P31411 (VATB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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
ORF Names:	SPAC637.05c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	503 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.
Subunit structure	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. Ref.3
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from sequence orthology. Source: PomBase vacuolar acidification Inferred from sequence orthology. Source: PomBase
Cellular_component	vacuolar proton-transporting V-type ATPase, V1 domain Inferred from sequence orthology. Source: PomBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from sequence orthology. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 503	503	V-type proton ATPase subunit B		PRO_0000144647
Amino acid modifications
	Modified residue	491	1	Phosphoserine Ref.4
	Modified residue	492	1	Phosphoserine Ref.4
	Modified residue	502	1	Phosphoserine Ref.4
	Modified residue	503	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P31411 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: BC1C15C7E915920F	FASTA	503	55,841
	10 20 30 40 50 60 MASLFDINAA AAVKDYSIKP RLSYNTVNSI TGPLVILDNI RRPQYNEIVN LNLPDGSVRS 70 80 90 100 110 120 GQVLEVAGHK AIVQVFEGTS GVDVRKTTID FTGHSMRIPV SEDMLGRVFN GSGLPIDKGP 130 140 150 160 170 180 NLLAEDYLDI NGSPINPYAR IYPEEMIQTG ISSIDGLNSI ARGQKIPIFS AAGLPHNEIA 190 200 210 220 230 240 AQICRQAGLV KRPTKDVHDG HEDNFSIVFA AMGVNLETAR FFQRDFEENG SFERVTLFLN 250 260 270 280 290 300 LANDPTIERI ITPRLALSAS EFLAYQTEKH VLTILTDMTS YADALREVSA AREEVPGRRG 310 320 330 340 350 360 YPGYMYTDLS TIYERAGRVE GRNGSITQIP ILTMPNDDIT HPIPDLTGYI TEGQIFVDRQ 370 380 390 400 410 420 LHNNAIYPPI NVLPSLSRLM KSAIGEGMTR NDHGDVSNQL YAMYAIGRDA ASMKSVVGEE 430 440 450 460 470 480 ALSQEDRLAL EFLGKFEKTF ISQGAYENRT IFETLDLAWS LLRIFPREML TRIPKKILDQ 490 500 YYSRSSAYTE SSKDVIDNTP ESS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-492; SER-502 AND SER-503, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X69638 Genomic DNA. Translation: CAA49339.1. CU329670 Genomic DNA. Translation: CAA22584.1.
PIR	S25335. T38997.
RefSeq	NP_594623.1. NM_001020051.2.
3D structure databases
ProteinModelPortal	P31411.
SMR	P31411. Positions 32-484.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC637.05c-1.
Proteomic databases
PaxDb	P31411.
PRIDE	P31411.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC637.05c.1; SPAC637.05c.1:pep; SPAC637.05c.
GeneID	2543408.
KEGG	spo:SPAC637.05c.
Organism-specific databases
PomBase	SPAC637.05c.
Phylogenomic databases
eggNOG	COG1156.
HOGENOM	HOG000165320.
KO	K02147.
OMA	LMKEGIG.
OrthoDB	EOG4QVGM6.
Family and domain databases
InterPro	IPR020003. ATPase_a/bsu_AS. IPR004100. ATPase_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR005723. ATPase_V1-cplx_bsu. IPR022879. V-ATPase_su_B/beta. [Graphical view]
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	20804423.

Entry information

Entry name

VATB_SCHPO

Accession

Primary (citable) accession number: P31411

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program