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 116 kDa subunit a isoform 2

Gene

ATP6V0A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the proton channel of V-ATPases. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:G66-33375-MONOMER.
ZFISH:G66-33375-MONOMER.
BRENDAi3.6.3.6. 2681.
ReactomeiR-HSA-1222556. ROS, RNS production in response to bacteria.
R-HSA-77387. Insulin receptor recycling.
R-HSA-917977. Transferrin endocytosis and recycling.
R-HSA-983712. Ion channel transport.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase 116 kDa subunit a isoform 2
Short name:
V-ATPase 116 kDa isoform a2
Alternative name(s):
Lysosomal H(+)-transporting ATPase V0 subunit a2
TJ6
Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18481. ATP6V0A2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 393CytoplasmicSequence analysisAdd BLAST393
Transmembranei394 – 412HelicalSequence analysisAdd BLAST19
Topological domaini413 – 414VacuolarSequence analysis2
Transmembranei415 – 431HelicalSequence analysisAdd BLAST17
Topological domaini432 – 445CytoplasmicSequence analysisAdd BLAST14
Transmembranei446 – 475HelicalSequence analysisAdd BLAST30
Topological domaini476 – 549VacuolarSequence analysisAdd BLAST74
Transmembranei550 – 569HelicalSequence analysisAdd BLAST20
Topological domaini570 – 587CytoplasmicSequence analysisAdd BLAST18
Transmembranei588 – 608HelicalSequence analysisAdd BLAST21
Topological domaini609 – 651VacuolarSequence analysisAdd BLAST43
Transmembranei652 – 671HelicalSequence analysisAdd BLAST20
Topological domaini672 – 739CytoplasmicSequence analysisAdd BLAST68
Transmembranei740 – 764HelicalSequence analysisAdd BLAST25
Topological domaini765 – 785VacuolarSequence analysisAdd BLAST21
Transmembranei786 – 824HelicalSequence analysisAdd BLAST39
Topological domaini825 – 856CytoplasmicSequence analysisAdd BLAST32

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Cutis laxa, autosomal recessive, 2A (ARCL2A)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by an excessive congenital skin wrinkling, a large fontanelle with delayed closure, a typical facial appearance with downslanting palpebral fissures, a general connective tissue weakness, and varying degrees of growth and developmental delay and neurological abnormalities. Some affected individuals develop seizures and mental deterioration later in life, whereas the skin phenotype tends to become milder with age. At the molecular level, an abnormal glycosylation of serum proteins is observed in many cases.
See also OMIM:219200
Wrinkly skin syndrome (WSS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal recessive disorder characterized by wrinkling of the skin of the dorsum of the hands and feet, an increased number of palmar and plantar creases, wrinkled abdominal skin, multiple musculoskeletal abnormalities, microcephaly, growth failure and developmental delay.
See also OMIM:278250

Organism-specific databases

DisGeNETi23545.
MalaCardsiATP6V0A2.
MIMi219200. phenotype.
278250. phenotype.
OpenTargetsiENSG00000185344.
Orphaneti357074. Autosomal recessive cutis laxa type 2, classic type.
2834. Wrinkly skin syndrome.
PharmGKBiPA38549.

Polymorphism and mutation databases

BioMutaiATP6V0A2.
DMDMi172046607.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001192161 – 856V-type proton ATPase 116 kDa subunit a isoform 2Add BLAST856

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi484N-linked (GlcNAc...)Sequence analysis1
Glycosylationi505N-linked (GlcNAc...)Sequence analysis1
Modified residuei695PhosphoserineCombined sources1
Modified residuei700PhosphoserineBy similarity1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9Y487.
MaxQBiQ9Y487.
PaxDbiQ9Y487.
PeptideAtlasiQ9Y487.
PRIDEiQ9Y487.

PTM databases

iPTMnetiQ9Y487.
PhosphoSitePlusiQ9Y487.
SwissPalmiQ9Y487.

