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Protein

V-type proton ATPase subunit H

Gene

Atp6v1h

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes (By similarity).By similarity

GO - Molecular functioni

  1. proton-transporting ATPase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. endocytosis Source: MGI
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_284331. Phagosomal maturation (early endosomal stage).
REACT_290403. Transferrin endocytosis and recycling.
REACT_324664. Insulin receptor recycling.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit H
Short name:
V-ATPase subunit H
Alternative name(s):
Vacuolar proton pump subunit H
Gene namesi
Name:Atp6v1h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1914864. Atp6v1h.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. lysosomal membrane Source: MGI
  3. vacuolar proton-transporting V-type ATPase, V1 domain Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483V-type proton ATPase subunit HPRO_0000124194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei483 – 4831PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BVE3.
PaxDbiQ8BVE3.
PRIDEiQ8BVE3.

PTM databases

PhosphoSiteiQ8BVE3.

Expressioni

Gene expression databases

BgeeiQ8BVE3.
CleanExiMM_ATP6V1H.
ExpressionAtlasiQ8BVE3. baseline and differential.
GenevestigatoriQ8BVE3.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). Interacts with AP2M1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi224360. 1 interaction.
IntActiQ8BVE3. 5 interactions.
MINTiMINT-4112764.
STRINGi10090.ENSMUSP00000040756.

Structurei

3D structure databases

ProteinModelPortaliQ8BVE3.
SMRiQ8BVE3. Positions 227-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase H subunit family.Curated

Phylogenomic databases

eggNOGiCOG5231.
GeneTreeiENSGT00390000003289.
HOGENOMiHOG000007240.
HOVERGENiHBG000459.
InParanoidiQ8BVE3.
KOiK02144.
OMAiDTLQENH.
OrthoDBiEOG7CCBQQ.
PhylomeDBiQ8BVE3.
TreeFamiTF313488.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PANTHERiPTHR10698. PTHR10698. 1 hit.
PfamiPF11698. V-ATPase_H_C. 1 hit.
PF03224. V-ATPase_H_N. 1 hit.
[Graphical view]
PIRSFiPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BVE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI
60 70 80 90 100
QRFEMKRSSE DKQEMLQTEG SQCAKTFINL MTHISKEQTV QYILTMVDDM
110 120 130 140 150
LQENHQRVSI FFDYAKRSKS TAWPYFLPML NRQDPFTVHM AARIIAKLAA
160 170 180 190 200
WGKELMEGSD LNYYFNWIKT QLSSQKLRGS GVAVETGTIS SSDSSQYVQC
210 220 230 240 250
VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ YQMIFSIWLL
260 270 280 290 300
AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE
310 320 330 340 350
TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS
360 370 380 390 400
SFDEYSSELK SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV
410 420 430 440 450
SDDPQVLAVA AHDVGEYVRH YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY
460 470 480
NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA ARS
Length:483
Mass (Da):55,855
Last modified:March 1, 2003 - v1
Checksum:iA976B7DC889B84CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti247 – 2471I → V in AAH09154 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK078767 mRNA. Translation: BAC37382.1.
BC009154 mRNA. Translation: AAH09154.1.
CCDSiCCDS14808.1.
RefSeqiNP_598587.2. NM_133826.4.
XP_006495496.1. XM_006495433.2.
UniGeneiMm.27082.

Genome annotation databases

EnsembliENSMUST00000044369; ENSMUSP00000040756; ENSMUSG00000033793.
GeneIDi108664.
KEGGimmu:108664.
UCSCiuc007afn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK078767 mRNA. Translation: BAC37382.1.
BC009154 mRNA. Translation: AAH09154.1.
CCDSiCCDS14808.1.
RefSeqiNP_598587.2. NM_133826.4.
XP_006495496.1. XM_006495433.2.
UniGeneiMm.27082.

3D structure databases

ProteinModelPortaliQ8BVE3.
SMRiQ8BVE3. Positions 227-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224360. 1 interaction.
IntActiQ8BVE3. 5 interactions.
MINTiMINT-4112764.
STRINGi10090.ENSMUSP00000040756.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteiQ8BVE3.

Proteomic databases

MaxQBiQ8BVE3.
PaxDbiQ8BVE3.
PRIDEiQ8BVE3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044369; ENSMUSP00000040756; ENSMUSG00000033793.
GeneIDi108664.
KEGGimmu:108664.
UCSCiuc007afn.1. mouse.

Organism-specific databases

CTDi51606.
MGIiMGI:1914864. Atp6v1h.

Phylogenomic databases

eggNOGiCOG5231.
GeneTreeiENSGT00390000003289.
HOGENOMiHOG000007240.
HOVERGENiHBG000459.
InParanoidiQ8BVE3.
KOiK02144.
OMAiDTLQENH.
OrthoDBiEOG7CCBQQ.
PhylomeDBiQ8BVE3.
TreeFamiTF313488.

Enzyme and pathway databases

ReactomeiREACT_284331. Phagosomal maturation (early endosomal stage).
REACT_290403. Transferrin endocytosis and recycling.
REACT_324664. Insulin receptor recycling.

Miscellaneous databases

NextBioi361187.
PROiQ8BVE3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BVE3.
CleanExiMM_ATP6V1H.
ExpressionAtlasiQ8BVE3. baseline and differential.
GenevestigatoriQ8BVE3.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PANTHERiPTHR10698. PTHR10698. 1 hit.
PfamiPF11698. V-ATPase_H_C. 1 hit.
PF03224. V-ATPase_H_N. 1 hit.
[Graphical view]
PIRSFiPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

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.
    Tissue: Testis.
  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: Mammary tumor.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 76-86; 108-116; 263-278; 284-290; 342-360; 397-419 AND 450-458, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiVATH_MOUSE
AccessioniPrimary (citable) accession number: Q8BVE3
Secondary accession number(s): Q921X8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: March 1, 2003
Last modified: April 1, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.