P32366 (VA0D_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
V-ATPase 39 kDa subunit
V-ATPase subunit M39
Vacuolar proton pump subunit d

Gene names

Name:	VMA6
Ordered Locus Names:	YLR447C
ORF Names:	L9324.8

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The active enzyme consists of a catalytic V1 domain attached to an integral membrane V0 proton pore complex. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores.
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). Ref.1
Subcellular location	Vacuole membrane; Peripheral membrane protein Ref.5.
Miscellaneous	Present with 1630 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the V-ATPase V0D/AC39 subunit family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Membrane Vacuole
PTM	Acetylation
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 vacuolar acidification Traceable author statement PubMed 10224039PubMed 9442887. Source: SGD vacuolar transport Inferred from mutant phenotype Ref.1. Source: SGD
Cellular_component	fungal-type vacuole membrane Inferred from direct assay Ref.1. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD vacuolar proton-transporting V-type ATPase, V0 domain Traceable author statement PubMed 10224039PubMed 9442887. Source: SGD
Molecular_function	proton-transporting ATPase activity, rotational mechanism Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VMA22	P38784	4	EBI-20201,EBI-20329
VMA7	P39111	5	EBI-20201,EBI-20272
VPH1	P32563	4	EBI-20201,EBI-20455

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 345	345	V-type proton ATPase subunit d		PRO_0000119360
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.4
Experimental info
	Sequence conflict	32	1	N → T in AAA35210. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32366 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 53A19450CAF35632	FASTA	345	39,791
	10 20 30 40 50 60 MEGVYFNIDN GFIEGVVRGY RNGLLSNNQY INLTQCDTLE DLKLQLSSTD YGNFLSSVSS 70 80 90 100 110 120 ESLTTSLIQE YASSKLYHEF NYIRDQSSGS TRKFMDYITY GYMIDNVALM ITGTIHDRDK 130 140 150 160 170 180 GEILQRCHPL GWFDTLPTLS VATDLESLYE TVLVDTPLAP YFKNCFDTAE ELDDMNIEII 190 200 210 220 230 240 RNKLYKAYLE DFYNFVTEEI PEPAKECMQT LLGFEADRRS INIALNSLQS SDIDPDLKSD 250 260 270 280 290 300 LLPNIGKLYP LATFHLAQAQ DFEGVRAALA NVYEYRGFLE TGNLEDHFYQ LEMELCRDAF 310 320 330 340 TQQFAISTVW AWMKSKEQEV RNITWIAECI AQNQRERINN YISVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Saccharomyces cerevisiae VMA6 gene encodes the 36-kDa subunit of the vacuolar H(+)-ATPase membrane sector." Bauerle C., Ho M.N., Lindorfer M.A., Stevens T.H. J. Biol. Chem. 268:12749-12757(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 45-61; 188-198; 256-266; 268-276 AND 338-344, SUBUNIT.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [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]	Bienvenut W.V., Peters C. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-18; 76-84; 164-181; 187-276; 298-314 AND 322-335, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1, MASS SPECTROMETRY.
[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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L11584 Genomic DNA. Translation: AAA35210.1. U22382 Genomic DNA. Translation: AAB67533.1. BK006945 Genomic DNA. Translation: DAA09747.1.
PIR	S55969.
RefSeq	NP_013552.3. NM_001182335.3.
3D structure databases
ProteinModelPortal	P32366.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1737N.
IntAct	P32366. 34 interactions.
MINT	MINT-386520.
STRING	4932.YLR447C.
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
PaxDb	P32366.
PeptideAtlas	P32366.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR447C; YLR447C; YLR447C.
GeneID	851168.
KEGG	sce:YLR447C.
Organism-specific databases
CYGD	YLR447c.
SGD	S000004439. VMA6.
Phylogenomic databases
eggNOG	COG1527.
GeneTree	ENSGT00390000002200.
HOGENOM	HOG000199065.
KO	K02146.
OMA	TWIAECI.
OrthoDB	EOG4HX88T.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32502-MONOMER.
Gene expression databases
Genevestigator	P32366.
GermOnline	YLR447C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002843. ATPase_V0-cplx_csu/dsu. IPR016727. ATPase_V0-cplx_dsu. [Graphical view]
PANTHER	PTHR11028. PTHR11028. 1 hit.
Pfam	PF01992. vATP-synt_AC39. 1 hit. [Graphical view]
PIRSF	PIRSF018497. V-ATP_synth_D. 1 hit.
SUPFAM	SSF103486. ATPase_V0/A0_c/d. 1 hit.
ProtoNet	Search...
Other
NextBio	967972.

Entry information

Entry name

VA0D_YEAST

Accession

Primary (citable) accession number: P32366
Secondary accession number(s): D6VZ81

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program