Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Voltage-gated hydrogen channel 1

Gene

Hvcn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.5 Publications

Enzyme regulationi

The dimers display cooperative channel gating. The channel activity is inhibited by zinc ions.4 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • voltage-gated proton channel activity Source: HGNC

GO - Biological processi

  • cellular response to pH Source: UniProtKB
  • cellular response to zinc ion Source: UniProtKB
  • proton transmembrane transport Source: HGNC
  • regulation of ion transmembrane transport Source: UniProtKB-KW
  • response to pH Source: HGNC
  • response to zinc ion Source: HGNC

Keywordsi

Molecular functionIon channel, Voltage-gated channel
Biological processIon transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-1300642 Sperm Motility And Taxes
R-MMU-6798695 Neutrophil degranulation

Protein family/group databases

TCDBi1.A.51.1.1 the voltage-gated proton channel (vpc) family

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated hydrogen channel 1
Alternative name(s):
Hydrogen voltage-gated channel 1
Short name:
HV1
Voltage sensor domain-only protein
Short name:
mVSOP
Gene namesi
Name:Hvcn1
Synonyms:Bts, Vsop
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1921346 Hvcn1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 96CytoplasmicSequence analysisAdd BLAST96
Transmembranei97 – 117Helical; Name=Segment S1Add BLAST21
Topological domaini118 – 134ExtracellularSequence analysisAdd BLAST17
Transmembranei135 – 157Helical; Name=Segment S2Add BLAST23
Topological domaini158 – 165CytoplasmicSequence analysis8
Transmembranei166 – 186Helical; Name=Segment S3Add BLAST21
Topological domaini187 – 193ExtracellularSequence analysis7
Transmembranei194 – 214Helical; Name=Segment S4Add BLAST21
Topological domaini215 – 269CytoplasmicSequence analysisAdd BLAST55

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi201R → Q: Faster channel activation kinetics. 1 Publication1
Mutagenesisi207R → Q: Same activation kinetics as wild-type. 1 Publication1
Mutagenesisi216 – 218VKT → GGG: Impairs gating cooperativity. 1 Publication3
Mutagenesisi230 – 232INI → NIN: Slows channel activation. 1 Publication3
Mutagenesisi231N → L: No effect on channel activation kinetics. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003421881 – 269Voltage-gated hydrogen channel 1Add BLAST269

Post-translational modificationi

Phosphorylation may enhance channel gating.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3U2S8
MaxQBiQ3U2S8
PaxDbiQ3U2S8
PRIDEiQ3U2S8
TopDownProteomicsiQ3U2S8

PTM databases

iPTMnetiQ3U2S8
PhosphoSitePlusiQ3U2S8

Expressioni

Tissue specificityi

Enriched in immune tissues, such as bone marrow, macrophages and spleen.1 Publication

Gene expression databases

BgeeiENSMUSG00000064267
ExpressionAtlasiQ3U2S8 baseline and differential
GenevisibleiQ3U2S8 MM

Interactioni

Subunit structurei

Homodimer.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-8401579,EBI-8401579

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-46134N
IntActiQ3U2S8, 1 interactor
MINTiQ3U2S8
STRINGi10090.ENSMUSP00000072401

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi87 – 90Combined sources4
Helixi96 – 120Combined sources25
Helixi134 – 155Combined sources22
Helixi164 – 184Combined sources21
Helixi220 – 261Combined sources42

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VMXX-ray1.45A/B/C/D220-266[»]
3VMYX-ray1.47A/B/C/D220-269[»]
3VMZX-ray1.55A/B/C/D220-269[»]
3VN0X-ray1.37A/B/C/D220-269[»]
3VYIX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L220-269[»]
3WKVX-ray3.45A73-215[»]
ProteinModelPortaliQ3U2S8
SMRiQ3U2S8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili221 – 2612 PublicationsAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi46 – 53Poly-Glu8
Compositional biasi173 – 176Poly-Val4

Domaini

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.1 Publication
The C-terminal coiled coil region mediates homodimerization and cooperative channel gating. It is essential for normal subcellular localization.1 Publication

Sequence similaritiesi

Belongs to the hydrogen channel family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IKBG Eukaryota
ENOG4111XHU LUCA
GeneTreeiENSGT00530000063670
HOGENOMiHOG000067871
HOVERGENiHBG102207
InParanoidiQ3U2S8
OMAiRMSKFLK
OrthoDBiEOG091G0L8G
PhylomeDBiQ3U2S8
TreeFamiTF332056

Family and domain databases

Gene3Di1.20.120.350, 1 hit
InterProiView protein in InterPro
IPR031846 Hvcn1
IPR005821 Ion_trans_dom
IPR031844 VGPC1_C
IPR027359 Volt_channel_dom_sf
PANTHERiPTHR12305:SF47 PTHR12305:SF47, 1 hit
PfamiView protein in Pfam
PF00520 Ion_trans, 1 hit
PF16799 VGPC1_C, 1 hit

Sequencei

Sequence statusi: Complete.

Q3U2S8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSHDPKAVT RRTKVAPTKR MSRFLKHFTV VGDDYHTWNV NYKKWENEEE
60 70 80 90 100
EEEPAPTSAE GEGNAEGPDA EAGSASTPRQ SLDFRSRLRK LFSSHRFQVI
110 120 130 140 150
IICLVVLDAL LVLAELLLDL KIIEPDEQDY AVTAFHYMSF AILVFFMLEI
160 170 180 190 200
FFKIFVFRLE FFHHKFEILD AFVVVVSFVL DLVLLFKSHH FEALGLLILL
210 220 230 240 250
RLWRVARIIN GIIISVKTRS ERQILRLKQI NIQLATKIQH LEFSCSEKEQ
260
EIERLNKLLK QNGLLGDVN
Length:269
Mass (Da):31,242
Last modified:July 1, 2008 - v2
Checksum:iB549CB553DEB6568
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66E → A in BAE33062 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002854 mRNA Translation: BAB22409.1
AK154880 mRNA Translation: BAE32899.1
AK155123 mRNA Translation: BAE33062.1
AK170422 mRNA Translation: BAE41787.1
BC021548 mRNA Translation: AAH21548.1
CCDSiCCDS19644.1
RefSeqiNP_001035954.1, NM_001042489.2
NP_083028.1, NM_028752.3
XP_006530535.1, XM_006530472.2
XP_006530536.1, XM_006530473.1
UniGeneiMm.28804

Genome annotation databases

EnsembliENSMUST00000072602; ENSMUSP00000072401; ENSMUSG00000064267
ENSMUST00000100747; ENSMUSP00000098312; ENSMUSG00000064267
GeneIDi74096
KEGGimmu:74096
UCSCiuc008zku.2 mouse

Similar proteinsi

Entry informationi

Entry nameiHVCN1_MOUSE
AccessioniPrimary (citable) accession number: Q3U2S8
Secondary accession number(s): Q9DCE4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: April 25, 2018
This is version 105 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health