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Q3U2S8

- HVCN1_MOUSE

UniProt

Q3U2S8 - HVCN1_MOUSE

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Protein

Voltage-gated hydrogen channel 1

Gene

Hvcn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- 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

  1. voltage-gated proton channel activity Source: HGNC

GO - Biological processi

  1. cellular response to pH Source: UniProtKB
  2. cellular response to zinc ion Source: UniProtKB
  3. proton transport Source: HGNC
  4. response to pH Source: HGNC
  5. response to zinc ion Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_196630. Sperm Motility And Taxes.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1921346. Hvcn1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9696CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei97 – 11721Helical; Name=Segment S1Add
BLAST
Topological domaini118 – 13417ExtracellularSequence AnalysisAdd
BLAST
Transmembranei135 – 15723Helical; Name=Segment S2Add
BLAST
Topological domaini158 – 1658CytoplasmicSequence Analysis
Transmembranei166 – 18621Helical; Name=Segment S3Add
BLAST
Topological domaini187 – 1937ExtracellularSequence Analysis
Transmembranei194 – 21421Helical; Name=Segment S4Add
BLAST
Topological domaini215 – 26955CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: HGNC
  2. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011R → Q: Faster channel activation kinetics. 1 Publication
Mutagenesisi207 – 2071R → Q: Same activation kinetics as wild-type. 1 Publication
Mutagenesisi216 – 2183VKT → GGG: Impairs gating cooperativity. 1 Publication
Mutagenesisi230 – 2323INI → NIN: Slows channel activation. 1 Publication
Mutagenesisi231 – 2311N → L: No effect on channel activation kinetics. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Voltage-gated hydrogen channel 1PRO_0000342188Add
BLAST

Post-translational modificationi

Phosphorylation may enhance channel gating.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3U2S8.
PaxDbiQ3U2S8.
PRIDEiQ3U2S8.

PTM databases

PhosphoSiteiQ3U2S8.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ3U2S8.
ExpressionAtlasiQ3U2S8. baseline and differential.
GenevestigatoriQ3U2S8.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

DIPiDIP-46134N.
IntActiQ3U2S8. 1 interaction.
MINTiMINT-4128643.
STRINGi10090.ENSMUSP00000072401.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi87 – 904Combined sources
Helixi96 – 12025Combined sources
Helixi134 – 15522Combined sources
Helixi164 – 18421Combined sources
Helixi193 – 21523Combined sources
Helixi220 – 26142Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 87-208, 220-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili221 – 261412 PublicationsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi46 – 538Poly-Glu
Compositional biasi173 – 1764Poly-Val

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

eggNOGiNOG46709.
GeneTreeiENSGT00530000063670.
HOGENOMiHOG000067871.
HOVERGENiHBG102207.
InParanoidiQ3U2S8.
OMAiEFSCSEK.
PhylomeDBiQ3U2S8.
TreeFamiTF332056.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
[Graphical view]
PfamiPF00520. Ion_trans. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661E → A in BAE33062. (PubMed:16141072)Curated

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_006530472.1.
XP_006530536.1. XM_006530473.1.
UniGeneiMm.28804.

Genome annotation databases

EnsembliENSMUST00000072602; ENSMUSP00000072401; ENSMUSG00000064267.
ENSMUST00000100747; ENSMUSP00000098312; ENSMUSG00000064267.
GeneIDi74096.
KEGGimmu:74096.
UCSCiuc008zku.1. mouse.

Cross-referencesi

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 .
CCDSi CCDS19644.1.
RefSeqi NP_001035954.1. NM_001042489.2.
NP_083028.1. NM_028752.3.
XP_006530535.1. XM_006530472.1.
XP_006530536.1. XM_006530473.1.
UniGenei Mm.28804.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VMX X-ray 1.45 A/B/C/D 220-266 [» ]
3VMY X-ray 1.47 A/B/C/D 220-269 [» ]
3VMZ X-ray 1.55 A/B/C/D 220-269 [» ]
3VN0 X-ray 1.37 A/B/C/D 220-269 [» ]
3VYI X-ray 2.30 A/B/C/D/E/F/G/H/I/J/K/L 220-269 [» ]
3WKV X-ray 3.45 A 73-215 [» ]
ProteinModelPortali Q3U2S8.
SMRi Q3U2S8. Positions 87-208, 220-266.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-46134N.
IntActi Q3U2S8. 1 interaction.
MINTi MINT-4128643.
STRINGi 10090.ENSMUSP00000072401.

Protein family/group databases

TCDBi 1.A.51.1.1. the voltage-gated proton channel (vpc) family.

PTM databases

PhosphoSitei Q3U2S8.

Proteomic databases

MaxQBi Q3U2S8.
PaxDbi Q3U2S8.
PRIDEi Q3U2S8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000072602 ; ENSMUSP00000072401 ; ENSMUSG00000064267 .
ENSMUST00000100747 ; ENSMUSP00000098312 ; ENSMUSG00000064267 .
GeneIDi 74096.
KEGGi mmu:74096.
UCSCi uc008zku.1. mouse.

Organism-specific databases

CTDi 84329.
MGIi MGI:1921346. Hvcn1.

Phylogenomic databases

eggNOGi NOG46709.
GeneTreei ENSGT00530000063670.
HOGENOMi HOG000067871.
HOVERGENi HBG102207.
InParanoidi Q3U2S8.
OMAi EFSCSEK.
PhylomeDBi Q3U2S8.
TreeFami TF332056.

Enzyme and pathway databases

Reactomei REACT_196630. Sperm Motility And Taxes.

Miscellaneous databases

ChiTaRSi Hvcn1. mouse.
NextBioi 339755.
PROi Q3U2S8.
SOURCEi Search...

Gene expression databases

Bgeei Q3U2S8.
ExpressionAtlasi Q3U2S8. baseline and differential.
Genevestigatori Q3U2S8.

Family and domain databases

Gene3Di 1.20.120.350. 1 hit.
InterProi IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
[Graphical view ]
Pfami PF00520. Ion_trans. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 73-215, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, ENZYME REGULATION.

Entry informationi

Entry nameiHVCN1_MOUSE
AccessioniPrimary (citable) accession number: Q3U2S8
Secondary accession number(s): Q9DCE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: November 26, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3