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Protein

V-type proton ATPase catalytic subunit A

Gene

vha-13

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.Curated

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi240 – 2478ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-CEL-1222556. ROS, RNS production in response to bacteria.
R-CEL-77387. Insulin receptor recycling.
R-CEL-917977. Transferrin endocytosis and recycling.

Protein family/group databases

TCDBi3.A.2.2.7. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase catalytic subunit A (EC:3.6.3.14)
Short name:
V-ATPase subunit A
Alternative name(s):
V-ATPase 69 kDa subunit
Vacuolar H ATPase protein 13
Vacuolar proton pump subunit alpha
Gene namesi
Name:vha-13Imported
ORF Names:Y49A3A.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiY49A3A.2; CE22210; WBGene00013025; vha-13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 606605V-type proton ATPase catalytic subunit APRO_0000232903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9XW92.
PaxDbiQ9XW92.
PRIDEiQ9XW92.

2D gel databases

World-2DPAGE0020:Q9XW92.

PTM databases

iPTMnetiQ9XW92.

Interactioni

Subunit structurei

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).

Protein-protein interaction databases

STRINGi6239.Y49A3A.2.4.

Structurei

3D structure databases

ProteinModelPortaliQ9XW92.
SMRiQ9XW92. Positions 7-606.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Sequence analysis

Phylogenomic databases

eggNOGiKOG1352. Eukaryota.
COG1155. LUCA.
GeneTreeiENSGT00550000074787.
HOGENOMiHOG000161057.
InParanoidiQ9XW92.
KOiK02145.
OMAiEGYPPYL.
PhylomeDBiQ9XW92.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00309. ATP_synth_A_arch.
InterProiIPR031686. ATP-synt_a_Xtn.
IPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR005725. ATPase_V1-cplx_asu.
IPR027417. P-loop_NTPase.
IPR022878. V-ATPase_asu.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
PF16886. ATP-synt_ab_Xtn. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01042. V-ATPase_V1_A. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9XW92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAESSYGFV YGVSGPVVTA EKMAGSAMYE LVRVGHQELV GEIIRLEGDY
60 70 80 90 100
ATIQVYEETS GVTIGDPVLR TGKPLSVELG PGIMGSIFDG IQRPLKDIAD
110 120 130 140 150
ITQSIYIPKG VSTNALSREA RWDFVVSKDL RVGGHVTGGD IIGTVDENLL
160 170 180 190 200
IKHKILLPPS ACGTITFVAP SGQYTVEDTL LELEFAGRKQ KFSMLQIWPV
210 220 230 240 250
RSPRPVTEKL AANNPLLCGQ RVLDALFPCV QGGTTAIPGA FGCGKTVISQ
260 270 280 290 300
SLSKYSNSDA IIYVGCGERG NEMSEVLRDF PELTMEVEGV TTSIMKRTAL
310 320 330 340 350
VANTSNMPVA AREASIYTGI TLAEYFRDMG LNVAMMADST SRWAEALREI
360 370 380 390 400
SGRLGEMPAD SGYPAYLAAR LASFYERAGR VKCLGSPERE GSVTIVGAVS
410 420 430 440 450
PPGGDFADPV TSATLGIVQV FWGLDKKLAQ RKHFPSINWL ISYSEYMRAL
460 470 480 490 500
EEFYEKNYPE FVSLRTKCKE ILQEEEDLSE IVQLVGKASL AESDKVTLEV
510 520 530 540 550
AKIIKDDFLQ QNGYTKYDRF CPFYKTVGML KNMIGFYDLA RHAVEATAQS
560 570 580 590 600
DNKITWNVIK DSMGDLIYQL SAMKFKDPVA DGEAKIRKDY EDLAEAMANA

FRNLED
Length:606
Mass (Da):66,460
Last modified:January 23, 2007 - v3
Checksum:iD1A73ECC57B85892
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL033512 Genomic DNA. Translation: CAA22076.1.
PIRiT27035.
RefSeqiNP_506559.1. NM_074158.4.
UniGeneiCel.38650.

Genome annotation databases

EnsemblMetazoaiY49A3A.2.1; Y49A3A.2.1; WBGene00013025.
Y49A3A.2.2; Y49A3A.2.2; WBGene00013025.
Y49A3A.2.3; Y49A3A.2.3; WBGene00013025.
Y49A3A.2.4; Y49A3A.2.4; WBGene00013025.
GeneIDi3564970.
KEGGicel:CELE_Y49A3A.2.
UCSCiY49A3A.2.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL033512 Genomic DNA. Translation: CAA22076.1.
PIRiT27035.
RefSeqiNP_506559.1. NM_074158.4.
UniGeneiCel.38650.

3D structure databases

ProteinModelPortaliQ9XW92.
SMRiQ9XW92. Positions 7-606.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.Y49A3A.2.4.

Protein family/group databases

TCDBi3.A.2.2.7. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

iPTMnetiQ9XW92.

2D gel databases

World-2DPAGE0020:Q9XW92.

Proteomic databases

EPDiQ9XW92.
PaxDbiQ9XW92.
PRIDEiQ9XW92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY49A3A.2.1; Y49A3A.2.1; WBGene00013025.
Y49A3A.2.2; Y49A3A.2.2; WBGene00013025.
Y49A3A.2.3; Y49A3A.2.3; WBGene00013025.
Y49A3A.2.4; Y49A3A.2.4; WBGene00013025.
GeneIDi3564970.
KEGGicel:CELE_Y49A3A.2.
UCSCiY49A3A.2.2. c. elegans.

Organism-specific databases

CTDi3564970.
WormBaseiY49A3A.2; CE22210; WBGene00013025; vha-13.

Phylogenomic databases

eggNOGiKOG1352. Eukaryota.
COG1155. LUCA.
GeneTreeiENSGT00550000074787.
HOGENOMiHOG000161057.
InParanoidiQ9XW92.
KOiK02145.
OMAiEGYPPYL.
PhylomeDBiQ9XW92.

Enzyme and pathway databases

ReactomeiR-CEL-1222556. ROS, RNS production in response to bacteria.
R-CEL-77387. Insulin receptor recycling.
R-CEL-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

PROiQ9XW92.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00309. ATP_synth_A_arch.
InterProiIPR031686. ATP-synt_a_Xtn.
IPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR005725. ATPase_V1-cplx_asu.
IPR027417. P-loop_NTPase.
IPR022878. V-ATPase_asu.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
PF16886. ATP-synt_ab_Xtn. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01042. V-ATPase_V1_A. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2Imported.
  2. Bienvenut W.V.
    Submitted (APR-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-33; 97-118; 122-128; 132-152; 192-201; 246-254; 371-377; 449-465; 503-516; 532-541 AND 554-574, ACETYLATION AT ALA-2.

Entry informationi

Entry nameiVATA_CAEEL
AccessioniPrimary (citable) accession number: Q9XW92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.