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Entry version 239 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
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Protein

V-type proton ATPase catalytic subunit A

Gene

VMA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar 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. It may participate in maintenance of cytoplasmic Ca2+ homeostasis. This is a catalytic subunit.1 Publication
PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates 'homing', a genetic event that converts a VMA1 allele lacking VDE into one that contains it.1 Publication

Miscellaneous

Present with 199895 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi257 – 264ATPBy similarity8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Endonuclease, Hydrolase, Nuclease, Translocase
Biological processHydrogen ion transport, Intron homing, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29571-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1222556 ROS and RNS production in phagocytes
R-SCE-77387 Insulin receptor recycling
R-SCE-917977 Transferrin endocytosis and recycling
R-SCE-9639288 Amino acids regulate mTORC1

Protein family/group databases

MEROPS protease database

More...
MEROPSi
N09.001

Restriction enzymes and methylases database

More...
REBASEi
2615 PI-SceI

Transport Classification Database

More...
TCDBi
3.A.2.2.3 the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
V-type proton ATPase catalytic subunit A (EC:7.1.2.2)
Short name:
V-ATPase subunit A
Alternative name(s):
Vacuolar proton pump subunit A
Cleaved into the following chain:
Endonuclease PI-SceI (EC:3.1.-.-)
Alternative name(s):
Sce VMA intein
VMA1-derived endonuclease
Short name:
VDE
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:VMA1
Synonyms:CLS8, TFP1
Ordered Locus Names:YDL185W
ORF Names:D1286
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YDL185W

Saccharomyces Genome Database

More...
SGDi
S000002344 VMA1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Vacuole

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi284C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with N-362; S-737 and S-738 in X10SSS VDE. 3 Publications1
Mutagenesisi362H → N: Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSS VDE. 1 Publication1
Mutagenesisi737N → S: Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSS VDE. 2 Publications1
Mutagenesisi738C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with S-284; N-362 and S-737 in X10SSS VDE. 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000024582 – 283V-type proton ATPase catalytic subunit A, 1st partAdd BLAST282
ChainiPRO_0000002459284 – 737Endonuclease PI-SceIAdd BLAST454
ChainiPRO_0000002460738 – 1071V-type proton ATPase catalytic subunit A, 2nd partAdd BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei131PhosphothreonineCombined sources1
Modified residuei858PhosphoserineCombined sources1
Modified residuei928PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Phosphoprotein, Protein splicing

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P17255

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P17255

PRoteomics IDEntifications database

More...
PRIDEi
P17255

2D gel databases

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P17255

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P17255

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).

Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31859, 492 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1192 Vacuolar proton translocating ATPase complex, Golgi variant
CPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant

Database of interacting proteins

More...
DIPi
DIP-2293N

Protein interaction database and analysis system

More...
IntActi
P17255, 103 interactors

Molecular INTeraction database

More...
MINTi
P17255

STRING: functional protein association networks

More...
STRINGi
4932.YDL185W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P17255 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11071
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P17255

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P17255

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini494 – 642DOD-type homing endonucleasePROSITE-ProRule annotationAdd BLAST149

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000141780

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P17255

KEGG Orthology (KO)

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KOi
K02145

Identification of Orthologs from Complete Genome Data

More...
OMAi
HNTVTQH

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1140.10, 1 hit
2.40.30.20, 1 hit
3.10.28.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031686 ATP-synth_a_Xtn
IPR023366 ATP_synth_asu-like_sf
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR003586 Hint_dom_C
IPR003587 Hint_dom_N
IPR036844 Hint_dom_sf
IPR007868 Hom_end_hint
IPR007869 Homing_endonuc_PI-Sce
IPR027434 Homing_endonucl
IPR006142 INTEIN
IPR030934 Intein_C
IPR004042 Intein_endonuc
IPR006141 Intein_N
IPR027417 P-loop_NTPase
IPR022878 V-ATPase_asu

