.
DR PANTHER; PTHR21094; PTHR21094; 1.
DR PIRSF; PIRSF027109; Golgi_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..223
FT /note="Golgi SNAP receptor complex member 1"
FT /id="PRO_0000212557"
FT TOPO_DOM 2..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..222
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ 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
