Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

V-type proton ATPase catalytic subunit A

Gene

ATP6V1A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi250 – 2578ATPBy similarity

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-BTA-1222556. ROS, RNS production in response to bacteria.
R-BTA-77387. Insulin receptor recycling.
R-BTA-917977. Transferrin endocytosis and recycling.
R-BTA-983712. Ion channel transport.

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 proton pump subunit alpha
Gene namesi
Name:ATP6V1A
Synonyms:ATP6A1, ATP6V1A1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617V-type proton ATPase catalytic subunit APRO_0000144559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361PhosphothreonineBy similarity
Modified residuei384 – 3841PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP31404.
PeptideAtlasiP31404.
PRIDEiP31404.

Expressioni

Gene expression databases

BgeeiENSBTAG00000002703.

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

STRINGi9913.ENSBTAP00000050728.

Structurei

3D structure databases

ProteinModelPortaliP31404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiKOG1352. Eukaryota.
COG1155. LUCA.
GeneTreeiENSGT00550000074787.
HOGENOMiHOG000161057.
HOVERGENiHBG053351.
InParanoidiP31404.
KOiK02145.
OMAiYSPYDRF.
OrthoDBiEOG091G03SR.
TreeFamiTF300811.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00309. ATP_synth_A_arch. 1 hit.
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.

P31404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFSKLPKIR DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL
60 70 80 90 100
VGEIIRLEGD MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD
110 120 130 140 150
GIQRPLSDIS SQTQSIYIPR GVNVSALSRD VKWDFTPCKN LRVGSHITGG
160 170 180 190 200
DIYGIVNENS LIKHKIMLPP RNRGTVTYIA PPGNYDTSDV VLELEFEGIK
210 220 230 240 250
EKFSMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC VQGGTTAIPG
260 270 280 290 300
AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG
310 320 330 340 350
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS
360 370 380 390 400
TSRWAEALRE ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER
410 420 430 440 450
EGSVSIVGAV SPPGGDFSDP VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW
460 470 480 490 500
LISYSKYMRA LDEYYDKHFT EFVPLRTKAK EILQEEEDLA EIVQLVGKAS
510 520 530 540 550
LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM LSNMIAFYDM
560 570 580 590 600
ARRAVETTAQ SDNKITWSII REHMGEILYK LSSMKFKDPV KDGEAKIKAD
610
YAQLLEDMQN AFRSLED
Length:617
Mass (Da):68,344
Last modified:May 30, 2006 - v2
Checksum:iEF27E9DB67B6CB9C
GO

Sequence cautioni

The sequence AAI05146 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA41276 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911G → C in AAA30392 (PubMed:1722207).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80430 mRNA. Translation: AAA30392.1.
X58386 mRNA. Translation: CAA41276.1. Different initiation.
BC105145 mRNA. Translation: AAI05146.1. Different initiation.
PIRiS19659.
RefSeqiNP_776929.1. NM_174504.2.
XP_015326478.1. XM_015470992.1.
UniGeneiBt.66154.

Genome annotation databases

EnsembliENSBTAT00000055158; ENSBTAP00000050728; ENSBTAG00000002703.
GeneIDi282147.
KEGGibta:282147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80430 mRNA. Translation: AAA30392.1.
X58386 mRNA. Translation: CAA41276.1. Different initiation.
BC105145 mRNA. Translation: AAI05146.1. Different initiation.
PIRiS19659.
RefSeqiNP_776929.1. NM_174504.2.
XP_015326478.1. XM_015470992.1.
UniGeneiBt.66154.

3D structure databases

ProteinModelPortaliP31404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000050728.

Proteomic databases

PaxDbiP31404.
PeptideAtlasiP31404.
PRIDEiP31404.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000055158; ENSBTAP00000050728; ENSBTAG00000002703.
GeneIDi282147.
KEGGibta:282147.

Organism-specific databases

CTDi523.

Phylogenomic databases

eggNOGiKOG1352. Eukaryota.
COG1155. LUCA.
GeneTreeiENSGT00550000074787.
HOGENOMiHOG000161057.
HOVERGENiHBG053351.
InParanoidiP31404.
KOiK02145.
OMAiYSPYDRF.
OrthoDBiEOG091G03SR.
TreeFamiTF300811.

Enzyme and pathway databases

ReactomeiR-BTA-1222556. ROS, RNS production in response to bacteria.
R-BTA-77387. Insulin receptor recycling.
R-BTA-917977. Transferrin endocytosis and recycling.
R-BTA-983712. Ion channel transport.

Gene expression databases

BgeeiENSBTAG00000002703.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00309. ATP_synth_A_arch. 1 hit.
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...

Entry informationi

Entry nameiVATA_BOVIN
AccessioniPrimary (citable) accession number: P31404
Secondary accession number(s): Q3MHQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 30, 2006
Last modified: September 7, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.