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Protein

V-type proton ATPase 16 kDa proteolipid subunit

Gene

Atp6v0c

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

Functioni

Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei139 – 1391Essential for proton translocationBy similarity

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • lysosomal lumen acidification Source: MGI
  • positive regulation of Wnt signaling pathway Source: MGI
  • vacuolar acidification Source: MGI
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-77387. Insulin receptor recycling.
R-MMU-917977. Transferrin endocytosis and recycling.
R-MMU-983712. Ion channel transport.

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 16 kDa proteolipid subunit
Short name:
V-ATPase 16 kDa proteolipid subunit
Alternative name(s):
PL16
Vacuolar proton pump 16 kDa proteolipid subunit
Gene namesi
Name:Atp6v0c
Synonyms:Atp6c, Atp6l, Atpl, Mvp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:88116. Atp6v0c.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010LumenalSequence analysis
Transmembranei11 – 3323HelicalSequence analysisAdd
BLAST
Topological domaini34 – 5522CytoplasmicSequence analysisAdd
BLAST
Transmembranei56 – 7621HelicalSequence analysisAdd
BLAST
Topological domaini77 – 9216LumenalSequence analysisAdd
BLAST
Transmembranei93 – 11422HelicalSequence analysisAdd
BLAST
Topological domaini115 – 13117CytoplasmicSequence analysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Topological domaini153 – 1553LumenalSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155V-type proton ATPase 16 kDa proteolipid subunitPRO_0000071744Add
BLAST

Post-translational modificationi

Ubiquitinated by RNF182, leading to its degradation via the ubiquitin-proteasome pathway.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiP63082.
MaxQBiP63082.
PaxDbiP63082.
PRIDEiP63082.
TopDownProteomicsiP63082.

PTM databases

iPTMnetiP63082.
PhosphoSiteiP63082.

Expressioni

Gene expression databases

BgeeiP63082.
CleanExiMM_ATP6V0C.
MM_MVP.
ExpressionAtlasiP63082. baseline.
GenevisibleiP63082. MM.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein; which is present as a hexamer that forms the proton-conducting pore). Interacts with RNF182; this interaction leads to ubiquitination and degradation via the proteasome pathway (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198274. 3 interactions.
IntActiP63082. 2 interactions.
MINTiMINT-1581356.
STRINGi10090.ENSMUSP00000024932.

Structurei

3D structure databases

ProteinModelPortaliP63082.
SMRiP63082. Positions 13-155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00550000074873.
HOVERGENiHBG002712.
InParanoidiP63082.
KOiK02155.
OMAiVEDNDMF.
OrthoDBiEOG7FV3RW.
PhylomeDBiP63082.
TreeFamiTF300025.

Family and domain databases

HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.

Sequencei

Sequence statusi: Complete.

P63082-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADIKNNPEY SSFFGVMGAS SAMVFSAMGA AYGTAKSGTG IAAMSVMRPE
60 70 80 90 100
LIMKSIIPVV MAGIIAIYGL VVAVLIANSL TDGITLYRSF LQLGAGLSVG
110 120 130 140 150
LSGLAAGFAI GIVGDAGVRG TAQQPRLFVG MILILIFAEV LGLYGLIVAL

ILSTK
Length:155
Mass (Da):15,808
Last modified:September 13, 2004 - v1
Checksum:i880C280C5AEB0C5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64298 mRNA. Translation: AAA39775.1.
U13842 Genomic DNA. Translation: AAC52413.1.
AB059662 Genomic DNA. Translation: BAB64538.1.
AF356008 Genomic DNA. Translation: AAL02098.1.
AK002570 mRNA. Translation: BAB22195.1.
AK002871 mRNA. Translation: BAB22419.1.
AK170346 mRNA. Translation: BAE41735.1.
CCDSiCCDS28476.1.
PIRiJN0063.
RefSeqiNP_033859.1. NM_009729.3.
UniGeneiMm.294761.
Mm.30155.
Mm.320896.

Genome annotation databases

EnsembliENSMUST00000024932; ENSMUSP00000024932; ENSMUSG00000024121.
ENSMUST00000098862; ENSMUSP00000111059; ENSMUSG00000024121.
GeneIDi11984.
KEGGimmu:11984.
UCSCiuc008aup.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64298 mRNA. Translation: AAA39775.1.
U13842 Genomic DNA. Translation: AAC52413.1.
AB059662 Genomic DNA. Translation: BAB64538.1.
AF356008 Genomic DNA. Translation: AAL02098.1.
AK002570 mRNA. Translation: BAB22195.1.
AK002871 mRNA. Translation: BAB22419.1.
AK170346 mRNA. Translation: BAE41735.1.
CCDSiCCDS28476.1.
PIRiJN0063.
RefSeqiNP_033859.1. NM_009729.3.
UniGeneiMm.294761.
Mm.30155.
Mm.320896.

3D structure databases

ProteinModelPortaliP63082.
SMRiP63082. Positions 13-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198274. 3 interactions.
IntActiP63082. 2 interactions.
MINTiMINT-1581356.
STRINGi10090.ENSMUSP00000024932.

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

iPTMnetiP63082.
PhosphoSiteiP63082.

Proteomic databases

EPDiP63082.
MaxQBiP63082.
PaxDbiP63082.
PRIDEiP63082.
TopDownProteomicsiP63082.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024932; ENSMUSP00000024932; ENSMUSG00000024121.
ENSMUST00000098862; ENSMUSP00000111059; ENSMUSG00000024121.
GeneIDi11984.
KEGGimmu:11984.
UCSCiuc008aup.2. mouse.

Organism-specific databases

CTDi527.
MGIiMGI:88116. Atp6v0c.

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00550000074873.
HOVERGENiHBG002712.
InParanoidiP63082.
KOiK02155.
OMAiVEDNDMF.
OrthoDBiEOG7FV3RW.
PhylomeDBiP63082.
TreeFamiTF300025.

Enzyme and pathway databases

ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-77387. Insulin receptor recycling.
R-MMU-917977. Transferrin endocytosis and recycling.
R-MMU-983712. Ion channel transport.

Miscellaneous databases

ChiTaRSiAtp6v0c. mouse.
PROiP63082.
SOURCEiSearch...

Gene expression databases

BgeeiP63082.
CleanExiMM_ATP6V0C.
MM_MVP.
ExpressionAtlasiP63082. baseline.
GenevisibleiP63082. MM.

Family and domain databases

HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNA encoding the 16 KDa subunit of vacuolar H(+)-ATPase from mouse cerebellum."
    Hanada H., Hasebe M., Moriyama Y., Maeda M., Futai M.
    Biochem. Biophys. Res. Commun. 176:1062-1067(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts."
    Laitala T., Howell M.L., Dean G.E., Vaananen H.K.
    Mol. Biol. Cell 7:129-142(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The murine genome contains one functional gene and two pseudogenes coding for the 16 kDa proteolipid subunit of vacuolar H+-ATPase."
    Hayami K., Noumi T., Inoue H., Sun-Wada G.H., Yoshimizu T., Kanazawa H.
    Gene 273:199-206(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Expression and localization of the mouse homolog of the yeast V-ATPase 21-kDa subunit c' (Vma16p)."
    Nishi T., Kawasaki-Nishi S., Forgac M.
    J. Biol. Chem. 276:34122-34130(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
  5. "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.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver and Lung.

Entry informationi

Entry nameiVATL_MOUSE
AccessioniPrimary (citable) accession number: P63082
Secondary accession number(s): P23967, Q3TD69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 6, 2016
This is version 117 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, 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

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 one 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.