V-type proton ATPase subunit a, Golgi isoform - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P37296 (STV1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	890 AA.
Sequence status	Complete.
Protein existence	Evidence 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 and do 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 an 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. Ref.6
Sequence similarities	Belongs to the V-ATPase 116 kDa subunit family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Endosome Golgi apparatus Membrane
Domain	Coiled coil Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro vacuolar acidification Inferred from genetic interaction Ref.4 Ref.1. Source: SGD
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW late endosome Inferred from direct assay. Source: SGD vacuolar proton-transporting V-type ATPase, V0 domain Inferred from direct assay Ref.1. Source: SGD
Molecular function	proton-transporting ATPase activity, rotational mechanism Inferred from genetic interaction Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 890

890

V-type proton ATPase subunit a, Golgi isoform

PRO_0000119225

Regions

Topological domain

1 – 450

450

Cytoplasmic Potential

Transmembrane

451 – 469

Helical; Potential

Topological domain

470 – 471

Vacuolar Potential

Transmembrane

472 – 488

Helical; Potential

Topological domain

489 – 502

Cytoplasmic Potential

Transmembrane

503 – 532

Helical; Potential

Topological domain

533 – 580

Vacuolar Potential

Transmembrane

581 – 600

Helical; Potential

Topological domain

601 – 618

Cytoplasmic Potential

Transmembrane

619 – 639

Helical; Potential

Topological domain

640 – 682

Vacuolar Potential

Transmembrane

683 – 702

Helical; Potential

Topological domain

703 – 779

Cytoplasmic Potential

Transmembrane

780 – 804

Helical; Potential

Topological domain

805 – 828

Vacuolar Potential

Transmembrane

829 – 867

Helical; Potential

Topological domain

868 – 890

Cytoplasmic Potential

Coiled coil

113 – 154

Potential

Coiled coil

297 – 347

Potential

Amino acid modifications

Modified residue

223

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11

Modified residue

228

Phosphoserine Ref.11

Experimental info

Sequence conflict

805

Q → E in AAA20596. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P37296 [UniParc].

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

FASTA

890

101,661

        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' referencesShow '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: 7514599] [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. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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: 11278748] [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: 14562095] [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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"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: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
[9]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, MASS SPECTROMETRY. Strain: ADR376.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, MASS SPECTROMETRY.
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-228, MASS SPECTROMETRY.
+	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.
PIR	S54554.
RefSeq	NP_013770.1. NM_001182552.1.
3D structure databases
ProteinModelPortal	P37296.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4450N.
IntAct	P37296. 1 interaction.
MINT	MINT-568679.
STRING	P37296.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR054W; YMR054W; YMR054W.
GeneID	855076.
KEGG	sce:YMR054W.
NMPDR	fig\|4932.3.peg.4817.
Organism-specific databases
CYGD	YMR054w.
SGD	S000004658. STV1.
Phylogenomic databases
eggNOG	fuNOG07921.
GeneTree	EFGT00050000006837.
HOGENOM	HBG629705.
OMA	FMELTEL.
OrthoDB	EOG4936S5.
Gene expression databases
ArrayExpress	P37296.
Genevestigator	P37296.
GermOnline	YMR054W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002490. ATPase_V0/A0-cplx_116kDa_su. [Graphical view]
KO	K02154.
PANTHER	PTHR11629. ATPase_V0/A0_116. 1 hit.
Pfam	PF01496. V_ATPase_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978354.

Entry information

Entry name

STV1_YEAST

Accession

Primary (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:	January 25, 2012
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents