SNC2_YEAST
ID SNC2_YEAST Reviewed; 115 AA.
AC P33328; D6W324;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Synaptobrevin homolog 2;
GN Name=SNC2; OrderedLocusNames=YOR327C;
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=S288c / GRF88;
RX PubMed=8374953; DOI=10.1016/0092-8674(93)90465-3;
RA Protopopov V., Govidan B., Novick P., Gerst J.E.;
RT "Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins
RT function on the late secretory pathway in S. cerevisiae.";
RL Cell 74:855-861(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896263;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<999::aid-yea976>3.0.co;2-e;
RA Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
RT "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces
RT cerevisiae chromosome XV: similarity to part of chromosome I.";
RL Yeast 12:999-1004(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [7]
RP PALMITOYLATION AT CYS-94.
RX PubMed=15973437; DOI=10.1038/sj.emboj.7600724;
RA Valdez-Taubas J., Pelham H.R.B.;
RT "Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its
RT ubiquitination and degradation.";
RL EMBO J. 24:2524-2532(2005).
RN [8]
RP PALMITOYLATION.
RX PubMed=16751107; DOI=10.1016/j.cell.2006.03.042;
RA Roth A.F., Wan J., Bailey A.O., Sun B., Kuchar J.A., Green W.N.,
RA Phinney B.S., Yates J.R. III, Davis N.G.;
RT "Global analysis of protein palmitoylation in yeast.";
RL Cell 125:1003-1013(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, 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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: SNC1 and SNC2 are vesicle-targeting proteins essential for
CC normal secretory traffic between the Golgi and the plasma membrane.
CC They may also be involved in vesicle fusion.
CC -!- INTERACTION:
CC P33328; P32867: SSO1; NbExp=2; IntAct=EBI-17512, EBI-2206525;
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Single-pass type IV membrane
CC protein. Note=Post-Golgi vesicle membrane. {ECO:0000305}.
CC -!- PTM: Palmitoylated by SWF1. {ECO:0000269|PubMed:15973437,
CC ECO:0000269|PubMed:16751107}.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; L16243; AAA19816.1; -; Unassigned_DNA.
DR EMBL; Z49821; CAA89974.1; -; Genomic_DNA.
DR EMBL; Z75235; CAA99647.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11090.1; -; Genomic_DNA.
DR PIR; S62059; S62059.
DR RefSeq; NP_014972.3; NM_001183747.3.
DR AlphaFoldDB; P33328; -.
DR SMR; P33328; -.
DR BioGRID; 34712; 309.
DR ComplexPortal; CPX-5321; Endosomal SNARE complex TLG2-VTI1-TLG1-SNC2.
DR ComplexPortal; CPX-5461; Endosomal SNARE complex PEP12-VTI1-SYN8-SNC2.
DR ComplexPortal; CPX-5462; Endosomal SNARE complex PEP12-VTI1-TLG1-SNC2.
DR ComplexPortal; CPX-5463; Vesicular SNARE complex SSO1-SEC9-SNC2.
DR ComplexPortal; CPX-5465; Vesicular SNARE complex SSO2-SEC9-SNC2.
DR ComplexPortal; CPX-5466; Vesicular SNARE complex SSO1-SPO20-SNC2.
DR DIP; DIP-4667N; -.
DR IntAct; P33328; 13.
DR MINT; P33328; -.
DR STRING; 4932.YOR327C; -.
DR TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; P33328; -.
DR SwissPalm; P33328; -.
DR MaxQB; P33328; -.
DR PaxDb; P33328; -.
DR PRIDE; P33328; -.
DR TopDownProteomics; P33328; -.
DR EnsemblFungi; YOR327C_mRNA; YOR327C; YOR327C.
DR GeneID; 854505; -.
DR KEGG; sce:YOR327C; -.
DR SGD; S000005854; SNC2.
DR VEuPathDB; FungiDB:YOR327C; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000155005; -.
DR HOGENOM; CLU_064620_2_1_1; -.
DR InParanoid; P33328; -.
DR OMA; CQDTFAT; -.
DR BioCyc; YEAST:G3O-33804-MON; -.
DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013026; RHOB GTPase cycle.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:P33328; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P33328; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IC:ComplexPortal.
DR GO; GO:0031201; C:SNARE complex; IPI:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0030658; C:transport vesicle membrane; IDA:SGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IC:ComplexPortal.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
DR GO; GO:0006887; P:exocytosis; IMP:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IC:ComplexPortal.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IC:ComplexPortal.
DR GO; GO:0043934; P:sporulation; IDA:ComplexPortal.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0099500; P:vesicle fusion to plasma membrane; IC:ComplexPortal.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IC:ComplexPortal.
DR DisProt; DP01502; -.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR016444; Synaptobrevin/VAMP.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45701; PTHR45701; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..115
FT /note="Synaptobrevin homolog 2"
FT /id="PRO_0000206745"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..112
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..115
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 27..87
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT LIPID 94
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15973437"
FT CROSSLNK 62
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 115
FT /note="S -> T (in Ref. 1; AAA19816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 115 AA; 12957 MW; 815F027FAD8A599B CRC64;
MSSSVPYDPY VPPEESNSGA NPNSQNKTAA LRQEIDDTVG IMRDNINKVA ERGERLTSIE
DKADNLAISA QGFKRGANRV RKQMWWKDLK MRMCLFLVVI ILLVVIIVPI VVHFS
