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Protein

V-type proton ATPase subunit B

Gene

vma2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. proton-transporting ATPase activity, rotational mechanism Source: PomBase

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: PomBase
  2. vacuolar acidification Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_188536. Phagosomal maturation (early endosomal stage).
REACT_188545. Transferrin endocytosis and recycling.
REACT_214315. Insulin receptor recycling.

Names & Taxonomyi

Protein namesi
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 namesi
Name:vma2
ORF Names:SPAC637.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC637.05c.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. vacuolar proton-transporting V-type ATPase, V1 domain Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503V-type proton ATPase subunit BPRO_0000144647Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei491 – 4911Phosphoserine1 Publication
Modified residuei492 – 4921Phosphoserine1 Publication
Modified residuei502 – 5021Phosphoserine1 Publication
Modified residuei503 – 5031Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP31411.
PaxDbiP31411.
PRIDEiP31411.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein). Interacts with rav1.1 Publication

Protein-protein interaction databases

BioGridi279830. 5 interactions.
MINTiMINT-4688355.
STRINGi4896.SPAC637.05c-1.

Structurei

3D structure databases

ProteinModelPortaliP31411.
SMRiP31411. Positions 32-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiCOG1156.
HOGENOMiHOG000165320.
InParanoidiP31411.
KOiK02147.
OMAiGRVTGRN.
OrthoDBiEOG7H79BK.
PhylomeDBiP31411.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31411-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASLFDINAA AAVKDYSIKP RLSYNTVNSI TGPLVILDNI RRPQYNEIVN
60 70 80 90 100
LNLPDGSVRS GQVLEVAGHK AIVQVFEGTS GVDVRKTTID FTGHSMRIPV
110 120 130 140 150
SEDMLGRVFN GSGLPIDKGP NLLAEDYLDI NGSPINPYAR IYPEEMIQTG
160 170 180 190 200
ISSIDGLNSI ARGQKIPIFS AAGLPHNEIA AQICRQAGLV KRPTKDVHDG
210 220 230 240 250
HEDNFSIVFA AMGVNLETAR FFQRDFEENG SFERVTLFLN LANDPTIERI
260 270 280 290 300
ITPRLALSAS EFLAYQTEKH VLTILTDMTS YADALREVSA AREEVPGRRG
310 320 330 340 350
YPGYMYTDLS TIYERAGRVE GRNGSITQIP ILTMPNDDIT HPIPDLTGYI
360 370 380 390 400
TEGQIFVDRQ LHNNAIYPPI NVLPSLSRLM KSAIGEGMTR NDHGDVSNQL
410 420 430 440 450
YAMYAIGRDA ASMKSVVGEE ALSQEDRLAL EFLGKFEKTF ISQGAYENRT
460 470 480 490 500
IFETLDLAWS LLRIFPREML TRIPKKILDQ YYSRSSAYTE SSKDVIDNTP

ESS
Length:503
Mass (Da):55,841
Last modified:November 1, 1995 - v2
Checksum:iBC1C15C7E915920F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69638 Genomic DNA. Translation: CAA49339.1.
CU329670 Genomic DNA. Translation: CAA22584.1.
PIRiS25335.
T38997.
RefSeqiNP_594623.1. NM_001020051.2.

Genome annotation databases

EnsemblFungiiSPAC637.05c.1; SPAC637.05c.1:pep; SPAC637.05c.
GeneIDi2543408.
KEGGispo:SPAC637.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69638 Genomic DNA. Translation: CAA49339.1.
CU329670 Genomic DNA. Translation: CAA22584.1.
PIRiS25335.
T38997.
RefSeqiNP_594623.1. NM_001020051.2.

3D structure databases

ProteinModelPortaliP31411.
SMRiP31411. Positions 32-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279830. 5 interactions.
MINTiMINT-4688355.
STRINGi4896.SPAC637.05c-1.

Proteomic databases

MaxQBiP31411.
PaxDbiP31411.
PRIDEiP31411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC637.05c.1; SPAC637.05c.1:pep; SPAC637.05c.
GeneIDi2543408.
KEGGispo:SPAC637.05c.

Organism-specific databases

PomBaseiSPAC637.05c.

Phylogenomic databases

eggNOGiCOG1156.
HOGENOMiHOG000165320.
InParanoidiP31411.
KOiK02147.
OMAiGRVTGRN.
OrthoDBiEOG7H79BK.
PhylomeDBiP31411.

Enzyme and pathway databases

ReactomeiREACT_188536. Phagosomal maturation (early endosomal stage).
REACT_188545. Transferrin endocytosis and recycling.
REACT_214315. Insulin receptor recycling.

Miscellaneous databases

NextBioi20804423.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the genes encoding subunits A and B of the vacuolar H(+)-ATPase of Schizosaccharomyces pombe."
    Ghislain M., Bowman E.J.
    Yeast 8:791-799(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Loss of regulators of vacuolar ATPase function and ceramide synthesis results in multidrug sensitivity in Schizosaccharomyces pombe."
    Dawson K., Toone W.M., Jones N., Wilkinson C.R.
    Eukaryot. Cell 7:926-937(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAV1.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-492; SER-502 AND SER-503, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiVATB_SCHPO
AccessioniPrimary (citable) accession number: P31411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.