Expressioni

Gene expression databases

BgeeiENSG00000185344.
CleanExiHS_ATP6V0A2.
ExpressionAtlasiQ9Y487. baseline and differential.
GenevisibleiQ9Y487. HS.

Organism-specific databases

HPAiHPA044279.

Interactioni

Subunit structurei

The V-ATPase is a heteromultimeric enzyme composed of at least thirteen different subunits. It has a membrane peripheral V1 sector for ATP hydrolysis and an integral V0 for proton translocation. The V1 sector comprises subunits A-H, whereas V0 includes subunits a, d, c, c', and c''. Directly interacts with PSCD2 through its N-terminal cytosolic tail in an intra-endosomal acidification-dependent manner. Disruption of this interaction results in the inhibition of endocytosis.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CYTH2Q994182EBI-988630,EBI-448974

GO - Molecular functioni

Protein-protein interaction databases

BioGridi117089. 55 interactors.
IntActiQ9Y487. 5 interactors.
STRINGi9606.ENSP00000332247.

Structurei

3D structure databases

ProteinModelPortaliQ9Y487.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase 116 kDa subunit family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2189. Eukaryota.
COG1269. LUCA.
GeneTreeiENSGT00390000004941.
HOGENOMiHOG000037059.
HOVERGENiHBG014606.
InParanoidiQ9Y487.
KOiK02154.
OMAiHPPAEHK.
OrthoDBiEOG091G01BI.
PhylomeDBiQ9Y487.
TreeFamiTF300346.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSLFRSETM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK
60 70 80 90 100
FVGEVKRCEE LERILVYLVQ EINRADIPLP EGEASPPAPP LKQVLEMQEQ
110 120 130 140 150
LQKLEVELRE VTKNKEKLRK NLLELIEYTH MLRVTKTFVK RNVEFEPTYE
160 170 180 190 200
EFPSLESDSL LDYSCMQRLG AKLGFVSGLI NQGKVEAFEK MLWRVCKGYT
210 220 230 240 250
IVSYAELDES LEDPETGEVI KWYVFLISFW GEQIGHKVKK ICDCYHCHVY
260 270 280 290 300
PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVYSRVI
310 320 330 340 350
QVKKMKAIYH MLNMCSFDVT NKCLIAEVWC PEADLQDLRR ALEEGSRESG
360 370 380 390 400
ATIPSFMNII PTKETPPTRI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT
410 420 430 440 450
IITFPFLFAV MFGDFGHGFV MFLFALLLVL NENHPRLNQS QEIMRMFFNG
460 470 480 490 500
RYILLLMGLF SVYTGLIYND CFSKSVNLFG SGWNVSAMYS SSHPPAEHKK
510 520 530 540 550
MVLWNDSVVR HNSILQLDPS IPGVFRGPYP LGIDPIWNLA TNRLTFLNSF
560 570 580 590 600
KMKMSVILGI IHMTFGVILG IFNHLHFRKK FNIYLVSIPE LLFMLCIFGY
610 620 630 640 650
LIFMIFYKWL VFSAETSRVA PSILIEFINM FLFPASKTSG LYTGQEYVQR
660 670 680 690 700
VLLVVTALSV PVLFLGKPLF LLWLHNGRSC FGVNRSGYTL IRKDSEEEVS
710 720 730 740 750
LLGSQDIEEG NHQVEDGCRE MACEEFNFGE ILMTQVIHSI EYCLGCISNT
760 770 780 790 800
ASYLRLWALS LAHAQLSDVL WAMLMRVGLR VDTTYGVLLL LPVIALFAVL
810 820 830 840 850
TIFILLIMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF SFSLLSSKFN

NDDSVA
Length:856
Mass (Da):98,082
Last modified:March 18, 2008 - v2
Checksum:i6C38B36FA33A92BA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti428L → W in AAD04632 (Ref. 1) Curated1
Sequence conflicti669L → P in BAF82080 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042730685R → Q.Corresponds to variant rs7969410dbSNPEnsembl.1
Natural variantiVAR_042731813A → V.Corresponds to variant rs17883456dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112972 mRNA. Translation: AAD04632.1.
AK289391 mRNA. Translation: BAF82080.1.
CH471054 Genomic DNA. Translation: EAW98434.1.
BC068531 mRNA. Translation: AAH68531.1.
CCDSiCCDS9254.1.
RefSeqiNP_036595.2. NM_012463.3.
UniGeneiHs.25786.

