ID   VAM7_YEAST              Reviewed;         316 AA.
AC   P32912; D6VTU3;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=Vacuolar morphogenesis protein 7;
GN   Name=VAM7; OrderedLocusNames=YGL212W;
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 [GENOMIC DNA].
RC   STRAIN=YWH019-7A;
RX   PubMed=1526999; DOI=10.1016/s0021-9258(19)37013-9;
RA   Wada Y., Anraku Y.;
RT   "Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae.
RT   II. VAM7, a gene for regulating morphogenic assembly of the vacuoles.";
RL   J. Biol. Chem. 267:18671-18675(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9153757;
RX   DOI=10.1002/(sici)1097-0061(199704)13:5<475::aid-yea101>3.0.co;2-0;
RA   Feuermann M., Simeonava L., Souciet J.-L., Potier S.;
RT   "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII
RT   reveals 11 open reading frames: two correspond to new genes.";
RL   Yeast 13:475-477(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8813766;
RX   DOI=10.1002/(sici)1097-0061(19960630)12:8<799::aid-yea965>3.0.co;2-u;
RA   Kail M., Juettner E., Vaux D.;
RT   "Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces
RT   cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and
RT   containing three novel transcribed open reading frames.";
RL   Yeast 12:799-807(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [5]
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   [6]
RP   CHARACTERIZATION.
RX   PubMed=9710615; DOI=10.1128/mcb.18.9.5308;
RA   Sato T.K., Darsow T., Emr S.D.;
RT   "Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function
RT   together in yeast vacuolar protein trafficking.";
RL   Mol. Cell. Biol. 18:5308-5319(1998).
RN   [7]
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   [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).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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: Essential for proper morphogenesis of the vacuole. May exist
CC       as structural reinforcement on the surface of the vacuolar membrane and
CC       be required for maintenance against rupture by osmotic pressure.
CC   -!- SUBUNIT: Possibly multimeric. Associates with VAM3.
CC   -!- INTERACTION:
CC       P32912; Q12255: NYV1; NbExp=11; IntAct=EBI-20232, EBI-35465;
CC       P32912; Q12270: RBD2; NbExp=3; IntAct=EBI-20232, EBI-31471;
CC       P32912; Q12241: VAM3; NbExp=11; IntAct=EBI-20232, EBI-20227;
CC       P32912; P20795: VPS33; NbExp=4; IntAct=EBI-20232, EBI-20395;
CC       P32912; P53845: YIF1; NbExp=3; IntAct=EBI-20232, EBI-28230;
CC   -!- SUBCELLULAR LOCATION: Vacuole.
CC   -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; D11379; BAA01977.1; -; Genomic_DNA.
DR   EMBL; U33754; AAC49494.1; -; Genomic_DNA.
DR   EMBL; Z72734; CAA96928.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07904.1; -; Genomic_DNA.
DR   PIR; S31263; S31263.
DR   RefSeq; NP_011303.1; NM_001181077.1.
DR   PDB; 1KMD; NMR; -; A=8-124.
DR   PDBsum; 1KMD; -.
DR   AlphaFoldDB; P32912; -.
DR   SMR; P32912; -.
DR   BioGRID; 33044; 715.
DR   ComplexPortal; CPX-1887; Vacuolar SNARE complex VAM3-VTI1-VAM7-YKT6.
DR   ComplexPortal; CPX-5401; Vacuolar SNARE complex VAM3-VTI1-VAM7-NYV1.
DR   DIP; DIP-1722N; -.
DR   IntAct; P32912; 36.
DR   MINT; P32912; -.
DR   STRING; 4932.YGL212W; -.
DR   TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR   iPTMnet; P32912; -.
DR   MaxQB; P32912; -.
DR   PaxDb; 4932-YGL212W; -.
DR   PeptideAtlas; P32912; -.
DR   EnsemblFungi; YGL212W_mRNA; YGL212W; YGL212W.
DR   GeneID; 852660; -.
DR   KEGG; sce:YGL212W; -.
DR   AGR; SGD:S000003180; -.
DR   SGD; S000003180; VAM7.
DR   VEuPathDB; FungiDB:YGL212W; -.
DR   eggNOG; KOG3202; Eukaryota.
DR   HOGENOM; CLU_033748_1_0_1; -.
DR   InParanoid; P32912; -.
DR   OMA; DSFDTRW; -.
DR   OrthoDB; 2019972at2759; -.
DR   BioCyc; YEAST:G3O-30689-MONOMER; -.
DR   BioGRID-ORCS; 852660; 7 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P32912; -.
DR   PRO; PR:P32912; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P32912; Protein.
DR   GO; GO:0000421; C:autophagosome membrane; EXP:ComplexPortal.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR   GO; GO:0031201; C:SNARE complex; IMP:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:ComplexPortal.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR   GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0061911; P:amphisome-lysosome fusion; NAS:ComplexPortal.
DR   GO; GO:0061909; P:autophagosome-lysosome fusion; IMP:SGD.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
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:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR   CDD; cd06897; PX_SNARE; 1.
DR   CDD; cd15858; SNARE_VAM7; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Reference proteome; Vacuole.
FT   CHAIN           1..316
FT                   /note="Vacuolar morphogenesis protein 7"
FT                   /id="PRO_0000065760"
FT   DOMAIN          1..124
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   DOMAIN          250..312
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   COILED          168..186
FT                   /evidence="ECO:0000255"
FT   STRAND          16..22
FT                   /evidence="ECO:0007829|PDB:1KMD"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:1KMD"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:1KMD"
FT   HELIX           42..56
FT                   /evidence="ECO:0007829|PDB:1KMD"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:1KMD"
FT   HELIX           92..100
FT                   /evidence="ECO:0007829|PDB:1KMD"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:1KMD"
FT   HELIX           112..117
FT                   /evidence="ECO:0007829|PDB:1KMD"
SQ   SEQUENCE   316 AA;  36711 MW;  2F992AEC0ACBC8FE CRC64;
     MAANSVGKMS EKLRIKVDDV KINPKYVLYG VSTPNKRLYK RYSEFWKLKT RLERDVGSTI
     PYDFPEKPGV LDRRWQRRYD DPEMIDERRI GLERFLNELY NDRFDSRWRD TKIAQDFLQL
     SKPNVSQEKS QQHLETADEV GWDEMIRDIK LDLDKESDGT PSVRGALRAR TKLHKLRERL
     EQDVQKKSLP STEVTRRAAL LRSLLKECDD IGTANIAQDR GRLLGVATSD NSSTTEVQGR
     TNNDLQQGQM QMVRDQEQEL VALHRIIQAQ RGLALEMNEE LQTQNELLTA LEDDVDNTGR
     RLQIANKKAR HFNNSA
//