Skip Header

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

Q8BVE3

- VATH_MOUSE

UniProt

Q8BVE3 - VATH_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

V-type proton ATPase subunit H

Gene

Atp6v1h

Organism
Mus musculus (Mouse)
Status
Reviewed - 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: Ensembl
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and 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: Chromosome 1

Organism-specific databases

MGIiMGI:1914864. Atp6v1h.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. lysosomal membrane Source: Ensembl
  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:
EMBL
GenBank
DDBJ
Links Updated
AK078767 mRNA. Translation: BAC37382.1.
BC009154 mRNA. Translation: AAH09154.1.
CCDSiCCDS14808.1.
RefSeqiNP_598587.2. NM_133826.4.
XP_006495496.1. XM_006495433.1.
UniGeneiMm.27082.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK078767 mRNA. Translation: BAC37382.1 .
BC009154 mRNA. Translation: AAH09154.1 .
CCDSi CCDS14808.1.
RefSeqi NP_598587.2. NM_133826.4.
XP_006495496.1. XM_006495433.1.
UniGenei Mm.27082.

3D structure databases

ProteinModelPortali Q8BVE3.
SMRi Q8BVE3. Positions 227-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 224360. 1 interaction.
IntActi Q8BVE3. 5 interactions.
MINTi MINT-4112764.
STRINGi 10090.ENSMUSP00000040756.

Protein family/group databases

TCDBi 3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSitei Q8BVE3.

Proteomic databases

MaxQBi Q8BVE3.
PaxDbi Q8BVE3.
PRIDEi Q8BVE3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000044369 ; ENSMUSP00000040756 ; ENSMUSG00000033793 .
GeneIDi 108664.
KEGGi mmu:108664.
UCSCi uc007afn.1. mouse.

Organism-specific databases

CTDi 51606.
MGIi MGI:1914864. Atp6v1h.

Phylogenomic databases

eggNOGi COG5231.
GeneTreei ENSGT00390000003289.
HOGENOMi HOG000007240.
HOVERGENi HBG000459.
InParanoidi Q8BVE3.
KOi K02144.
OMAi DTLQENH.
OrthoDBi EOG7CCBQQ.
PhylomeDBi Q8BVE3.
TreeFami TF313488.

Enzyme and pathway databases

Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSi ATP6V1H. mouse.
NextBioi 361187.
PROi Q8BVE3.
SOURCEi Search...

Gene expression databases

Bgeei Q8BVE3.
CleanExi MM_ATP6V1H.
ExpressionAtlasi Q8BVE3. baseline and differential.
Genevestigatori Q8BVE3.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view ]
PANTHERi PTHR10698. PTHR10698. 1 hit.
Pfami PF11698. V-ATPase_H_C. 1 hit.
PF03224. V-ATPase_H_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMi SSF48371. SSF48371. 1 hit.
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.
    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: October 29, 2014
This is version 102 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