SSO1_YEAST
ID SSO1_YEAST Reviewed; 290 AA.
AC P32867; D6W3D8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Protein SSO1;
GN Name=SSO1; OrderedLocusNames=YPL232W; ORFNames=P1405;
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.
RC STRAIN=ATCC 26787 / X2180-1B;
RX PubMed=8223426; DOI=10.1002/j.1460-2075.1993.tb06093.x;
RA Aalto M.K., Ronne H., Keraenen S.;
RT "Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane
RT proteins that function in vesicular transport.";
RL EMBO J. 12:4095-4104(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RA Schueller H.-J.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2900835; DOI=10.1016/s0021-9258(18)37757-3;
RA Mohamed A.H., Chirala S.S., Mody N.H., Huang W.Y., Wakil S.J.;
RT "Primary structure of the multifunctional alpha subunit protein of yeast
RT fatty acid synthase derived from FAS2 gene sequence.";
RL J. Biol. Chem. 263:12315-12325(1988).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Required for vesicle fusion with the plasma membrane.
CC -!- INTERACTION:
CC P32867; P22214: SEC22; NbExp=2; IntAct=EBI-2206525, EBI-16577;
CC P32867; P40357: SEC9; NbExp=14; IntAct=EBI-2206525, EBI-16904;
CC P32867; P33328: SNC2; NbExp=2; IntAct=EBI-2206525, EBI-17512;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; X67729; CAA47959.1; -; mRNA.
DR EMBL; X76890; CAA54217.1; -; Genomic_DNA.
DR EMBL; X94561; CAA64255.1; -; Genomic_DNA.
DR EMBL; Z73588; CAA97949.1; -; Genomic_DNA.
DR EMBL; J03936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006949; DAA11204.1; -; Genomic_DNA.
DR PIR; S39569; S39569.
DR RefSeq; NP_015092.1; NM_001184046.1.
DR PDB; 1FIO; X-ray; 2.10 A; A=31-225.
DR PDB; 3B5N; X-ray; 1.60 A; B/F/J=189-257.
DR PDBsum; 1FIO; -.
DR PDBsum; 3B5N; -.
DR AlphaFoldDB; P32867; -.
DR BMRB; P32867; -.
DR SMR; P32867; -.
DR BioGRID; 35930; 141.
DR ComplexPortal; CPX-1365; Vesicular SNARE complex SSO1-SEC9-SNC1.
DR ComplexPortal; CPX-5463; Vesicular SNARE complex SSO1-SEC9-SNC2.
DR ComplexPortal; CPX-5464; Vesicular SNARE complex SSO1-SPO20-SNC1.
DR ComplexPortal; CPX-5466; Vesicular SNARE complex SSO1-SPO20-SNC2.
DR ComplexPortal; CPX-5521; Vacuolar SNARE complex SSO1-SEC9-NYV1.
DR DIP; DIP-2494N; -.
DR IntAct; P32867; 7.
DR STRING; 4932.YPL232W; -.
DR TCDB; 8.A.91.1.5; the syntaxin (syntaxin) family.
DR iPTMnet; P32867; -.
DR SwissPalm; P32867; -.
DR MaxQB; P32867; -.
DR PaxDb; P32867; -.
DR PRIDE; P32867; -.
DR EnsemblFungi; YPL232W_mRNA; YPL232W; YPL232W.
DR GeneID; 855844; -.
DR KEGG; sce:YPL232W; -.
DR SGD; S000006153; SSO1.
DR VEuPathDB; FungiDB:YPL232W; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_042423_0_1_1; -.
DR InParanoid; P32867; -.
DR OMA; ARRWKWY; -.
DR BioCyc; YEAST:G3O-34119-MON; -.
DR Reactome; R-SCE-114516; Disinhibition of SNARE formation.
DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-SCE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; P32867; -.
DR PRO; PR:P32867; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32867; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:SGD.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IPI:CAFA.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IC:ComplexPortal.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0035493; P:SNARE complex assembly; IMP:CAFA.
DR GO; GO:0043934; P:sporulation; IDA:ComplexPortal.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0099500; P:vesicle fusion to plasma membrane; IC:ComplexPortal.
DR CDD; cd00179; SynN; 1.
DR DisProt; DP01503; -.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..290
FT /note="Protein SSO1"
FT /id="PRO_0000210274"
FT TOPO_DOM 1..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..287
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 190..252
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT CONFLICT 97
FT /note="E -> G (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="G -> V (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 31..64
FT /evidence="ECO:0007829|PDB:1FIO"
FT HELIX 70..104
FT /evidence="ECO:0007829|PDB:1FIO"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1FIO"
FT HELIX 109..151
FT /evidence="ECO:0007829|PDB:1FIO"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:1FIO"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:1FIO"
FT HELIX 190..256
FT /evidence="ECO:0007829|PDB:3B5N"
SQ SEQUENCE 290 AA; 33106 MW; 6E4C6D35C3CD9D94 CRC64;
MSYNNPYQLE TPFEESYELD EGSSAIGAEG HDFVGFMNKI SQINRDLDKY DHTINQVDSL
HKRLLTEVNE EQASHLRHSL DNFVAQATDL QFKLKNEIKS AQRDGIHDTN KQAQAENSRQ
RFLKLIQDYR IVDSNYKEEN KEQAKRQYMI IQPEATEDEV EAAISDVGGQ QIFSQALLNA
NRRGEAKTAL AEVQARHQEL LKLEKSMAEL TQLFNDMEEL VIEQQENVDV IDKNVEDAQL
DVEQGVGHTD KAVKSARKAR KNKIRCWLIV FAIIVVVVVV VVVPAVVKTR
