ID   VATL_HUMAN              Reviewed;         155 AA.
AC   P27449; Q6FH26;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE            Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE   AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN   Name=ATP6V0C; Synonyms=ATP6C, ATP6L, ATPL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1709739; DOI=10.1073/pnas.88.10.4289;
RA   Gillespie G.A.J., Somlo S., Germino G.G., Weinstat-Saslow D., Reeders S.T.;
RT   "CpG island in the region of an autosomal dominant polycystic kidney
RT   disease locus defines the 5' end of a gene encoding a putative proton
RT   channel.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:4289-4293(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Muscle, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-155.
RX   PubMed=1532310; DOI=10.1016/0006-291x(92)90562-y;
RA   Hasebe M., Hanada H., Moriyama Y., Maeda M., Futai M.;
RT   "Vacuolar type H(+)-ATPase genes: presence of four genes including
RT   pseudogenes for the 16-kDa proteolipid subunit in the human genome.";
RL   Biochem. Biophys. Res. Commun. 183:856-863(1992).
RN   [6]
RP   INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
RX   PubMed=7636472; DOI=10.1099/0022-1317-76-8-1909;
RA   Koralnik I.J., Mulloy J.C., Andresson T., Fullen J., Franchini G.;
RT   "Mapping of the intermolecular association of human T cell
RT   leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16 kDa
RT   subunit protein.";
RL   J. Gen. Virol. 76:1909-1916(1995).
RN   [7]
RP   INTERACTION WITH LASS2.
RX   PubMed=11543633; DOI=10.1006/geno.2001.6614;
RA   Pan H., Qin W.-X., Huo K.-K., Wan D.-F., Yu Y., Xu Z.-G., Hu Q.-D.,
RA   Gu K.T., Zhou X.-M., Jiang H.-Q., Zhang P.-P., Huang Y., Li Y.-Y.,
RA   Gu J.-R.;
RT   "Cloning, mapping, and characterization of a human homologue of the yeast
RT   longevity assurance gene LAG1.";
RL   Genomics 77:58-64(2001).
RN   [8]
RP   INTERACTION WITH RNF182, AND UBIQUITINATION.
RX   PubMed=18298843; DOI=10.1186/1750-1326-3-4;
RA   Liu Q.Y., Lei J.X., Sikorska M., Liu R.;
RT   "A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the
RT   brains of Alzheimer's patients and targets ATP6V0C for degradation.";
RL   Mol. Neurodegener. 3:4-4(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [11] {ECO:0007744|PDB:6WLW, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, AND
RP   IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX   PubMed=33065002; DOI=10.1016/j.molcel.2020.09.029;
RA   Wang L., Wu D., Robinson C.V., Wu H., Fu T.M.;
RT   "Structures of a Complete Human V-ATPase Reveal Mechanisms of Its
RT   Assembly.";
RL   Mol. Cell 80:501-511.e3(2020).
CC   -!- FUNCTION: Proton-conducting pore forming subunit of the V0 complex of
CC       vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC       peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC       complex (V0) that translocates protons (PubMed:33065002). V-ATPase is
CC       responsible for acidifying and maintaining the pH of intracellular
CC       compartments and in some cell types, is targeted to the plasma
CC       membrane, where it is responsible for acidifying the extracellular
CC       environment (By similarity). {ECO:0000250|UniProtKB:P23956,
CC       ECO:0000269|PubMed:33065002}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (PubMed:33065002). The V1 complex consists of three
CC       catalytic AB heterodimers that form a heterohexamer, three peripheral
CC       stalks each consisting of EG heterodimers, one central rotor including
CC       subunits D and F, and the regulatory subunits C and H
CC       (PubMed:33065002). The proton translocation complex V0 consists of the
CC       proton transport subunit a, a ring of proteolipid subunits c9c'',
CC       rotary subunit d, subunits e and f, and the accessory subunits
CC       ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002). Interacts with the V0
CC       complex V-ATPase subunit a4 ATP6V0A4 (By similarity). Interacts with
CC       LASS2 (PubMed:11543633). Interacts with RNF182; this interaction leads
CC       to ubiquitination and degradation via the proteasome pathway
CC       (PubMed:18298843). {ECO:0000250|UniProtKB:P63082,
CC       ECO:0000269|PubMed:11543633, ECO:0000269|PubMed:18298843,
CC       ECO:0000269|PubMed:33065002}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory protein
CC       p12I. {ECO:0000269|PubMed:7636472}.
