P23968 (VATO_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
V-type proton ATPase subunit c''
Short name=V-ATPase subunit c''

Alternative name(s):
V-ATPase 22 kDa proteolipid subunit
Vacuolar proton pump c'' subunit

Gene names

Name:	VMA16
Synonyms:	PPA1
Ordered Locus Names:	YHR026W

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

General annotation (Comments)

Function	Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
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). The proteolipid components c, c' and c'' are present as a hexameric ring that forms the proton-conducting pore.
Subcellular location	Membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the V-ATPase proteolipid subunit family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from direct assay. Source: MGI vacuolar acidification Traceable author statement. Source: SGD
Cellular component	integral to membrane Inferred from direct assay. Source: SGD vacuolar proton-transporting V-type ATPase, V0 domain Traceable author statement. Source: SGD
Molecular function	hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from direct assay. Source: MGI proton-transporting ATPase activity, rotational mechanism Traceable author statement. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 213	213	V-type proton ATPase subunit c''		PRO_0000071780
Regions
	Topological domain	1 – 14	14	Cytoplasmic Potential
	Transmembrane	15 – 35	21	Helical; Potential
	Topological domain	36 – 61	26	Extracellular Potential
	Transmembrane	62 – 82	21	Helical; Potential
	Topological domain	83 – 100	18	Cytoplasmic Potential
	Transmembrane	101 – 121	21	Helical; Potential
	Topological domain	122 – 145	24	Extracellular Potential
	Transmembrane	146 – 167	22	Helical; Potential
	Topological domain	168 – 179	12	Cytoplasmic Potential
	Transmembrane	180 – 205	26	Helical; Potential
	Topological domain	206 – 213	8	Extracellular Potential
Sites
	Site	108	1	Essential for proton translocation
Experimental info
	Mutagenesis	108	1	E → D: Partial inactivation. Ref.5
	Mutagenesis	108	1	E → L, Q or V: Inactivation. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P23968 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 033FF5A516B97F8B	FASTA	213	22,596
	10 20 30 40 50 60 MNKESKDDDM SLGKFSFSHF LYYLVLIVVI VYGLYKLFTG HGSDINFGKF LLRTSPYMWA 70 80 90 100 110 120 NLGIALCVGL SVVGAAWGIF ITGSSMIGAG VRAPRITTKN LISIIFCEVV AIYGLIIAIV 130 140 150 160 170 180 FSSKLTVATA ENMYSKSNLY TGYSLFWAGI TVGASNLICG IAVGITGATA AISDAADSAL 190 200 210 FVKILVIEIF GSILGLLGLI VGLLMAGKAS EFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A yeast protein, homologous to the proteolipid of the chromaffin granule proton-ATPase, is important for cell growth." Apperson M., Jensen R.E., Suda K., Witte C., Yaffe M.P. Biochem. Biophys. Res. Commun. 168:574-579(1990) [PubMed: 2139779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [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]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase." Hirata R., Graham L.A., Takatsuki A., Stevens T.H., Anraku Y. J. Biol. Chem. 272:4795-4803(1997) [PubMed: 9030535] [Abstract] Cited for: MUTAGENESIS OF GLU-108.
[6]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M35294 Genomic DNA. Translation: AAA34892.1. U10399 Genomic DNA. Translation: AAB68881.1. AY692797 Genomic DNA. Translation: AAT92816.1. BK006934 Genomic DNA. Translation: DAA06717.1.
PIR	A34633.
RefSeq	NP_011891.1. NM_001179156.1.
3D structure databases
ProteinModelPortal	P23968.
SMR	P23968. Positions 59-123, 138-206.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4054N.
IntAct	P23968. 2 interactions.
MINT	MINT-539549.
STRING	P23968.
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.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR026W; YHR026W; YHR026W.
GeneID	856421.
KEGG	sce:YHR026W.
NMPDR	fig|4932.3.peg.3037.
Organism-specific databases
CYGD	YHR026w.
SGD	S000001068. VMA16.
Phylogenomic databases
eggNOG	fuNOG06707.
GeneTree	EFGT00050000000644.
HOGENOM	HBG325773.
OMA	VNLFCGI.
OrthoDB	EOG43FM6C.
Gene expression databases
ArrayExpress	P23968.
Genevestigator	P23968.
GermOnline	YHR026W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002379. ATPase_F0/V0-cplx_csu. IPR000245. ATPase_V0-cplx_csu. [Graphical view]
Gene3D	G3DSA:1.20.20.10. ATPase_F0/V0_c. 2 hits.
KO	K03661.
Pfam	PF00137. ATP-synt_C. 2 hits. [Graphical view]
PRINTS	PR00122. VACATPASE.
SUPFAM	SSF81333. ATPase_F0/V0_c. 2 hits.
ProtoNet	Search...
Other
NextBio	981991.

Entry information

Entry name

VATO_YEAST

Accession

Primary (citable) accession number: P23968
Secondary accession number(s): D3DKX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	December 14, 2011
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program