HVCN1
entrez
84329
canonical
uniprot
Q96D96
canonical
ensembl
ENSG00000122986
resolver
ensp
ENSP00000242607
resolver
ensp
ENSP00000412052
resolver
ensp
ENSP00000558619
resolver
ensp
ENSP00000558620
resolver
ensp
ENSP00000558622
resolver
ensp
ENSP00000558623
resolver
ensp
ENSP00000558624
resolver
ensp
ENSP00000618706
resolver
ensp
ENSP00000618711
resolver
ensp
ENSP00000722192
resolver
ensp
ENSP00000771987
resolver
genesymbol
HVCN1
resolver
genesymbol_syn
VSOP
resolver
hgnc
HGNC:28240
resolver
uniprot
A8MQ37
resolver
uniprot
B4DEB3
resolver
uniprot
F8WCH5
resolver
uniprot
Q6UW11
resolver
uniprot
Q96IS5
resolver
uniprot_entry
HVCN1_HUMAN
resolver
uniprot_sec
A8MQ37
resolver
uniprot_sec
B4DEB3
resolver
uniprot_sec
F8WCH5
resolver
uniprot_sec
Q6UW11
resolver
uniprot_sec
Q96IS5
resolver
activity_regulation
ACTIVITY REGULATION: The channel gating depends on both the membrane potential and the transmembrane pH gradient. The dimers display cooperative channel gating (By similarity). The channel activity is inhibited by zinc ions and by toxins, and activated by endocannabinoid anandamide and fatty acids. {ECO:0000250, ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:20548053, ECO:0000269|PubMed:22020278}.
uniprot
proteins
amino_acid_sequence
MATWDEKAVTRRAKVAPAERMSKFLRHFTVVGDDYHAWNINYKKWENEEEEEEEEQPPPTPVSGEEGRAAAPDVAPAPGPAPRAPLDFRGMLRKLFSSHRFQVIIICLVVLDALLVLAELILDLKIIQPDKNNYAAMVFHYMSITILVFFMMEIIFKLFVFRLEFFHHKFEILDAVVVVVSFILDIVLLFQEHQFEALGLLILLRLWRVARIINGIIISVKTRSERQLLRLKQMNVQLAAKIQHLEFSCSEKEQEIERLNKLLRQHGLLGEVN
uniprot
proteins
function
FUNCTION: Voltage-gated proton-selective channel that conducts outward proton currents in response to intracellular acidification. Lacks a canonical ion-channel pore domain and mediates proton permeability via its voltage sensor domain (PubMed:16554753, PubMed:20037153, PubMed:20548053, PubMed:22020278, PubMed:27859356, PubMed:30478045, PubMed:37669933). Appears to play a dominant role in regulation of CO2/HCO3(-)/H(+) equilibrium in sperm flagellum. Prevents the acidification resulting from HCO3(-) synthesis and thus sustains high HCO3(-) levels inside sperm for capacitation (PubMed:20144758, PubMed:30478045, PubMed:37669933). Provides for proton efflux that compensates for electron charge generated by NADPH oxidase activity either in the extracellular or phagosomal compartments, thus enabling the production of high levels of bactericidal reactive oxygen species during the respiratory burst (PubMed:20037153, PubMed:30478045). Opens when the pH of airway surface liquid exceeds 7 and contributes to respiratory epithelial acid secretion to maintain pH in the mucosa (PubMed:20548053). {ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:20037153, ECO:0000269|PubMed:20144758, ECO:0000269|PubMed:20548053, ECO:0000269|PubMed:22020278, ECO:0000269|PubMed:27859356, ECO:0000269|PubMed:30478045, ECO:0000269|PubMed:37669933}.
uniprot
proteins
mass_dalton
31683
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="T->A: Loss of a phosphorylation site. Reduces phosphorylation."; /evidence="ECO:0000269|PubMed:20037153"; MUTAGEN 97; /note="S->A: Loss of a phosphorylation site. Strongly reduces phosphorylation."; /evidence="ECO:0000269|PubMed:20037153"; MUTAGEN 112; /note="D->A,F,N,S: Alters channel selectivity. Converts the proton channel to an anion channel."; /evidence="ECO:0000269|PubMed:22020278"; MUTAGEN 112; /note="D->E: No effect on channel activity and proton selectivity."; /evidence="ECO:0000269|PubMed:22020278"; MUTAGEN 112; /note="D->V: Abolishes channel activity."; /evidence="ECO:0000269|PubMed:22020278"; MUTAGEN 140; /note="H->A: Exhibits selectivity to protons but sensitivity to zinc ions is abolished; when associated with A-193."; /evidence="ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:22020278"; MUTAGEN 193; /note="H->A: Exhibits selectivity to protons but sensitivity to zinc ions is abolished; when associated with A-140."; /evidence="ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:22020278"; MUTAGEN 205; /note="R->A: Faster channel activation and deactivation kinetics."; /evidence="ECO:0000269|PubMed:16554753"; MUTAGEN 208; /note="R->A: Faster channel activation and deactivation kinetics."; /evidence="ECO:0000269|PubMed:16554753"; MUTAGEN 211; /note="R->A: Faster channel deactivation kinetics."; /evidence="ECO:0000269|PubMed:16554753
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved in sperm. The cleaved protomer forms homodimers and heterodimers with the full-length protomer. It confers reduced dependence to intracellular pH changes. {ECO:0000269|PubMed:27859356}.; PTM: Phosphorylated in vitro by PRKCD. Phosphorylation may enhance channel gating. {ECO:0000269|PubMed:20037153}.
uniprot
proteins
protein_family
Voltage-gated proton channel (VPC) (TC 1.A.51) family
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16554753
uniprot
proteins
pubmed
20037153
uniprot
proteins
pubmed
20144758
uniprot
proteins
pubmed
20147290
uniprot
proteins
pubmed
20548053
uniprot
proteins
pubmed
22020278
uniprot
proteins
pubmed
24415791
uniprot
proteins
pubmed
27859356
uniprot
proteins
pubmed
30478045
uniprot
proteins
pubmed
37669933
uniprot
proteins
sequence_length
273
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20144758, ECO:0000269|PubMed:22020278}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000305|PubMed:20548053}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:24415791}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:20144758}; Multi-pass membrane protein {ECO:0000255}. Note=Detected within the principal piece of the sperm flagellum (PubMed:20144758). Detected mainly at intracellular membranes upon overexpression in HeLa cells (PubMed:20147290). {ECO:0000269|PubMed:20144758, ECO:0000269|PubMed:20147290}.
uniprot
proteins
transmembrane_region
TRANSMEM 101..121; /note="Helical; Name=Segment S1"; /evidence="ECO:0000250"; TRANSMEM 139..161; /note="Helical; Name=Segment S2"; /evidence="ECO:0000250"; TRANSMEM 170..190; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250"; TRANSMEM 198..218; /note="Helical; Name=Segment S4"; /evidence="ECO:0000250
uniprot
proteins