V-type proton ATPase subunit B - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P16140 (VATB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 129. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
V-type proton ATPase subunit B
Short name=V-ATPase subunit B

Alternative name(s):
V-ATPase 57 kDa subunit
Vacuolar proton pump subunit B

Gene names

Name:	VMA2
Synonyms:	VAT2
Ordered Locus Names:	YBR127C
ORF Names:	YBR1002

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	517 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mv, inside positive and acidic, in the vacuolar membrane vesicles. Ref.8
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). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase. Ref.9
Miscellaneous	Present with 131000 molecules/cell in log phase SD medium. Ref.10
Sequence similarities	Belongs to the ATPase alpha/beta chains family.
Caution	Ref.7 sequence was incorrectly thought to originate from bovine.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro cellular calcium ion homeostasis Inferred from mutant phenotype. Source: SGD vacuolar acidification Inferred from mutant phenotype Ref.8. Source: SGD
Cellular component	fungal-type vacuole membrane Inferred from direct assay. Source: SGD vacuolar proton-transporting V-type ATPase, V1 domain Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.9. Source: IntAct proton-transporting ATPase activity, rotational mechanism Inferred from mutant phenotype Ref.8. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAV1	P47104	4	EBI-20254,EBI-25471

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 517

517

V-type proton ATPase subunit B

PRO_0000144648

Amino acid modifications

Modified residue

Phosphoserine Ref.11 Ref.15

Modified residue

Phosphothreonine Ref.15

Modified residue

Phosphoserine Ref.15

Modified residue

137

Phosphoserine Ref.15

Modified residue

378

Phosphoserine Ref.15

Modified residue

501

Phosphothreonine Ref.14 Ref.15

Modified residue

503

Phosphoserine Ref.13 Ref.14 Ref.15

Modified residue

504

Phosphoserine Ref.14 Ref.15

Modified residue

511

Phosphoserine; by ATM or ATR Ref.12 Ref.14 Ref.15

Modified residue

515

Phosphoserine Ref.12 Ref.14 Ref.15

Experimental info

Sequence conflict

K → V AA sequence Ref.8

Sequence conflict

V → L in AAA66890. Ref.1

Sequence conflict

227

Q → R in AAA30389. Ref.7

Sequence conflict

500 – 517

DTRSS…EESLI → TQEAPVRRRTPAKKNL in AAA66890. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P16140 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 02A7DEC571EFF7C2
Show »

FASTA

517

57,749

        10         20         30         40         50         60 
MVLSDKELFA INKKAVEQGF NVKPRLNYNT VSGVNGPLVI LEKVKFPRYN EIVNLTLPDG 

        70         80         90        100        110        120 
TVRQGQVLEI RGDRAIVQVF EGTSGIDVKK TTVEFTGESL RIPVSEDMLG RIFDGSGRPI 

       130        140        150        160        170        180 
DNGPKVFAED YLDINGSPIN PYARIYPEEM ISTGVSAIDT MNSIARGQKI PIFSASGLPH 

       190        200        210        220        230        240 
NEIAAQICRQ AGLVRPTKDV HDGHEENFSI VFAAMGVNLE TARFFKQDFE ENGSLERTSL 

       250        260        270        280        290        300 
FLNLANDPTI ERIITPRLAL TTAEYLAYQT ERHVLTILTD MSSYADALRE VSAAREEVPG 

       310        320        330        340        350        360 
RRGYPGYMYT DLSTIYERAG RVEGRNGSIT QIPILTMPND DITHPIPDLT GYITEGQIFV 

       370        380        390        400        410        420 
DRQLHNKGIY PPINVLPSLS RLMKSAIGEG MTRKDHGDVS NQLYAKYAIG KDAAAMKAVV 

       430        440        450        460        470        480 
GEEALSIEDK LSLEFLEKFE KTFITQGAYE DRTVFESLDQ AWSLLRIYPK EMLNRISPKI 

       490        500        510 
LDEFYDRARD DADEDEEDPD TRSSGKKKDA SQEESLI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A conserved gene encoding the 57-kDa subunit of the yeast vacuolar H+-ATPase." Nelson H., Mandiyan S., Nelson N. J. Biol. Chem. 264:1775-1778(1989) [PubMed: 2521486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Erratum Nelson H., Mandiyan S., Nelson N. J. Biol. Chem. 264:5313-5313(1989) Cited for: SEQUENCE REVISION.
[3]	"The sequence of 29.7 kb from the right arm of chromosome II reveals 13 complete open reading frames, of which ten correspond to new genes." Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F., Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M., Herbert C.J. Yeast 10:S1-S11(1994) [PubMed: 8091856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[7]	"Differential expression of the 'B' subunit of the vacuolar H(+)-ATPase in bovine tissues." Puopolo K., Kumamoto C., Adachi I., Magner R., Forgac M. J. Biol. Chem. 267:3696-3706(1992) [PubMed: 1371275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-517.
[8]	"Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase." Yamashiro C.T., Kane P.M., Wolczyk D.F., Preston R.A., Stevens T.H. Mol. Cell. Biol. 10:3737-3749(1990) [PubMed: 2141385] [Abstract] Cited for: PROTEIN SEQUENCE OF 13-28, FUNCTION.
[9]	"Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly." Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J. Nat. Cell Biol. 3:384-391(2001) [PubMed: 11283612] [Abstract] Cited for: INTERACTION WITH RAV1 AND RAV2.
[10]	"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].
[11]	"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-4, MASS SPECTROMETRY. Strain: YAL6B.
[12]	"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-511 AND SER-515, MASS SPECTROMETRY. Strain: ADR376.
[13]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, MASS SPECTROMETRY.
[14]	"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 THR-501; SER-503; SER-504; SER-511 AND SER-515, MASS SPECTROMETRY.
[15]	"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-4; THR-83; SER-84; SER-137; SER-378; THR-501; SER-503; SER-504; SER-511 AND SER-515, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04450 Genomic DNA. Translation: AAA66890.1. X75891 Genomic DNA. Translation: CAA53486.1. Z35996 Genomic DNA. Translation: CAA85084.1. AY693158 Genomic DNA. Translation: AAT93177.1. M83130 mRNA. Translation: AAA30389.1. BK006936 Genomic DNA. Translation: DAA07244.1.
PIR	B42254. S45996.
RefSeq	NP_009685.1. NM_001178475.1.
3D structure databases
ProteinModelPortal	P16140.
SMR	P16140. Positions 19-516.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2292N.
IntAct	P16140. 514 interactions.
MINT	MINT-563511.
STRING	P16140.
Protein family/group databases
TCDB	3.A.2.2.3. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.
Proteomic databases
PeptideAtlas	P16140.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR127C; YBR127C; YBR127C.
GeneID	852424.
KEGG	sce:YBR127C.
NMPDR	fig\|4932.3.peg.389.
Organism-specific databases
CYGD	YBR127c.
SGD	S000000331. VMA2.
Phylogenomic databases
eggNOG	fuNOG05941.
GeneTree	EFGT00050000004047.
HOGENOM	HBG565875.
OMA	VVFINLA.
OrthoDB	EOG4QVGM6.
Gene expression databases
ArrayExpress	P16140.
Genevestigator	P16140.
GermOnline	YBR127C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR020003. ATPase_a/bsu_AS. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR005723. ATPase_V1-cplx_bsu. IPR022879. V-ATPase_su_B/beta. [Graphical view]
KO	K02147.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01040. V-ATPase_V1_B. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971294.

Entry information

Entry name

VATB_YEAST

Accession

Primary (citable) accession number: P16140
Secondary accession number(s): D6VQC4, P32123

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 129 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 II

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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic 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