Q3U2S8 (HVCN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Hvcn1
Synonyms:	Bts, Vsop

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. Ref.3
Enzyme regulation	Sensitive to zinc ions and is inhibited by them. Ref.3
Subunit structure	Homodimer By similarity.
Subcellular location	Membrane; Multi-pass membrane protein. Note: Associates mainly with intracellular compartment membranes By similarity. Ref.3
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 is essential for localization By similarity. Ref.3
Sequence similarities	Belongs to the hydrogen channel family.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Membrane
Domain	Coiled coil Transmembrane Transmembrane helix
Molecular function	Ion channel Voltage-gated channel
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to pH Inferred from direct assay Ref.3. Source: HGNC response to zinc ion Inferred from direct assay Ref.3. Source: HGNC
Cellular_component	integral to membrane Inferred by curator Ref.3. Source: HGNC
Molecular_function	voltage-gated proton channel activity Inferred from direct assay Ref.3. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 269

269

Voltage-gated hydrogen channel 1

PRO_0000342188

Regions

Topological domain

1 – 96

96

Cytoplasmic Potential

Transmembrane

97 – 117

21

Helical; Name=Segment S1; By similarity

Topological domain

118 – 136

19

Extracellular Potential

Transmembrane

137 – 157

21

Helical; Name=Segment S2; By similarity

Topological domain

158 – 165

8

Cytoplasmic Potential

Transmembrane

166 – 186

21

Helical; Name=Segment S3; By similarity

Topological domain

187 – 193

7

Extracellular Potential

Transmembrane

194 – 214

21

Helical; Name=Segment S4; By similarity

Topological domain

215 – 269

55

Cytoplasmic Potential

Coiled coil

221 – 261

41

Potential

Compositional bias

46 – 53

8

Poly-Glu

Compositional bias

173 – 176

4

Poly-Val

Experimental info

Mutagenesis

201

1

R → Q: Faster channel activation kinetics. Ref.3

Mutagenesis

207

1

R → Q: Same activation kinetics as wild-type. Ref.3

Sequence conflict

66

1

E → A in BAE33062. Ref.1

Secondary structure

1

.

.

.

269

Helix Strand Turn

Details...

Helix

220 – 261

42

Sequences

	Sequence		Length	Mass (Da)
	Q3U2S8 [UniParc]. Last modified July 1, 2008. Version 2. Checksum: B549CB553DEB6568	FASTA	269	31,242
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.

IPI

IPI00120788.

RefSeq

NP_001035954.1. NM_001042489.1.
NP_083028.1. NM_028752.2.

UniGene

Mm.28804.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q3U2S8.

SMR

Q3U2S8. Positions 220-266.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46134N.

STRING

10090.ENSMUSP00000072401.

Protein family/group databases

TCDB

1.A.51.1.1. voltage-gated proton channel (VPC) family.

PTM databases

PhosphoSite

Q3U2S8.

Proteomic databases

PaxDb

Q3U2S8.

PRIDE

Q3U2S8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000072602; ENSMUSP00000072401; ENSMUSG00000064267.
ENSMUST00000100747; ENSMUSP00000098312; ENSMUSG00000064267.

GeneID

74096.

KEGG

mmu:74096.

UCSC

uc008zku.1. mouse.

Organism-specific databases

CTD

84329.

MGI

MGI:1921346. Hvcn1.

Phylogenomic databases

eggNOG

NOG46709.

GeneTree

ENSGT00530000063670.

HOGENOM

HOG000067871.

HOVERGEN

HBG102207.

InParanoid

Q3U2S8.

OMA

FFMMEIF.

OrthoDB

EOG4GF3G9.

Gene expression databases

ArrayExpress

Q3U2S8.

Bgee

Q3U2S8.

Genevestigator

Q3U2S8.

Family and domain databases

InterPro

IPR005821. Ion_trans_dom.
[Graphical view]

Pfam

PF00520. Ion_trans. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HVCN1. mouse.

NextBio

339755.

SOURCE

Search...

Entry information

Entry name

HVCN1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program