CC   -!- INTERACTION:
CC       P27449; Q13520: AQP6; NbExp=3; IntAct=EBI-721179, EBI-13059134;
CC       P27449; P07307-3: ASGR2; NbExp=3; IntAct=EBI-721179, EBI-12808270;
CC       P27449; P19397: CD53; NbExp=3; IntAct=EBI-721179, EBI-6657396;
CC       P27449; Q07108: CD69; NbExp=3; IntAct=EBI-721179, EBI-2836595;
CC       P27449; P11912: CD79A; NbExp=3; IntAct=EBI-721179, EBI-7797864;
CC       P27449; Q96G23: CERS2; NbExp=3; IntAct=EBI-721179, EBI-1057080;
CC       P27449; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-721179, EBI-17710733;
CC       P27449; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-721179, EBI-11977093;
CC       P27449; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-721179, EBI-11749983;
CC       P27449; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-721179, EBI-18013275;
CC       P27449; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-721179, EBI-517508;
CC       P27449; Q96KC8: DNAJC1; NbExp=3; IntAct=EBI-721179, EBI-296550;
CC       P27449; Q92838: EDA; NbExp=4; IntAct=EBI-721179, EBI-529425;
CC       P27449; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-721179, EBI-526033;
CC       P27449; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-721179, EBI-781551;
CC       P27449; P84090: ERH; NbExp=3; IntAct=EBI-721179, EBI-711389;
CC       P27449; P22794: EVI2A; NbExp=3; IntAct=EBI-721179, EBI-2870359;
CC       P27449; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-721179, EBI-18938272;
CC       P27449; O15552: FFAR2; NbExp=3; IntAct=EBI-721179, EBI-2833872;
CC       P27449; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-721179, EBI-12142257;
CC       P27449; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-721179, EBI-13345167;
CC       P27449; O00155: GPR25; NbExp=3; IntAct=EBI-721179, EBI-10178951;
CC       P27449; O15529: GPR42; NbExp=3; IntAct=EBI-721179, EBI-18076404;
CC       P27449; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-721179, EBI-18053395;
CC       P27449; Q13651: IL10RA; NbExp=3; IntAct=EBI-721179, EBI-1031656;
CC       P27449; P16871: IL7R; NbExp=3; IntAct=EBI-721179, EBI-80490;
CC       P27449; Q92876: KLK6; NbExp=3; IntAct=EBI-721179, EBI-2432309;
CC       P27449; P26715: KLRC1; NbExp=3; IntAct=EBI-721179, EBI-9018187;
CC       P27449; Q8N386: LRRC25; NbExp=3; IntAct=EBI-721179, EBI-11304917;
CC       P27449; Q8IX19: MCEMP1; NbExp=5; IntAct=EBI-721179, EBI-2816356;
CC       P27449; P21757: MSR1; NbExp=6; IntAct=EBI-721179, EBI-1776976;
CC       P27449; Q6P499: NIPAL3; NbExp=3; IntAct=EBI-721179, EBI-10252783;
CC       P27449; P35372-10: OPRM1; NbExp=3; IntAct=EBI-721179, EBI-12807478;
CC       P27449; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-721179, EBI-16427978;
CC       P27449; Q6UXB8: PI16; NbExp=3; IntAct=EBI-721179, EBI-12810028;
CC       P27449; P25788: PSMA3; NbExp=3; IntAct=EBI-721179, EBI-348380;
CC       P27449; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-721179, EBI-7545592;
CC       P27449; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-721179, EBI-10192441;
CC       P27449; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-721179, EBI-17247926;
CC       P27449; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-721179, EBI-13389236;
CC       P27449; P30825: SLC7A1; NbExp=3; IntAct=EBI-721179, EBI-4289564;
CC       P27449; Q9BZL3: SMIM3; NbExp=6; IntAct=EBI-721179, EBI-741850;
CC       P27449; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-721179, EBI-17498703;
CC       P27449; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-721179, EBI-17280858;
CC       P27449; P27105: STOM; NbExp=3; IntAct=EBI-721179, EBI-1211440;
CC       P27449; Q96L08: SUSD3; NbExp=3; IntAct=EBI-721179, EBI-18194029;
CC       P27449; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-721179, EBI-7238458;
CC       P27449; Q9P0T7: TMEM9; NbExp=3; IntAct=EBI-721179, EBI-723976;
CC       P27449; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-721179, EBI-744988;
CC       P27449; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-721179, EBI-748373;
CC       P27449; P0CK45: E5; Xeno; NbExp=2; IntAct=EBI-721179, EBI-7015490;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC       membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Ubiquitinated by RNF182, leading to its degradation via the
CC       ubiquitin-proteasome pathway. {ECO:0000269|PubMed:18298843}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; M62762; AAA60039.1; -; mRNA.
