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Q3U2S8 (HVCN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Hvcn1
Synonyms:Bts, Vsop
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3 Ref.4 Ref.5 Ref.6

Enzyme regulation

The dimers display cooperative channel gating. The channel activity is inhibited by zinc ions. Ref.3 Ref.4 Ref.5

Subunit structure

Homodimer. Ref.5 Ref.6

Subcellular location

Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein Ref.3 Ref.5 Ref.6.

Tissue specificity

Enriched in immune tissues, such as bone marrow, macrophages and spleen. Ref.3

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. Ref.3

The C-terminal coiled coil region mediates homodimerization and cooperative channel gating. It is essential for normal subcellular localization. Ref.3

Post-translational modification

Phosphorylation may enhance channel gating By similarity.

Sequence similarities

Belongs to the hydrogen channel family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 269269Voltage-gated hydrogen channel 1
PRO_0000342188

Regions

Topological domain1 – 9696Cytoplasmic Potential
Transmembrane97 – 11721Helical; Name=Segment S1; By similarity
Topological domain118 – 13619Extracellular Potential
Transmembrane137 – 15721Helical; Name=Segment S2; By similarity
Topological domain158 – 1658Cytoplasmic Potential
Transmembrane166 – 18621Helical; Name=Segment S3; By similarity
Topological domain187 – 1937Extracellular Potential
Transmembrane194 – 21421Helical; Name=Segment S4; By similarity
Topological domain215 – 26955Cytoplasmic Potential
Coiled coil221 – 26141 Ref.5 Ref.6
Compositional bias46 – 538Poly-Glu
Compositional bias173 – 1764Poly-Val

Experimental info

Mutagenesis2011R → Q: Faster channel activation kinetics. Ref.3
Mutagenesis2071R → Q: Same activation kinetics as wild-type. Ref.3
Mutagenesis216 – 2183VKT → GGG: Impairs gating cooperativity. Ref.5
Mutagenesis230 – 2323INI → NIN: Slows channel activation. Ref.5
Mutagenesis2311N → L: No effect on channel activation kinetics. Ref.5
Sequence conflict661E → A in BAE33062. Ref.1

Secondary structure

... 269
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q3U2S8 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: B549CB553DEB6568

FASTA26931,242
        10         20         30         40         50         60 
MTSHDPKAVT RRTKVAPTKR MSRFLKHFTV VGDDYHTWNV NYKKWENEEE EEEPAPTSAE 

        70         80         90        100        110        120 
GEGNAEGPDA EAGSASTPRQ SLDFRSRLRK LFSSHRFQVI IICLVVLDAL LVLAELLLDL 

       130        140        150        160        170        180 
KIIEPDEQDY AVTAFHYMSF AILVFFMLEI FFKIFVFRLE FFHHKFEILD AFVVVVSFVL 

       190        200        210        220        230        240 
DLVLLFKSHH FEALGLLILL RLWRVARIIN GIIISVKTRS ERQILRLKQI NIQLATKIQH 

       250        260 
LEFSCSEKEQ EIERLNKLLK QNGLLGDVN 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Kidney.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Salivary gland.
[3]"A voltage sensor-domain protein is a voltage-gated proton channel."
Sasaki M., Takagi M., Okamura Y.
Science 312:589-592(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, ENZYME REGULATION, MUTAGENESIS OF ARG-201 AND ARG-207.
[4]"Voltage-gated proton channels maintain pH in human neutrophils during phagocytosis."
Morgan D., Capasso M., Musset B., Cherny V.V., Rios E., Dyer M.J., DeCoursey T.E.
Proc. Natl. Acad. Sci. U.S.A. 106:18022-18027(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[5]"The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H(+) channel Hv1."
Fujiwara Y., Kurokawa T., Takeshita K., Kobayashi M., Okochi Y., Nakagawa A., Okamura Y.
Nat. Commun. 3:816-816(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 220-266, SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, COILED COIL, MUTAGENESIS OF ASN-231; 216-VAL--THR-218 AND 230-ILE--ILE-232, ENZYME REGULATION.
[6]"Gating of the designed trimeric/tetrameric voltage-gated H+ channel."
Fujiwara Y., Kurokawa T., Takeshita K., Nakagawa A., Larsson H.P., Okamura Y.
J. Physiol. (Lond.) 591:627-640(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 220-269, SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, COILED COIL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001035954.1. NM_001042489.2.
NP_083028.1. NM_028752.3.
XP_006530535.1. XM_006530472.1.
XP_006530536.1. XM_006530473.1.
UniGeneMm.28804.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ3U2S8.
SMRQ3U2S8. Positions 96-210, 220-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46134N.
IntActQ3U2S8. 1 interaction.
MINTMINT-4128643.
STRING10090.ENSMUSP00000072401.

Protein family/group databases

TCDB1.A.51.1.1. the voltage-gated proton channel (vpc) family.

PTM databases

PhosphoSiteQ3U2S8.

Proteomic databases

PaxDbQ3U2S8.
PRIDEQ3U2S8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072602; ENSMUSP00000072401; ENSMUSG00000064267.
ENSMUST00000100747; ENSMUSP00000098312; ENSMUSG00000064267.
GeneID74096.
KEGGmmu:74096.
UCSCuc008zku.1. mouse.

Organism-specific databases

CTD84329.
MGIMGI:1921346. Hvcn1.

Phylogenomic databases

eggNOGNOG46709.
GeneTreeENSGT00530000063670.
HOGENOMHOG000067871.
HOVERGENHBG102207.
InParanoidQ3U2S8.
OMAEFSCSEK.
PhylomeDBQ3U2S8.
TreeFamTF332056.

Gene expression databases

ArrayExpressQ3U2S8.
BgeeQ3U2S8.
GenevestigatorQ3U2S8.

Family and domain databases

Gene3D1.20.120.350. 1 hit.
InterProIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
[Graphical view]
PfamPF00520. Ion_trans. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHVCN1. mouse.
NextBio339755.
PROQ3U2S8.
SOURCESearch...

Entry information

Entry nameHVCN1_MOUSE
AccessionPrimary (citable) accession number: Q3U2S8
Secondary accession number(s): Q9DCE4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: April 16, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot