NYV1_YEAST
ID NYV1_YEAST Reviewed; 253 AA.
AC Q12255; D6VY93;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Vacuolar v-SNARE NYV1;
DE Short=R-SNARE NYV1;
DE AltName: Full=New v-SNARE 1;
DE AltName: Full=Synaptobrevin NYV1;
GN Name=NYV1; Synonyms=MAM2; OrderedLocusNames=YLR093C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 14-27; 108-143 AND 196-214, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [5]
RP FUNCTION, AND INTERACTION WITH VAM3.
RX PubMed=9144293; DOI=10.1038/387199a0;
RA Nichols B.J., Ungermann C., Pelham H.R.B., Wickner W.T., Haas A.;
RT "Homotypic vacuolar fusion mediated by t- and v-SNAREs.";
RL Nature 387:199-202(1997).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10385523; DOI=10.1083/jcb.145.7.1435;
RA Ungermann C., Fischer von Mollard G., Jensen O.N., Margolis N.,
RA Stevens T.H., Wickner W.T.;
RT "Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex
RT on isolated vacuoles, are essential for homotypic fusion.";
RL J. Cell Biol. 145:1435-1442(1999).
RN [7]
RP IDENTIFICATION OF INTRON.
RX PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT "Test of intron predictions reveals novel splice sites, alternatively
RT spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL Nucleic Acids Res. 28:1700-1706(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH PMC1.
RX PubMed=11080502; DOI=10.1074/jbc.m009191200;
RA Takita Y., Engstrom L., Ungermann C., Cunningham K.W.;
RT "Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p.";
RL J. Biol. Chem. 276:6200-6206(2001).
RN [9]
RP INTERACTION WITH THE VTC COMPLEX.
RX PubMed=11823419; DOI=10.1093/emboj/21.3.259;
RA Mueller O., Bayer M.J., Peters C., Andersen J.S., Mann M., Mayer A.;
RT "The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-
RT complex formation.";
RL EMBO J. 21:259-269(2002).
RN [10]
RP FUNCTION.
RX PubMed=14734531; DOI=10.1083/jcb.200310105;
RA Merz A.J., Wickner W.T.;
RT "Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole
RT lumen.";
RL J. Cell Biol. 164:195-206(2004).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
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 [13]
RP STRUCTURE BY NMR OF 1-149.
RX PubMed=16855025; DOI=10.1091/mbc.e06-02-0128;
RA Wen W., Chen L., Wu H., Sun X., Zhang M., Banfield D.K.;
RT "Identification of the yeast R-SNARE Nyv1p as a novel longin domain-
RT containing protein.";
RL Mol. Biol. Cell 17:4282-4299(2006).
CC -!- FUNCTION: Vacuolar v-SNARE required for docking. Only involved in
CC homotypic vacuole fusion. Required for Ca(2+) efflux from the vacuolar
CC lumen, a required signal for subsequent membrane fusion events, by
CC inhibiting vacuolar Ca(2+)-ATPase PMC1 and promoting Ca(2+) release
CC when forming trans-SNARE assemblies during the docking step.
CC {ECO:0000269|PubMed:10385523, ECO:0000269|PubMed:11080502,
CC ECO:0000269|PubMed:14734531, ECO:0000269|PubMed:9144293}.
CC -!- SUBUNIT: Present in a pentameric cis-SNARE complex composed of the v-
CC SNAREs NYV1, VTI1 and YKT6, and the t-SNAREs VAM3 and VAM7 on vacuolar
CC membranes. Interacts in trans with the cognate t-SNARE VAM3 during the
CC docking step of homotypic vacuolar fusion. Interacts with the vacuolar
CC transporter chaperone (VTC) complex and the vacuolar Ca(2+)-ATPase
CC PMC1. {ECO:0000269|PubMed:10385523, ECO:0000269|PubMed:11080502,
CC ECO:0000269|PubMed:11823419, ECO:0000269|PubMed:9144293}.