DR   EMBL; CR541930; CAG46728.1; -; mRNA.
DR   EMBL; CR541951; CAG46749.1; -; mRNA.
DR   EMBL; BT007155; AAP35819.1; -; mRNA.
DR   EMBL; BC004537; AAH04537.1; -; mRNA.
DR   EMBL; BC007389; AAH07389.1; -; mRNA.
DR   EMBL; BC007759; AAH07759.1; -; mRNA.
DR   EMBL; BC009290; AAH09290.1; -; mRNA.
DR   CCDS; CCDS10470.1; -.
DR   PIR; A39367; A39367.
DR   RefSeq; NP_001185498.1; NM_001198569.1.
DR   RefSeq; NP_001685.1; NM_001694.3.
DR   PDB; 6WLW; EM; 3.00 A; 1/2/3/4/5/6/7/8/9=1-155.
DR   PDB; 6WM2; EM; 3.10 A; 1/2/3/4/5/6/7/8/9=1-155.
DR   PDB; 6WM3; EM; 3.40 A; 1/2/3/4/5/6/7/8/9=1-155.
DR   PDB; 6WM4; EM; 3.60 A; 1/2/3/4/5/6/7/8/9=1-155.
DR   PDB; 7U4T; EM; 3.60 A; 1/2/3/4/5/6/7/8/9=1-155.
DR   PDB; 7UNF; EM; 4.08 A; 0/2/3/4/5/6/7/8/9=1-155.
DR   PDBsum; 6WLW; -.
DR   PDBsum; 6WM2; -.
DR   PDBsum; 6WM3; -.
DR   PDBsum; 6WM4; -.
DR   PDBsum; 7U4T; -.
DR   PDBsum; 7UNF; -.
DR   AlphaFoldDB; P27449; -.
DR   EMDB; EMD-21844; -.
DR   EMDB; EMD-21847; -.
DR   EMDB; EMD-21848; -.
DR   EMDB; EMD-21849; -.
DR   EMDB; EMD-26334; -.
DR   EMDB; EMD-26623; -.
DR   SMR; P27449; -.
DR   BioGRID; 107010; 148.
DR   ComplexPortal; CPX-2470; Vacuolar proton translocating ATPase complex, ATP6V0A1 variant.
DR   ComplexPortal; CPX-6904; Vacuolar proton translocating ATPase complex, ATP6V0A2 variant.
DR   ComplexPortal; CPX-6905; Vacuolar proton translocating ATPase complex, ATP6V0A3 variant.
DR   ComplexPortal; CPX-6912; Vacuolar proton translocating ATPase complex, ATP6V0A4 variant.
DR   CORUM; P27449; -.
DR   IntAct; P27449; 76.
DR   MINT; P27449; -.
DR   STRING; 9606.ENSP00000329757; -.
DR   DrugBank; DB01133; Tiludronic acid.
DR   iPTMnet; P27449; -.
DR   PhosphoSitePlus; P27449; -.
DR   BioMuta; ATP6V0C; -.
DR   DMDM; 137479; -.
DR   EPD; P27449; -.
DR   jPOST; P27449; -.
DR   MassIVE; P27449; -.
DR   MaxQB; P27449; -.