Genome annotation databases

EnsembliENST00000330342; ENSP00000332247; ENSG00000185344.
GeneIDi23545.
KEGGihsa:23545.
UCSCiuc001ufr.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112972 mRNA. Translation: AAD04632.1.
AK289391 mRNA. Translation: BAF82080.1.
CH471054 Genomic DNA. Translation: EAW98434.1.
BC068531 mRNA. Translation: AAH68531.1.
CCDSiCCDS9254.1.
RefSeqiNP_036595.2. NM_012463.3.
UniGeneiHs.25786.

3D structure databases

ProteinModelPortaliQ9Y487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117089. 55 interactors.
IntActiQ9Y487. 5 interactors.
STRINGi9606.ENSP00000332247.

PTM databases

iPTMnetiQ9Y487.
PhosphoSitePlusiQ9Y487.
SwissPalmiQ9Y487.

Polymorphism and mutation databases

BioMutaiATP6V0A2.
DMDMi172046607.

Proteomic databases

EPDiQ9Y487.
MaxQBiQ9Y487.
PaxDbiQ9Y487.
PeptideAtlasiQ9Y487.
PRIDEiQ9Y487.

Protocols and materials databases

DNASUi23545.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330342; ENSP00000332247; ENSG00000185344.
GeneIDi23545.
KEGGihsa:23545.
UCSCiuc001ufr.4. human.

Organism-specific databases

CTDi23545.
DisGeNETi23545.
GeneCardsiATP6V0A2.
GeneReviewsiATP6V0A2.
H-InvDBHIX0011113.
HGNCiHGNC:18481. ATP6V0A2.
HPAiHPA044279.
MalaCardsiATP6V0A2.
MIMi219200. phenotype.
278250. phenotype.
611716. gene.
neXtProtiNX_Q9Y487.
OpenTargetsiENSG00000185344.
Orphaneti357074. Autosomal recessive cutis laxa type 2, classic type.
2834. Wrinkly skin syndrome.
PharmGKBiPA38549.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2189. Eukaryota.
COG1269. LUCA.
GeneTreeiENSGT00390000004941.
HOGENOMiHOG000037059.
HOVERGENiHBG014606.
InParanoidiQ9Y487.
KOiK02154.
OMAiHPPAEHK.
OrthoDBiEOG091G01BI.
PhylomeDBiQ9Y487.
TreeFamiTF300346.

Enzyme and pathway databases

BioCyciMetaCyc:G66-33375-MONOMER.
ZFISH:G66-33375-MONOMER.
BRENDAi3.6.3.6. 2681.
ReactomeiR-HSA-1222556. ROS, RNS production in response to bacteria.
R-HSA-77387. Insulin receptor recycling.
R-HSA-917977. Transferrin endocytosis and recycling.
R-HSA-983712. Ion channel transport.

Miscellaneous databases

ChiTaRSiATP6V0A2. human.
GeneWikiiATP6V0A2.
GenomeRNAii23545.
PROiQ9Y487.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185344.
CleanExiHS_ATP6V0A2.
ExpressionAtlasiQ9Y487. baseline and differential.
GenevisibleiQ9Y487. HS.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVPP2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y487
Secondary accession number(s): A8K026, Q6NUM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 18, 2008
Last modified: November 2, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

The N-terminal peptide may increase IL1B secretion by peripheral blood monocytes; however as this region is probably in the cytosol, the in vivo relevance of this observation needs to be confirmed.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.