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

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P25515 (VATL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 114. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

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

Alternative name(s):
Guanine nucleotide exchange factor 2
V-ATPase 16 kDa proteolipid subunit 1
Vacuolar proton pump c subunit

Gene names

Name:	VMA3
Synonyms:	CLS7, CUP5, GEF2
Ordered Locus Names:	YEL027W

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	160 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. It is an electrogenic proton pump that generates a proton motive force of 180 mv, inside positive and acidic, in the vacuolar membrane vesicles.
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	Vacuole membrane; Multi-pass membrane protein.
Miscellaneous	Present with 8450 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the V-ATPase proteolipid subunit family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Membrane Vacuole
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro cellular copper ion homeostasis Inferred from mutant phenotype. Source: SGD cellular iron ion homeostasis Inferred from mutant phenotype. Source: SGD endocytosis Inferred from mutant phenotype. Source: SGD protein targeting to vacuole Inferred from mutant phenotype. Source: SGD vacuolar acidification Traceable author statement. Source: SGD vacuole organization Inferred from mutant phenotype. 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 ion transmembrane transporter activity 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 – 160

160

V-type proton ATPase subunit c

PRO_0000071762

Regions

Topological domain

1 – 8

Vacuolar Potential

Transmembrane

9 – 31

Helical; Potential

Topological domain

32 – 53

Cytoplasmic Potential

Transmembrane

54 – 74

Helical; Potential

Topological domain

75 – 90

Vacuolar Potential

Transmembrane

91 – 112

Helical; Potential

Topological domain

113 – 124

Cytoplasmic Potential

Transmembrane

125 – 150

Helical; Potential

Topological domain

151 – 160

Vacuolar Potential

Sites

Site

137

Essential for proton translocation

Experimental info

Mutagenesis

137

E → D: Partial inactivation. Ref.5

Mutagenesis

137

E → Q, V or K: Inactivation. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P25515 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: FB8A142FFA1FA964
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FASTA

160

16,351

        10         20         30         40         50         60 
MTELCPVYAP FFGAIGCASA IIFTSLGAAY GTAKSGVGIC ATCVLRPDLL FKNIVPVIMA 

        70         80         90        100        110        120 
GIIAIYGLVV SVLVCYSLGQ KQALYTGFIQ LGAGLSVGLS GLAAGFAIGI VGDAGVRGSS 

       130        140        150        160 
QQPRLFVGMI LILIFAEVLG LYGLIVALLL NSRATQDVVC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The progenitor of ATP synthases was closely related to the current vacuolar H+-ATPase." Nelson H., Nelson N. FEBS Lett. 247:147-153(1989) [PubMed: 2540044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Mutational analysis of yeast vacuolar H(+)-ATPase." Moumi T., Beltran C., Nelson H., Nelson N. Proc. Natl. Acad. Sci. U.S.A. 88:1938-1942(1991) [PubMed: 1825730] [Abstract] Cited for: MUTAGENESIS OF GLU-137.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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	X15155 mRNA. Translation: CAA33249.1. U18530 Genomic DNA. Translation: AAB64504.1. AY558342 Genomic DNA. Translation: AAS56668.1. BK006939 Genomic DNA. Translation: DAA07625.1.
PIR	PXBYL6. S22257.
RefSeq	NP_010887.1. NM_001178842.1.
3D structure databases
ProteinModelPortal	P25515.
SMR	P25515. Positions 8-154.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-8123N.
MINT	MINT-1353979.
STRING	P25515.
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	P25515.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YEL027W; YEL027W; YEL027W.
GeneID	856686.
KEGG	sce:YEL027W.
NMPDR	fig\|4932.3.peg.1941.
Organism-specific databases
CYGD	YEL027w.
SGD	S000000753. VMA3.
Phylogenomic databases
eggNOG	fuNOG09177.
GeneTree	EFGT00050000000644.
HOGENOM	HBG325773.
OMA	CASAIIF.
OrthoDB	EOG4FN7T7.
Gene expression databases
ArrayExpress	P25515.
Genevestigator	P25515.
GermOnline	YEL027W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002379. ATPase_F0/V0-cplx_csu. IPR000245. ATPase_V0-cplx_csu. IPR011555. ATPase_V0-cplx_csu_euk. [Graphical view]
Gene3D	G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.
KO	K02155.
Pfam	PF00137. ATP-synt_C. 2 hits. [Graphical view]
PRINTS	PR00122. VACATPASE.
SUPFAM	SSF81333. ATPase_F0/V0_c. 1 hit.
TIGRFAMs	TIGR01100. V_ATP_synt_C. 1 hit.
ProtoNet	Search...
Other
NextBio	982721.

Entry information

Entry name

VATL1_YEAST

Accession

Primary (citable) accession number: P25515
Secondary accession number(s): D3DLM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	December 14, 2011
This is version 114 of the entry and version 1 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 V

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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

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