ID   HVCN1_XENTR             Reviewed;         230 AA.
AC   Q5M8L8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Voltage-gated hydrogen channel 1;
DE   AltName: Full=Hydrogen voltage-gated channel 1;
DE            Short=HV1;
GN   Name=hvcn1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the voltage-dependent proton permeability of
CC       excitable membranes. Forms a proton-selective channel through which
CC       protons may pass in accordance with their electrochemical gradient (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at every
CC       third position. Unlike other voltage-gated ion channels it lacks the
CC       pore domain (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal coiled coil region mediates homodimerization. It
CC       is essential for normal subcellular localization (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hydrogen channel family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC087968; AAH87968.1; -; mRNA.
DR   RefSeq; NP_001011262.1; NM_001011262.1.
DR   RefSeq; XP_012816523.1; XM_012961069.2.
DR   RefSeq; XP_012816526.1; XM_012961072.2.
DR   AlphaFoldDB; Q5M8L8; -.
DR   SMR; Q5M8L8; -.
DR   PaxDb; Q5M8L8; -.
DR   DNASU; 496712; -.
DR   Ensembl; ENSXETT00000045238; ENSXETP00000045238; ENSXETG00000020934.
DR   GeneID; 496712; -.
DR   KEGG; xtr:496712; -.
DR   CTD; 84329; -.
DR   Xenbase; XB-GENE-955585; hvcn1.
DR   eggNOG; ENOG502RX8B; Eukaryota.
DR   HOGENOM; CLU_076372_0_0_1; -.
DR   InParanoid; Q5M8L8; -.
DR   OMA; HLEFSCT; -.
DR   OrthoDB; 1601156at2759; -.
DR   PhylomeDB; Q5M8L8; -.
DR   Reactome; R-XTR-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-XTR-1300642; Sperm Motility And Taxes.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000020934; Expressed in testis and 11 other tissues.
DR   ExpressionAtlas; Q5M8L8; baseline and differential.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030171; F:voltage-gated proton channel activity; ISS:UniProtKB.
DR   GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
DR   GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 1.
DR   InterPro; IPR031846; Hvcn1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR46480; PTHR46480; 1.
DR   Pfam; PF00520; Ion_trans; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN           1..230
FT                   /note="Voltage-gated hydrogen channel 1"
FT                   /id="PRO_0000342192"
FT   TOPO_DOM        1..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        59..79
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        80..96
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        97..119
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        120..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        128..148
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        149..155
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=Segment S4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        177..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   COILED          177..226
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   230 AA;  26575 MW;  60A58C62504AEC38 CRC64;
     MAGCLRHFTS VGDDTKKKAW KEEDVEVAHE EEPKNTPHPF IASYSFRGAL KWLFSSHKFQ
     IVIICLVILD ALFVLVEVLL DLELLAEKVD HIIPEIFHYL SISVLSFFIL EIAGKLYAFR
     LEFFHHKFEV FDAAIVVISF IIDIVYISRE DIFNAVGLLI LLRLWRVARI VNGIIVSVKT
     QAEDKIHRLK ENQESLLEKV AHLEQQCAQQ EQEIVRLQTL LQQHNVFPAS