Q13488 · VPP3_HUMAN
- ProteinV-type proton ATPase 116 kDa subunit a 3
- GeneTCIRG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids830 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Seems to be directly involved in T-cell activation (PubMed:10329006).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Seems to be directly involved in T-cell activation (PubMed:10329006).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameV-type proton ATPase 116 kDa subunit a 3
- Short namesV-ATPase 116 kDa subunit a 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13488
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-385 | Cytoplasmic | ||||
Sequence: MGSMFRSEEVALVQLFLPTAAAYTCVSRLGELGLVEFRDLNASVSAFQRRFVVDVRRCEELEKTFTFLQEEVRRAGLVLPPPKGRLPAPPPRDLLRIQEETERLAQELRDVRGNQQALRAQLHQLQLHAAVLRQGHEPQLAAAHTDGASERTPLLQAPGGPHQDLRVNFVAGAVEPHKAPALERLLWRACRGFLIASFRELEQPLEHPVTGEPATWMTFLISYWGEQIGQKIRKITDCFHCHVFPFLQQEEARLGALQQLQQQSQELQEVLGETERFLSQVLGRVLQLLPPGQVQVHKMKAVYLALNQCSVSTTHKCLIAEAWCSVRDLPALQEALRDSSMEEGVSAVAHRIPCRDMPPTLIRTNRFTASFQGIVDAYGVGRYQE | ||||||
Transmembrane | 386-404 | Helical | ||||
Sequence: VNPAPYTIITFPFLFAVMF | ||||||
Topological domain | 405-406 | Vacuolar | ||||
Sequence: GD | ||||||
Transmembrane | 407-423 | Helical | ||||
Sequence: VGHGLLMFLFALAMVLA | ||||||
Topological domain | 424-438 | Cytoplasmic | ||||
Sequence: ENRPAVKAAQNEIWQ | ||||||
Transmembrane | 439-468 | Helical | ||||
Sequence: TFFRGRYLLLLMGLFSIYTGFIYNECFSRA | ||||||
Topological domain | 469-532 | Vacuolar | ||||
Sequence: TSIFPSGWSVAAMANQSGWSDAFLAQHTMLTLDPNVTGVFLGPYPFGIDPIWSLAANHLSFLNS | ||||||
Transmembrane | 533-552 | Helical | ||||
Sequence: FKMKMSVILGVVHMAFGVVL | ||||||
Topological domain | 553-570 | Cytoplasmic | ||||
Sequence: GVFNHVHFGQRHRLLLET | ||||||
Transmembrane | 571-591 | Helical | ||||
Sequence: LPELTFLLGLFGYLVFLVIYK | ||||||
Topological domain | 592-635 | Vacuolar | ||||
Sequence: WLCVWAARAASAPSILIHFINMFLFSHSPSNRLLYPRQEVVQAT | ||||||
Transmembrane | 636-655 | Helical | ||||
Sequence: LVVLALAMVPILLLGTPLHL | ||||||
Topological domain | 656-720 | Cytoplasmic | ||||
Sequence: LHRHRRRLRRRPADRQEENKAGLLDLPDASVNGWSSDEEKAGGLDDEEEAELVPSEVLMHQAIHT | ||||||
Transmembrane | 721-745 | Helical | ||||
Sequence: IEFCLGCVSNTASYLRLWALSLAHA | ||||||
Topological domain | 746-766 | Vacuolar | ||||
Sequence: QLSEVLWAMVMRIGLGLGREV | ||||||
Transmembrane | 767-807 | Helical | ||||
Sequence: GVAAVVLVPIFAAFAVMTVAILLVMEGLSAFLHALRLHWVE | ||||||
Topological domain | 808-830 | Cytoplasmic | ||||
Sequence: FQNKFYSGTGYKLSPFTFAATDD |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Osteopetrosis, autosomal recessive 1 (OPTB1)
- Note
- DescriptionA rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves.
