ID   SSO2_YEAST              Reviewed;         295 AA.
AC   P39926; D6W007;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 197.
DE   RecName: Full=Protein SSO2;
GN   Name=SSO2; OrderedLocusNames=YMR183C; ORFNames=YM8010.13C;
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 [MRNA].
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872; DOI=10.1038/387s090;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-34, AND
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).
CC   -!- FUNCTION: Required for vesicle fusion with the plasma membrane.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC       membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X67730; CAA47960.1; -; mRNA.
DR   EMBL; Z49808; CAA89916.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10081.1; -; Genomic_DNA.
DR   PIR; S55130; S55130.
DR   RefSeq; NP_013908.1; NM_001182689.1.
DR   PDB; 5LG4; X-ray; 2.90 A; A=36-227.
DR   PDB; 5M4Y; X-ray; 2.20 A; A/C/E=36-227.
DR   PDB; 7Q83; X-ray; 2.19 A; B/D=1-270.
DR   AlphaFoldDB; P39926; -.
DR   SMR; P39926; -.
DR   BioGRID; 35361; 406.
DR   ComplexPortal; CPX-1369; Vesicular SNARE complex SSO2-SEC9-SNC1.
DR   ComplexPortal; CPX-5465; Vesicular SNARE complex SSO2-SEC9-SNC2.
DR   DIP; DIP-2951N; -.
DR   FunCoup; P39926; 652.
DR   IntAct; P39926; 17.
DR   MINT; P39926; -.
DR   STRING; 4932.YMR183C; -.
DR   TCDB; 8.A.91.1.5; the syntaxin (syntaxin) family.
DR   CarbonylDB; P39926; -.
DR   iPTMnet; P39926; -.
DR   SwissPalm; P39926; -.
DR   PaxDb; 4932-YMR183C; -.
DR   PeptideAtlas; P39926; -.
DR   EnsemblFungi; YMR183C_mRNA; YMR183C; YMR183C.
DR   GeneID; 855221; -.
DR   KEGG; sce:YMR183C; -.
DR   AGR; SGD:S000004795; -.
DR   SGD; S000004795; SSO2.
DR   VEuPathDB; FungiDB:YMR183C; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   HOGENOM; CLU_042423_0_1_1; -.
DR   InParanoid; P39926; -.
DR   OMA; RWICFIL; -.
DR   OrthoDB; 10255013at2759; -.
DR   BioCyc; YEAST:G3O-32871-MONOMER; -.
DR   Reactome; R-SCE-114516; Disinhibition of SNARE formation.
DR   Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR   Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR   Reactome; R-SCE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   BioGRID-ORCS; 855221; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P39926; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P39926; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; NAS: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; IPI:ComplexPortal.
DR   GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR   GO; GO:0005484; F:SNAP receptor activity; IPI:SGD.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0031321; P:ascospore-type prospore assembly; IGI:SGD.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; TAS:SGD.
DR   GO; GO:0048210; P:Golgi vesicle fusion to target membrane; NAS:ComplexPortal.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:ComplexPortal.
DR   GO; GO:0072660; P:maintenance of protein location in plasma membrane; IGI:SGD.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IDA:ComplexPortal.
DR   GO; GO:0099500; P:vesicle fusion to plasma membrane; NAS:ComplexPortal.
DR   CDD; cd15849; SNARE_Sso1; 1.
DR   CDD; cd00179; SynN; 1.
DR   DisProt; DP01504; -.
DR   FunFam; 1.20.58.70:FF:000008; Syntaxin family protein; 1.
DR   Gene3D; 1.20.58.70; -; 1.
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:SF307; PROTEIN SSO1-RELATED; 1.
DR   PANTHER; PTHR19957; SYNTAXIN; 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; t-snare proteins; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
DR   PDBsum; 5LG4; -.
DR   PDBsum; 5M4Y; -.
DR   PDBsum; 7Q83; -.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..295
FT                   /note="Protein SSO2"
FT                   /id="PRO_0000210275"
FT   TOPO_DOM        1..269
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..291
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          194..256
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   COILED          39..100
FT                   /evidence="ECO:0000255"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        222
FT                   /note="E -> K (in Ref. 1; CAA47960)"
FT                   /evidence="ECO:0000305"
FT   HELIX           36..69
FT                   /evidence="ECO:0007829|PDB:7Q83"
FT   HELIX           74..108
FT                   /evidence="ECO:0007829|PDB:7Q83"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:7Q83"
FT   HELIX           113..148
FT                   /evidence="ECO:0007829|PDB:7Q83"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:5LG4"
FT   HELIX           161..168
FT                   /evidence="ECO:0007829|PDB:5M4Y"
FT   STRAND          169..172
FT                   /evidence="ECO:0007829|PDB:5M4Y"
FT   TURN            174..177
FT                   /evidence="ECO:0007829|PDB:5LG4"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:5LG4"
FT   HELIX           199..222
FT                   /evidence="ECO:0007829|PDB:7Q83"
SQ   SEQUENCE   295 AA;  33734 MW;  454CF2B45FFE8E22 CRC64;
     MSNANPYENN NPYAENYEMQ EDLNNAPTGH SDGSDDFVAF MNKINSINAN LSRYENIINQ
     IDAQHKDLLT QVSEEQEMEL RRSLDDYISQ ATDLQYQLKA DIKDAQRDGL HDSNKQAQAE
     NCRQKFLKLI QDYRIIDSNY KEESKEQAKR QYTIIQPEAT DEEVEAAIND VNGQQIFSQA
     LLNANRRGEA KTALAEVQAR HQELLKLEKT MAELTQLFND MEELVIEQQE NVDVIDKNVE
     DAQQDVEQGV GHTNKAVKSA RKARKNKIRC LIICFIIFAI VVVVVVVPSV VETRK
//