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Protein

V-type proton ATPase 16 kDa proteolipid subunit

Gene

ATP6V0C

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Sitei139Essential for proton translocationBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-1222556 ROS, RNS production in phagocytes
R-BTA-6798695 Neutrophil degranulation
R-BTA-77387 Insulin receptor recycling
R-BTA-917977 Transferrin endocytosis and recycling
R-BTA-983712 Ion channel transport

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):
Vacuolar proton pump 16 kDa proteolipid subunit
Gene namesi
Name:ATP6V0C
Synonyms:ATP6C, ATP6L
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Organism-specific databases

VGNCiVGNC:26311 ATP6V0C

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 10LumenalSequence analysis10
Transmembranei11 – 33HelicalSequence analysisAdd BLAST23
Topological domaini34 – 55CytoplasmicSequence analysisAdd BLAST22
Transmembranei56 – 76HelicalSequence analysisAdd BLAST21
Topological domaini77 – 92LumenalSequence analysisAdd BLAST16
Transmembranei93 – 114HelicalSequence analysisAdd BLAST22
Topological domaini115 – 131CytoplasmicSequence analysisAdd BLAST17
Transmembranei132 – 152HelicalSequence analysisAdd BLAST21
Topological domaini153 – 155LumenalSequence analysis3

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000717421 – 155V-type proton ATPase 16 kDa proteolipid subunitAdd BLAST155

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiP23956

Expressioni

Gene expression databases

BgeeiENSBTAG00000026428
ExpressionAtlasiP23956 baseline and differential

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 LASS2 (By similarity). 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

CORUMiP23956
IntActiP23956, 1 interactor
MINTiP23956
STRINGi9913.ENSBTAP00000037385

Structurei

3D structure databases

ProteinModelPortaliP23956
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0232 Eukaryota
COG0636 LUCA
GeneTreeiENSGT00550000074873
HOGENOMiHOG000056520
HOVERGENiHBG002712
InParanoidiP23956
KOiK02155
OMAiDMFARGI
OrthoDBiEOG091G0U1Y
TreeFamiTF300025

Family and domain databases

InterProiView protein in InterPro
IPR002379 ATPase_proteolipid_c-like_dom
IPR000245 ATPase_proteolipid_csu
IPR011555 ATPase_proteolipid_su_C_euk
IPR035921 F/V-ATP_Csub_sf
PfamiView protein in Pfam
PF00137 ATP-synt_C, 2 hits
PRINTSiPR00122 VACATPASE
SUPFAMiSSF81333 SSF81333, 2 hits
TIGRFAMsiTIGR01100 V_ATP_synt_C, 1 hit

Sequencei

Sequence statusi: Complete.

P23956-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEAKNGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE
60 70 80 90 100
MIMKSIIPVV MAGIIAIYGL VVAVLIANSL NDGISLYRSF LQLGAGLSVG
110 120 130 140 150
LSGLAAGFAI GIVGDAGVRG TAQQPRLFVG MILILIFAEV LGLYGLIVAL

ILSTK
Length:155
Mass (Da):15,720
Last modified:March 1, 1992 - v1
Checksum:i326B20B5F7D7D607
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03835 mRNA Translation: AAA30397.1
BC102659 mRNA Translation: AAI02660.1
PIRiA31320 PXBOV6
RefSeqiNP_001017954.1, NM_001017954.1
UniGeneiBt.64839

Genome annotation databases

EnsembliENSBTAT00000037556; ENSBTAP00000037385; ENSBTAG00000026428
GeneIDi550622
KEGGibta:550622

Similar proteinsi

Entry informationi

Entry nameiVATL_BOVIN
AccessioniPrimary (citable) accession number: P23956
Secondary accession number(s): Q3SZY0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: May 23, 2018
This is version 145 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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