The PANTHER Classification System

More...
PANTHERi
PTHR43607 PTHR43607, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
PF16886 ATP-synt_ab_Xtn, 1 hit
PF05204 Hom_end, 2 hits
PF05203 Hom_end_hint, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00379 INTEIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00305 HintC, 1 hit
SM00306 HintN, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50615 SSF50615, 1 hit
SSF51294 SSF51294, 1 hit
SSF52540 SSF52540, 2 hits
SSF55608 SSF55608, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit
PS50818 INTEIN_C_TER, 1 hit
PS50819 INTEIN_ENDONUCLEASE, 1 hit
PS50817 INTEIN_N_TER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P17255-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGAIENARK EIKRISLEDH AESEYGAIYS VSGPVVIAEN MIGCAMYELV
60 70 80 90 100
KVGHDNLVGE VIRIDGDKAT IQVYEETAGL TVGDPVLRTG KPLSVELGPG
110 120 130 140 150
LMETIYDGIQ RPLKAIKEES QSIYIPRGID TPALDRTIKW QFTPGKFQVG
160 170 180 190 200
DHISGGDIYG SVFENSLISS HKILLPPRSR GTITWIAPAG EYTLDEKILE
210 220 230 240 250
VEFDGKKSDF TLYHTWPVRV PRPVTEKLSA DYPLLTGQRV LDALFPCVQG
260 270 280 290 300
GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCFAKGTN VLMADGSIEC
310 320 330 340 350
IENIEVGNKV MGKDGRPREV IKLPRGRETM YSVVQKSQHR AHKSDSSREV
360 370 380 390 400
PELLKFTCNA THELVVRTPR SVRRLSRTIK GVEYFEVITF EMGQKKAPDG
410 420 430 440 450
RIVELVKEVS KSYPISEGPE RANELVESYR KASNKAYFEW TIEARDLSLL
460 470 480 490 500
GSHVRKATYQ TYAPILYEND HFFDYMQKSK FHLTIEGPKV LAYLLGLWIG
510 520 530 540 550
DGLSDRATFS VDSRDTSLME RVTEYAEKLN LCAEYKDRKE PQVAKTVNLY
560 570 580 590 600
SKVVRGNGIR NNLNTENPLW DAIVGLGFLK DGVKNIPSFL STDNIGTRET
610 620 630 640 650
FLAGLIDSDG YVTDEHGIKA TIKTIHTSVR DGLVSLARSL GLVVSVNAEP
660 670 680 690 700
AKVDMNGTKH KISYAIYMSG GDVLLNVLSK CAGSKKFRPA PAAAFARECR
710 720 730 740 750
GFYFELQELK EDDYYGITLS DDSDHQFLLA NQVVVHNCGE RGNEMAEVLM
760 770 780 790 800
EFPELYTEMS GTKEPIMKRT TLVANTSNMP VAAREASIYT GITLAEYFRD
810 820 830 840 850
QGKNVSMIAD SSSRWAEALR EISGRLGEMP ADQGFPAYLG AKLASFYERA
860 870 880 890 900
GKAVALGSPD RTGSVSIVAA VSPAGGDFSD PVTTATLGIT QVFWGLDKKL
910 920 930 940 950
AQRKHFPSIN TSVSYSKYTN VLNKFYDSNY PEFPVLRDRM KEILSNAEEL
960 970 980 990 1000
EQVVQLVGKS ALSDSDKITL DVATLIKEDF LQQNGYSTYD AFCPIWKTFD
1010 1020 1030 1040 1050
MMRAFISYHD EAQKAVANGA NWSKLADSTG DVKHAVSSSK FFEPSRGEKE
1060 1070
VHGEFEKLLS TMQERFAEST D
Length:1,071
Mass (Da):118,637
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2A4C65D2F59426FD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti875G → D in AAB63978 (PubMed:2905423).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J05409 Genomic DNA Translation: AAA34664.1
X83276 Genomic DNA Translation: CAA58261.1
Z74233 Genomic DNA Translation: CAA98760.1
Z74233 Genomic DNA Translation: CAA98761.1 Sequence problems.
Z74233 Genomic DNA Translation: CAA98762.1
X58857 Genomic DNA Translation: CAA41657.1
M21609 Genomic DNA Translation: AAB63978.1
BK006938 Genomic DNA Translation: DAA11677.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A35746 PXBYVA

NCBI Reference Sequences

More...
RefSeqi
NP_010096.1, NM_001180245.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDL185W_mRNA; YDL185W; YDL185W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851342

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDL185W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Description of Sce VMA in Inbase