DR   PaxDb; 9606-ENSP00000329757; -.
DR   PeptideAtlas; P27449; -.
DR   ProteomicsDB; 54393; -.
DR   Pumba; P27449; -.
DR   TopDownProteomics; P27449; -.
DR   Antibodypedia; 23806; 90 antibodies from 19 providers.
DR   DNASU; 527; -.
DR   Ensembl; ENST00000330398.9; ENSP00000329757.4; ENSG00000185883.12.
DR   GeneID; 527; -.
DR   KEGG; hsa:527; -.
DR   MANE-Select; ENST00000330398.9; ENSP00000329757.4; NM_001694.4; NP_001685.1.
DR   UCSC; uc002cqn.4; human.
DR   AGR; HGNC:855; -.
DR   CTD; 527; -.
DR   DisGeNET; 527; -.
DR   GeneCards; ATP6V0C; -.
DR   HGNC; HGNC:855; ATP6V0C.
DR   HPA; ENSG00000185883; Low tissue specificity.
DR   MalaCards; ATP6V0C; -.
DR   MIM; 108745; gene.
DR   neXtProt; NX_P27449; -.
DR   OpenTargets; ENSG00000185883; -.
DR   PharmGKB; PA25149; -.
DR   VEuPathDB; HostDB:ENSG00000185883; -.
DR   eggNOG; KOG0232; Eukaryota.
DR   GeneTree; ENSGT00550000074873; -.
DR   HOGENOM; CLU_085752_1_2_1; -.
DR   InParanoid; P27449; -.
DR   OMA; CAMGVLR; -.
DR   OrthoDB; 168305at2759; -.
DR   PhylomeDB; P27449; -.
DR   TreeFam; TF300025; -.
DR   BioCyc; MetaCyc:MONOMER66-34368; -.
DR   PathwayCommons; P27449; -.
DR   Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-77387; Insulin receptor recycling.
DR   Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-HSA-983712; Ion channel transport.
DR   SignaLink; P27449; -.
DR   SIGNOR; P27449; -.
DR   BioGRID-ORCS; 527; 866 hits in 1175 CRISPR screens.
DR   ChiTaRS; ATP6V0C; human.
DR   GeneWiki; ATP6V0C; -.
DR   GenomeRNAi; 527; -.
DR   Pharos; P27449; Tbio.
DR   PRO; PR:P27449; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P27449; Protein.
DR   Bgee; ENSG00000185883; Expressed in superior frontal gyrus and 95 other cell types or tissues.
DR   ExpressionAtlas; P27449; baseline and differential.
DR   GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; NAS:ComplexPortal.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; NAS:ComplexPortal.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR   GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; TAS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:ProtInc.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0048388; P:endosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0051452; P:intracellular pH reduction; NAS:ComplexPortal.
DR   GO; GO:0007042; P:lysosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; TAS:ProtInc.
DR   GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0007035; P:vacuolar acidification; NAS:ComplexPortal.
DR   CDD; cd18175; ATP-synt_Vo_c_ATP6C_rpt1; 1.
DR   CDD; cd18176; ATP-synt_Vo_c_ATP6C_rpt2; 1.
DR   Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR000245; ATPase_proteolipid_csu.
DR   InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   NCBIfam; TIGR01100; V_ATP_synt_C; 1.
DR   PANTHER; PTHR10263:SF5; V-TYPE PROTON ATPASE 16 KDA PROTEOLIPID SUBUNIT C; 1.
DR   PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
DR   Genevisible; P27449; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasmic vesicle; Host-virus interaction;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Synapse; Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..155
FT                   /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT                   /id="PRO_0000071743"
FT   TOPO_DOM        1..10
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..92
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..155
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   SITE            139
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250|UniProtKB:P63081"
FT   HELIX           9..12
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           13..45
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           57..76
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           86..123
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           128..137
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           140..152
FT                   /evidence="ECO:0007829|PDB:6WLW"
SQ   SEQUENCE   155 AA;  15736 MW;  91141854A0492A5B CRC64;
     MSESKSGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE QIMKSIIPVV
     MAGIIAIYGL VVAVLIANSL NDDISLYKSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
     TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
//