- See alsoMIM:259700
Natural variants in OPTB1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_020988 | 141 | A>P | in OPTB1 | |
VAR_019569 | 405 | G>R | in OPTB1; dbSNP:rs137853150 | |
VAR_019570 | 444 | R>L | in OPTB1; dbSNP:rs137853151 | |
VAR_020989 | 462 | missing | in OPTB1; dbSNP:rs771271907 | |
VAR_020990 | 517 | D>N | in OPTB1; dbSNP:rs369264588 | |
VAR_020991 | 775 | P>R | in OPTB1 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_054340 | 56 | in dbSNP:rs36027301 | |||
Sequence: R → W | ||||||
Natural variant | VAR_020988 | 141 | in OPTB1 | |||
Sequence: A → P | ||||||
Natural variant | VAR_054341 | 161 | in dbSNP:rs34227834 | |||
Sequence: P → L | ||||||
Natural variant | VAR_019569 | 405 | in OPTB1; dbSNP:rs137853150 | |||
Sequence: G → R | ||||||
Natural variant | VAR_019570 | 444 | in OPTB1; dbSNP:rs137853151 | |||
Sequence: R → L | ||||||
Natural variant | VAR_020989 | 462 | in OPTB1; dbSNP:rs771271907 | |||
Sequence: Missing | ||||||
Natural variant | VAR_020990 | 517 | in OPTB1; dbSNP:rs369264588 | |||
Sequence: D → N | ||||||
Natural variant | VAR_020991 | 775 | in OPTB1 | |||
Sequence: P → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,116 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000119218 | 1-830 | UniProt | V-type proton ATPase 116 kDa subunit a 3 | |||
Sequence: MGSMFRSEEVALVQLFLPTAAAYTCVSRLGELGLVEFRDLNASVSAFQRRFVVDVRRCEELEKTFTFLQEEVRRAGLVLPPPKGRLPAPPPRDLLRIQEETERLAQELRDVRGNQQALRAQLHQLQLHAAVLRQGHEPQLAAAHTDGASERTPLLQAPGGPHQDLRVNFVAGAVEPHKAPALERLLWRACRGFLIASFRELEQPLEHPVTGEPATWMTFLISYWGEQIGQKIRKITDCFHCHVFPFLQQEEARLGALQQLQQQSQELQEVLGETERFLSQVLGRVLQLLPPGQVQVHKMKAVYLALNQCSVSTTHKCLIAEAWCSVRDLPALQEALRDSSMEEGVSAVAHRIPCRDMPPTLIRTNRFTASFQGIVDAYGVGRYQEVNPAPYTIITFPFLFAVMFGDVGHGLLMFLFALAMVLAENRPAVKAAQNEIWQTFFRGRYLLLLMGLFSIYTGFIYNECFSRATSIFPSGWSVAAMANQSGWSDAFLAQHTMLTLDPNVTGVFLGPYPFGIDPIWSLAANHLSFLNSFKMKMSVILGVVHMAFGVVLGVFNHVHFGQRHRLLLETLPELTFLLGLFGYLVFLVIYKWLCVWAARAASAPSILIHFINMFLFSHSPSNRLLYPRQEVVQATLVVLALAMVPILLLGTPLHLLHRHRRRLRRRPADRQEENKAGLLDLPDASVNGWSSDEEKAGGLDDEEEAELVPSEVLMHQAIHTIEFCLGCVSNTASYLRLWALSLAHAQLSEVLWAMVMRIGLGLGREVGVAAVVLVPIFAAFAVMTVAILLVMEGLSAFLHALRLHWVEFQNKFYSGTGYKLSPFTFAATDD | |||||||
Modified residue (large scale data) | 685 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 691 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform long is highly expressed in osteoclastomas. Isoform short is highly expressed in thymus.
Gene expression databases
Organism-specific databases
Interaction
Subunit
V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (By similarity).
The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (By similarity).
The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By similarity).
The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (By similarity).
The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13488 | POGZ Q7Z3K3 | 3 | EBI-3914669, EBI-1389308 | |
BINARY | Q13488 | TLX3 O43711 | 3 | EBI-3914669, EBI-3939165 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 139-158 | Disordered | ||||
Sequence: QLAAAHTDGASERTPLLQAP | ||||||
Region | 681-701 | Disordered | ||||
Sequence: LPDASVNGWSSDEEKAGGLDD |
Sequence similarities
Belongs to the V-ATPase 116 kDa subunit family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q13488-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameLong
- Length830
- Mass (Da)92,968
- Last updated2009-02-10 v3
- Checksum50751B41B171D9D2
Q13488-2
- NameShort
- Differences from canonical
- 1-216: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q8TCH1 | Q8TCH1_HUMAN | TCIRG1 | 61 | ||
H0YEL3 | H0YEL3_HUMAN | TCIRG1 | 104 | ||
H0YCE3 | H0YCE3_HUMAN | TCIRG1 | 290 | ||
E9PNA6 | E9PNA6_HUMAN | TCIRG1 | 299 | ||
E9PM12 | E9PM12_HUMAN | TCIRG1 | 217 | ||
E9PMC5 | E9PMC5_HUMAN | TCIRG1 | 174 | ||
A0A8V8TNB5 | A0A8V8TNB5_HUMAN | TCIRG1 | 310 | ||
A0A8V8TM28 | A0A8V8TM28_HUMAN | TCIRG1 | 813 | ||
A0A8V8TN16 | A0A8V8TN16_HUMAN | TCIRG1 | 673 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_000345 | 1-216 | in isoform Short | |||
Sequence: Missing | ||||||
Sequence conflict | 377 | in Ref. 1; AAA97878 | ||||
Sequence: A → R | ||||||
Sequence conflict | 603 | in Ref. 1; AAA97878 | ||||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U45285 EMBL· GenBank· DDBJ | AAA97878.1 EMBL· GenBank· DDBJ | mRNA | ||
AF025374 EMBL· GenBank· DDBJ | AAC35742.1 EMBL· GenBank· DDBJ | mRNA | ||
AF033033 EMBL· GenBank· DDBJ | AAD31081.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471076 EMBL· GenBank· DDBJ | EAW74691.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC018133 EMBL· GenBank· DDBJ | AAH18133.1 EMBL· GenBank· DDBJ | mRNA | ||
BC032465 EMBL· GenBank· DDBJ | AAH32465.1 EMBL· GenBank· DDBJ | mRNA |