CC -!- INTERACTION:
CC Q12255; Q12154: GET3; NbExp=3; IntAct=EBI-35465, EBI-2989;
CC Q12255; Q12241: VAM3; NbExp=21; IntAct=EBI-35465, EBI-20227;
CC Q12255; P32912: VAM7; NbExp=11; IntAct=EBI-35465, EBI-20232;
CC Q12255; Q04338: VTI1; NbExp=11; IntAct=EBI-35465, EBI-20519;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Single-pass type IV membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1885 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67537.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAT92805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA97654.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z73265; CAA97654.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U53876; AAB67537.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY692786; AAT92805.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006945; DAA09409.1; -; Genomic_DNA.
DR PIR; S64927; S64927.
DR RefSeq; NP_013194.2; NM_001181980.1.
DR PDB; 2FZ0; NMR; -; A=1-149.
DR PDBsum; 2FZ0; -.
DR AlphaFoldDB; Q12255; -.
DR SMR; Q12255; -.
DR BioGRID; 31366; 83.
DR ComplexPortal; CPX-5401; Vacuolar SNARE complex VAM3-VTI1-VAM7-NYV1.
DR ComplexPortal; CPX-5521; Vacuolar SNARE complex SSO1-SEC9-NYV1.
DR DIP; DIP-2248N; -.
DR IntAct; Q12255; 16.
DR MINT; Q12255; -.
DR STRING; 4932.YLR093C; -.
DR TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; Q12255; -.
DR MaxQB; Q12255; -.
DR PaxDb; Q12255; -.
DR PRIDE; Q12255; -.
DR TopDownProteomics; Q12255; -.
DR EnsemblFungi; YLR093C_mRNA; YLR093C; YLR093C.
DR GeneID; 850782; -.
DR KEGG; sce:YLR093C; -.
DR SGD; S000004083; NYV1.
DR VEuPathDB; FungiDB:YLR093C; -.
DR eggNOG; KOG0860; Eukaryota.
DR HOGENOM; CLU_1107824_0_0_1; -.
DR InParanoid; Q12255; -.
DR OMA; DGYDCYY; -.
DR BioCyc; YEAST:G3O-32243-MON; -.
DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR EvolutionaryTrace; Q12255; -.
DR PRO; PR:Q12255; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12255; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
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; IC:ComplexPortal.
DR GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IDA:ComplexPortal.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0007036; P:vacuolar calcium ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0099500; P:vesicle fusion to plasma membrane; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR Gene3D; 3.30.450.230; -; 1.
DR InterPro; IPR038426; Nyv1_longin_sf.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR019005; Vacuolar_R-SNAR_Nyv1_longi_dom.
DR Pfam; PF09426; Nyv1_N; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Direct protein sequencing; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..253
FT /note="Vacuolar v-SNARE NYV1"
FT /id="PRO_0000206780"
FT TOPO_DOM 1..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT DOMAIN 167..227
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 147..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:2FZ0"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:2FZ0"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2FZ0"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:2FZ0"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2FZ0"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2FZ0"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2FZ0"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:2FZ0"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:2FZ0"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:2FZ0"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:2FZ0"
SQ SEQUENCE 253 AA; 28964 MW; 494B587CF0F85997 CRC64;
MKRFNVSYVE VIKNGETISS CFQPFQKNEN YGTITSANEQ ITPVIFHNLI MDMVLPKVVP
IKGNKVTKMS MNLIDGFDCF YSTDDHDPKT VYVCFTLVDM PKILPIRILS GLQEYESNAT
NELLSSHVGQ ILDSFHEELV EYRNQTLNSS GNGQSSNGNG QNTISDIGDA TEDQIKDVIQ
IMNDNIDKFL ERQERVSLLV DKTSQLNSSS NKFRRKAVNI KEIMWWQKVK NITLLTFTII
LFVSAAFMFF YLW
