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P37296 (STV1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V-type proton ATPase subunit a, Golgi isoform

Short name=V-ATPase a 2 subunit
Alternative name(s):
Similar to VPH1 protein 1
V-ATPase 101 kDa subunit
V-ATPase subunit AC115
Vacuolar proton translocating ATPase subunit a 2
Gene names
Name:STV1
Ordered Locus Names:YMR054W
ORF Names:YM9796.07
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length890 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in Golgi- and endosome-residing V-ATPase complexes. Enzymes containing this subunit have a 4-fold lower ratio of proton transport to ATP hydrolysis than complexes containing the vacuolar isoform anddo not dissociate V1 and V0 in response to glucose depletion. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Ref.1 Ref.4

Subunit structure

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e).

Subcellular location

Endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein Ref.1 Ref.5.

Post-translational modification

Glycosylated.

Miscellaneous

Present with 1084 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the V-ATPase 116 kDa subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 890890V-type proton ATPase subunit a, Golgi isoform
PRO_0000119225

Regions

Topological domain1 – 450450Cytoplasmic Potential
Transmembrane451 – 46919Helical; Potential
Topological domain470 – 4712Vacuolar Potential
Transmembrane472 – 48817Helical; Potential
Topological domain489 – 50214Cytoplasmic Potential
Transmembrane503 – 53230Helical; Potential
Topological domain533 – 58048Vacuolar Potential
Transmembrane581 – 60020Helical; Potential
Topological domain601 – 61818Cytoplasmic Potential
Transmembrane619 – 63921Helical; Potential
Topological domain640 – 68243Vacuolar Potential
Transmembrane683 – 70220Helical; Potential
Topological domain703 – 77977Cytoplasmic Potential
Transmembrane780 – 80425Helical; Potential
Topological domain805 – 82824Vacuolar Potential
Transmembrane829 – 86739Helical; Potential
Topological domain868 – 89023Cytoplasmic Potential
Coiled coil113 – 15442 Potential
Coiled coil297 – 34751 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue2231Phosphoserine Ref.8 Ref.9 Ref.10
Modified residue2281Phosphoserine Ref.10

Experimental info

Sequence conflict8051Q → E in AAA20596. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37296 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 7CA12E37C1E42C67

FASTA890101,661
        10         20         30         40         50         60 
MNQEEAIFRS ADMTYVQLYI PLEVIREVTF LLGKMSVFMV MDLNKDLTAF QRGYVNQLRR 

        70         80         90        100        110        120 
FDEVERMVGF LNEVVEKHAA ETWKYILHID DEGNDIAQPD MADLINTMEP LSLENVNDMV 

       130        140        150        160        170        180 
KEITDCESRA RQLDESLDSL RSKLNDLLEQ RQVIFECSKF IEVNPGIAGR ATNPEIEQEE 

       190        200        210        220        230        240 
RDVDEFRMTP DDISETLSDA FSFDDETPQD RGALGNDLTR NQSVEDLSFL EQGYQHRYMI 

       250        260        270        280        290        300 
TGSIRRTKVD ILNRILWRLL RGNLIFQNFP IEEPLLEGKE KVEKDCFIIF THGETLLKKV 

       310        320        330        340        350        360 
KRVIDSLNGK IVSLNTRSSE LVDTLNRQID DLQRILDTTE QTLHTELLVI HDQLPVWSAM 

       370        380        390        400        410        420 
TKREKYVYTT LNKFQQESQG LIAEGWVPST ELIHLQDSLK DYIETLGSEY STVFNVILTN 

       430        440        450        460        470        480 
KLPPTYHRTN KFTQAFQSIV DAYGIATYKE INAGLATVVT FPFMFAIMFG DMGHGFILFL 

       490        500        510        520        530        540 
MALFLVLNER KFGAMHRDEI FDMAFTGRYV LLLMGAFSVY TGLLYNDIFS KSMTIFKSGW 

       550        560        570        580        590        600 
QWPSTFRKGE SIEAKKTGVY PFGLDFAWHG TDNGLLFSNS YKMKLSILMG YAHMTYSFMF 

       610        620        630        640        650        660 
SYINYRAKNS KVDIIGNFIP GLVFMQSIFG YLSWAIVYKW SKDWIKDDKP APGLLNMLIN 

       670        680        690        700        710        720 
MFLAPGTIDD QLYSGQAKLQ VVLLLAALVC VPWLLLYKPL TLRRLNKNGG GGRPHGYQSV 

       730        740        750        760        770        780 
GNIEHEEQIA QQRHSAEGFQ GMIISDVASV ADSINESVGG GEQGPFNFGD VMIHQVIHTI 

       790        800        810        820        830        840 
EFCLNCISHT ASYLRLWALS LAHAQLSSVL WDMTISNAFS SKNSGSPLAV MKVVFLFAMW 

       850        860        870        880        890 
FVLTVCILVF MEGTSAMLHA LRLHWVEAMS KFFEGEGYAY EPFSFRAIIE 

« Hide

References

« Hide 'large scale' references
[1]"STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p."
Manolson M.F., Wu B., Proteau D., Taillon B.E., Roberts B.T., Hoyt M.A., Jones E.W.
J. Biol. Chem. 269:14064-14074(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: ATCC 26109 / X2180.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation."
Kawasaki-Nishi S., Nishi T., Forgac M.
J. Biol. Chem. 276:17941-17948(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U06465 Genomic DNA. Translation: AAA20596.1.
Z49703 Genomic DNA. Translation: CAA89764.1.
BK006946 Genomic DNA. Translation: DAA09953.1.
PIRS54554.
RefSeqNP_013770.1. NM_001182552.1.

3D structure databases

ProteinModelPortalP37296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35230. 87 interactions.
DIPDIP-4450N.
IntActP37296. 2 interactions.
MINTMINT-568679.
STRING4932.YMR054W.

Protein family/group databases

TCDB3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

PaxDbP37296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR054W; YMR054W; YMR054W.
GeneID855076.
KEGGsce:YMR054W.

Organism-specific databases

CYGDYMR054w.
SGDS000004658. STV1.

Phylogenomic databases

eggNOGCOG1269.
GeneTreeENSGT00390000004941.
HOGENOMHOG000037059.
KOK02154.
OMAFTIAIMV.
OrthoDBEOG7TJ3S8.

Enzyme and pathway databases

BioCycYEAST:G3O-32759-MONOMER.

Gene expression databases

GenevestigatorP37296.

Family and domain databases

InterProIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERPTHR11629. PTHR11629. 1 hit.
PfamPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFPIRSF001293. ATP6V0A1. 1 hit.
ProtoNetSearch...

Other

NextBio978354.
PROP37296.

Entry information

Entry nameSTV1_YEAST
AccessionPrimary (citable) accession number: P37296
Secondary accession number(s): D6VZM9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families