UniProt functional annotation for Q96D96



	UniProt functional annotation for Q96D96

UniProt code: Q96D96.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis. {ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:20037153, ECO:0000269|PubMed:22020278}.

Activity regulation: The dimers display cooperative channel gating (By similarity). The channel activity is inhibited by zinc ions. {ECO:0000250, ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:22020278}.

Subunit: Homodimer. {ECO:0000269|PubMed:20147290}.

Subcellular location: Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Detected mainly at intracellular membranes upon overexpression in HeLa cells (PuMed:20147290), but not in other cell types.

Tissue specificity: Enriched in immune tissues, such as lymph nodes, B- lymphocytes, monocytes and spleen. {ECO:0000269|PubMed:16554753}.

Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Unlike other voltage-gated ion channels it lacks the pore domain. {ECO:0000269|PubMed:20147290}.

Domain: The C-terminal coiled coil region mediates homodimerization and cooperative channel gating. It is essential for normal subcellular localization. {ECO:0000269|PubMed:20147290}.

Ptm: Phosphorylation may enhance channel gating. {ECO:0000269|PubMed:20037153}.

Similarity: Belongs to the hydrogen channel family. {ECO:0000305}.

Sequence caution: Sequence=AAQ89413.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis. {ECO:0000269\|PubMed:16554753, ECO:0000269\|PubMed:20037153, ECO:0000269\|PubMed:22020278}.


Activity regulation:		The dimers display cooperative channel gating (By similarity). The channel activity is inhibited by zinc ions. {ECO:0000250, ECO:0000269\|PubMed:16554753, ECO:0000269\|PubMed:22020278}.
Subunit:		Homodimer. {ECO:0000269\|PubMed:20147290}.
Subcellular location:		Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Detected mainly at intracellular membranes upon overexpression in HeLa cells (PuMed:20147290), but not in other cell types.
Tissue specificity:		Enriched in immune tissues, such as lymph nodes, B- lymphocytes, monocytes and spleen. {ECO:0000269\|PubMed:16554753}.
Domain:		The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Unlike other voltage-gated ion channels it lacks the pore domain. {ECO:0000269\|PubMed:20147290}.
Domain:		The C-terminal coiled coil region mediates homodimerization and cooperative channel gating. It is essential for normal subcellular localization. {ECO:0000269\|PubMed:20147290}.
Ptm:		Phosphorylation may enhance channel gating. {ECO:0000269\|PubMed:20037153}.
Similarity:		Belongs to the hydrogen channel family. {ECO:0000305}.
Sequence caution:		Sequence=AAQ89413.1; Type=Frameshift; Evidence={ECO:0000305};