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05409 Genomic DNA Translation: AAA34664.1
X83276 Genomic DNA Translation: CAA58261.1
Z74233 Genomic DNA Translation: CAA98760.1
Z74233 Genomic DNA Translation: CAA98761.1 Sequence problems.
Z74233 Genomic DNA Translation: CAA98762.1
X58857 Genomic DNA Translation: CAA41657.1
M21609 Genomic DNA Translation: AAB63978.1
BK006938 Genomic DNA Translation: DAA11677.1
PIRiA35746 PXBYVA
RefSeqiNP_010096.1, NM_001180245.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DFAX-ray2.00A284-737[»]
1EF0X-ray2.10A/B283-741[»]
1GPPX-ray1.35A284-466[»]
A693-736[»]
1JVAX-ray2.10A/B274-747[»]
1LWSX-ray3.50A284-737[»]
1LWTX-ray3.20A284-737[»]
1UM2X-ray2.90A/B284-737[»]
C/D274-747[»]
1VDEX-ray2.40A/B284-737[»]
3J9Telectron microscopy6.90A/C/E2-1071[»]
3J9Uelectron microscopy7.60A/C/E2-1071[»]
3J9Velectron microscopy8.30A/C/E2-1071[»]
5BW9X-ray7.00A/B/C/a/b/c1-1071[»]
5D80X-ray6.20A/B/C/a/b/c1-1071[»]
5VOXelectron microscopy6.80A/C/E1-1071[»]
5VOYelectron microscopy7.90A/C/E1-1071[»]
5VOZelectron microscopy7.60A/C/E1-1071[»]
SMRiP17255
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31859, 492 interactors
ComplexPortaliCPX-1192 Vacuolar proton translocating ATPase complex, Golgi variant
CPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-2293N
IntActiP17255, 103 interactors
MINTiP17255
STRINGi4932.YDL185W

Protein family/group databases

MEROPSiN09.001
REBASEi2615 PI-SceI
TCDBi3.A.2.2.3 the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

PTM databases

iPTMnetiP17255

2D gel databases

UCD-2DPAGEiP17255

Proteomic databases

MaxQBiP17255
PaxDbiP17255
PRIDEiP17255

Genome annotation databases

EnsemblFungiiYDL185W_mRNA; YDL185W; YDL185W
GeneIDi851342
KEGGisce:YDL185W

Organism-specific databases

EuPathDBiFungiDB:YDL185W
SGDiS000002344 VMA1

Phylogenomic databases

HOGENOMiHOG000141780
InParanoidiP17255
KOiK02145
OMAiHNTVTQH

Enzyme and pathway databases

BioCyciYEAST:G3O-29571-MONOMER
ReactomeiR-SCE-1222556 ROS and RNS production in phagocytes
R-SCE-77387 Insulin receptor recycling
R-SCE-917977 Transferrin endocytosis and recycling
R-SCE-9639288 Amino acids regulate mTORC1

Miscellaneous databases

EvolutionaryTraceiP17255

Protein Ontology

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PROi
PR:P17255
RNActiP17255 protein

Family and domain databases

Gene3Di1.10.1140.10, 1 hit
2.40.30.20, 1 hit
3.10.28.10, 2 hits
InterProiView protein in InterPro
IPR031686 ATP-synth_a_Xtn
IPR023366 ATP_synth_asu-like_sf
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR003586 Hint_dom_C
IPR003587 Hint_dom_N
IPR036844 Hint_dom_sf
IPR007868 Hom_end_hint
IPR007869 Homing_endonuc_PI-Sce
IPR027434 Homing_endonucl
IPR006142 INTEIN
IPR030934 Intein_C
IPR004042 Intein_endonuc
IPR006141 Intein_N
IPR027417 P-loop_NTPase
IPR022878 V-ATPase_asu
PANTHERiPTHR43607 PTHR43607, 1 hit
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
PF16886 ATP-synt_ab_Xtn, 1 hit
PF05204 Hom_end, 2 hits
PF05203 Hom_end_hint, 1 hit
PRINTSiPR00379 INTEIN
SMARTiView protein in SMART
SM00305 HintC, 1 hit
SM00306 HintN, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF51294 SSF51294, 1 hit
SSF52540 SSF52540, 2 hits
SSF55608 SSF55608, 2 hits
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit
PS50818 INTEIN_C_TER, 1 hit
PS50819 INTEIN_ENDONUCLEASE, 1 hit
PS50817 INTEIN_N_TER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVATA_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P17255
Secondary accession number(s): D6VRG7, O74301, Q9Y7W5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 239 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  5. Intein-containing proteins
    List of intein-containing protein entries
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