VAM7_YEAST
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 03-AUG-2022, entry version 191.
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; 709.
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; P32912; -.
DR PRIDE; P32912; -.
DR EnsemblFungi; YGL212W_mRNA; YGL212W; YGL212W.
DR GeneID; 852660; -.
DR KEGG; sce:YGL212W; -.
DR SGD; S000003180; VAM7.
DR VEuPathDB; FungiDB:YGL212W; -.
DR eggNOG; KOG3202; Eukaryota.
DR HOGENOM; CLU_033748_1_0_1; -.
DR InParanoid; P32912; -.
DR OMA; NITMMRI; -.
DR BioCyc; YEAST:G3O-30689-MON; -.
DR EvolutionaryTrace; P32912; -.
DR PRO; PR:P32912; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32912; protein.
DR GO; GO:0000421; C:autophagosome membrane; IC: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:0016021; C:integral component of membrane; IBA:GO_Central.
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; IC: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 Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF64268; SSF64268; 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
