ID   HVCN1_CIOIN             Reviewed;         342 AA.
AC   Q1JV40;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Voltage-gated hydrogen channel 1;
DE   AltName: Full=Hydrogen voltage-gated channel 1;
DE            Short=HV1;
DE   AltName: Full=Voltage sensor domain-only protein;
GN   Name=HVCN1; Synonyms=VSOP, VSX1;
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16556803; DOI=10.1126/science.1122352;
RA   Sasaki M., Takagi M., Okamura Y.;
RT   "A voltage sensor-domain protein is a voltage-gated proton channel.";
RL   Science 312:589-592(2006).
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, ECO:0000269|PubMed:16556803}.
CC   -!- ACTIVITY REGULATION: Less sensitive to zinc ions as compared to the
CC       mammalian homologs. {ECO:0000269|PubMed:16556803}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:16556803};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16556803}.
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.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hydrogen channel family. {ECO:0000305}.
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DR   EMBL; AB218779; BAE94277.1; -; mRNA.
DR   RefSeq; NP_001071937.1; NM_001078469.1.
DR   AlphaFoldDB; Q1JV40; -.
DR   SMR; Q1JV40; -.
DR   DIP; DIP-46135N; -.
DR   STRING; 7719.NP_001071937.1; -.
DR   TCDB; 1.A.51.1.3; the voltage-gated proton channel (vpc) family.
DR   Ensembl; ENSCINT00000026764; ENSCINP00000026518; ENSCING00000014744.
DR   GeneID; 778897; -.
DR   KEGG; cin:778897; -.
DR   CTD; 84329; -.
DR   eggNOG; ENOG502RX8B; Eukaryota.
DR   GeneTree; ENSGT00940000174276; -.
DR   HOGENOM; CLU_799143_0_0_1; -.
DR   InParanoid; Q1JV40; -.
DR   OMA; KSHNMIN; -.
DR   OrthoDB; 1601156at2759; -.
DR   TreeFam; TF332056; -.
DR   Proteomes; UP000008144; Unassembled WGS sequence.
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..342
FT                   /note="Voltage-gated hydrogen channel 1"
FT                   /id="PRO_0000342193"
FT   TOPO_DOM        1..148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        149..169
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        170..185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        186..208
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        209..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        218..238
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        239..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        248..268
FT                   /note="Helical; Name=Segment S4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        269..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          271..315
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   342 AA;  38501 MW;  C4081816822DBF0A CRC64;
     MEGDNCNKSR HKSHNMINPN YASVRCTQPL PSVIQLRSRN KMIGITEDPS SDSEPVSSNQ
     PLLLTNLSYE VHTFNDNNNH ERPAPQEQST QNTMISMQSE QKSDRFTASN LGMFQYMKFE
     IGEDGDDHEE EAILTNREKL RHILHSKPIH VAIIVLVVLD SFLVVGELLI DLKVIIVPHG
     NPAPEILHGF SLSILSIFMV EIALKIIADH RHFIHHKVEV LDAVVVVISF GVDIALIFVG
     ESEALAAIGL LVILRLWRVF RIINGIIVTV KTKADDRVHE IKKKNSELEL QIHNLEEKLS
     QKEQDMSRLH EILRCNNIDI PPTVPLTTSV QIHSTTTASA DV