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Protein

Vacuolar morphogenesis protein 7

Gene

VAM7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for proper morphogenesis of the vacuole. May exist as structural reinforcement on the surface of the vacuolar membrane and be required for maintenance against rupture by osmotic pressure.

GO - Molecular functioni

  1. phosphatidylinositol-3-phosphate binding Source: SGD
  2. SNAP receptor activity Source: SGD

GO - Biological processi

  1. piecemeal microautophagy of nucleus Source: SGD
  2. vacuole fusion, non-autophagic Source: SGD
  3. vesicle fusion Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-30689-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar morphogenesis protein 7
Gene namesi
Name:VAM7
Ordered Locus Names:YGL212W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL212w.
EuPathDBiFungiDB:YGL212W.
SGDiS000003180. VAM7.

Subcellular locationi

GO - Cellular componenti

  1. fungal-type vacuole membrane Source: SGD
  2. SNARE complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Vacuolar morphogenesis protein 7PRO_0000065760Add
BLAST

Proteomic databases

MaxQBiP32912.
PaxDbiP32912.

Expressioni

Gene expression databases

GenevestigatoriP32912.

Interactioni

Subunit structurei

Possibly multimeric. Associates with VAM3.

Binary interactionsi

WithEntry#Exp.IntActNotes
RBD2Q122703EBI-20232,EBI-31471
VAM3Q122415EBI-20232,EBI-20227
YIF1P538453EBI-20232,EBI-28230

Protein-protein interaction databases

BioGridi33044. 258 interactions.
DIPiDIP-1722N.
IntActiP32912. 36 interactions.
MINTiMINT-384943.
STRINGi4932.YGL212W.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 227Combined sources
Beta strandi27 – 326Combined sources
Beta strandi38 – 403Combined sources
Helixi42 – 5615Combined sources
Helixi82 – 898Combined sources
Helixi92 – 1009Combined sources
Helixi107 – 1104Combined sources
Helixi112 – 1176Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KMDNMR-A8-124[»]
ProteinModelPortaliP32912.
SMRiP32912. Positions 8-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 124124PXPROSITE-ProRule annotationAdd
BLAST
Domaini250 – 31263t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili168 – 18619Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG259218.
InParanoidiP32912.
KOiK08502.
OMAiKLPLRSY.
OrthoDBiEOG7DRJF0.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANSVGKMS EKLRIKVDDV KINPKYVLYG VSTPNKRLYK RYSEFWKLKT
60 70 80 90 100
RLERDVGSTI PYDFPEKPGV LDRRWQRRYD DPEMIDERRI GLERFLNELY
110 120 130 140 150
NDRFDSRWRD TKIAQDFLQL SKPNVSQEKS QQHLETADEV GWDEMIRDIK
160 170 180 190 200
LDLDKESDGT PSVRGALRAR TKLHKLRERL EQDVQKKSLP STEVTRRAAL
210 220 230 240 250
LRSLLKECDD IGTANIAQDR GRLLGVATSD NSSTTEVQGR TNNDLQQGQM
260 270 280 290 300
QMVRDQEQEL VALHRIIQAQ RGLALEMNEE LQTQNELLTA LEDDVDNTGR
310
RLQIANKKAR HFNNSA
Length:316
Mass (Da):36,711
Last modified:October 1, 1993 - v1
Checksum:i2F992AEC0ACBC8FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11379 Genomic DNA. Translation: BAA01977.1.
U33754 Genomic DNA. Translation: AAC49494.1.
Z72734 Genomic DNA. Translation: CAA96928.1.
BK006941 Genomic DNA. Translation: DAA07904.1.
PIRiS31263.
RefSeqiNP_011303.1. NM_001181077.1.

Genome annotation databases

EnsemblFungiiYGL212W; YGL212W; YGL212W.
GeneIDi852660.
KEGGisce:YGL212W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11379 Genomic DNA. Translation: BAA01977.1.
U33754 Genomic DNA. Translation: AAC49494.1.
Z72734 Genomic DNA. Translation: CAA96928.1.
BK006941 Genomic DNA. Translation: DAA07904.1.
PIRiS31263.
RefSeqiNP_011303.1. NM_001181077.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KMDNMR-A8-124[»]
ProteinModelPortaliP32912.
SMRiP32912. Positions 8-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33044. 258 interactions.
DIPiDIP-1722N.
IntActiP32912. 36 interactions.
MINTiMINT-384943.
STRINGi4932.YGL212W.

Proteomic databases

MaxQBiP32912.
PaxDbiP32912.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL212W; YGL212W; YGL212W.
GeneIDi852660.
KEGGisce:YGL212W.

Organism-specific databases

CYGDiYGL212w.
EuPathDBiFungiDB:YGL212W.
SGDiS000003180. VAM7.

Phylogenomic databases

eggNOGiNOG259218.
InParanoidiP32912.
KOiK08502.
OMAiKLPLRSY.
OrthoDBiEOG7DRJF0.

Enzyme and pathway databases

BioCyciYEAST:G3O-30689-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32912.
NextBioi971942.
PROiP32912.

Gene expression databases

GenevestigatoriP32912.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. II. VAM7, a gene for regulating morphogenic assembly of the vacuoles."
    Wada Y., Anraku Y.
    J. Biol. Chem. 267:18671-18675(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: YWH019-7A.
  2. "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII reveals 11 open reading frames: two correspond to new genes."
    Feuermann M., Simeonava L., Souciet J.-L., Potier S.
    Yeast 13:475-477(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and containing three novel transcribed open reading frames."
    Kail M., Juettner E., Vaux D.
    Yeast 12:799-807(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking."
    Sato T.K., Darsow T., Emr S.D.
    Mol. Cell. Biol. 18:5308-5319(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVAM7_YEAST
AccessioniPrimary (citable) accession number: P32912
Secondary accession number(s): D6VTU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 29, 2015
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2360 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.