ID   VATC1_HUMAN             Reviewed;         382 AA.
AC   P21283;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=V-type proton ATPase subunit C 1;
DE            Short=V-ATPase subunit C 1;
DE   AltName: Full=Vacuolar proton pump subunit C 1;
GN   Name=ATP6V1C1; Synonyms=ATP6C, ATP6D, VATC;
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].
RC   TISSUE=Osteoclastoma;
RX   PubMed=8250920; DOI=10.1006/bbrc.1993.2434;
RA   van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.;
RT   "Cloning and tissue distribution of subunits C, D, and E of the human
RT   vacuolar H(+)-ATPase.";
RL   Biochem. Biophys. Res. Commun. 197:15-21(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11707601; DOI=10.1073/pnas.241525498;
RA   Tanner S.M., Austin J.L., Leone G., Rush L.J., Plass C., Heinonen K.,
RA   Mrozek K., Sill H., Knuutila S., Kolitz J.E., Archer K.J., Caligiuri M.A.,
RA   Bloomfield C.D., de La Chapelle A.;
RT   "BAALC, the human member of a novel mammalian neuroectoderm gene lineage,
RT   is implicated in hematopoiesis and acute leukemia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:13901-13906(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
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   [4]
RP   PROTEIN SEQUENCE OF 2-13; 45-60 AND 200-211, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RA   Kanor S., Bienvenut W.V., Quadroni M.;
RL   Submitted (DEC-2005) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 36-382.
RC   TISSUE=Brain;
RX   PubMed=2147024; DOI=10.1016/s0021-9258(17)30516-1;
RA   Nelson H., Mandiyan S., Noumi T., Moriyama Y., Miedel M.C., Nelson N.;
RT   "Molecular cloning of cDNA encoding the C subunit of H(+)-ATPase from
RT   bovine chromaffin granules.";
RL   J. Biol. Chem. 265:20390-20393(1990).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=12384298; DOI=10.1016/s0378-1119(02)00884-3;
RA   Smith A.N., Borthwick K.J., Karet F.E.;
RT   "Molecular cloning and characterization of novel tissue-specific isoforms
RT   of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation
RT   in autosomal recessive distal renal tubular acidosis.";
RL   Gene 297:169-177(2002).
RN   [7]
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 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: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (PubMed:33065002). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment (By similarity). Subunit C is
CC       necessary for the assembly of the catalytic sector of the enzyme and is
CC       likely to have a specific function in its catalytic activity (By
CC       similarity). {ECO:0000250|UniProtKB:P21282,
CC       ECO:0000250|UniProtKB:P31412, 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).
CC       {ECO:0000269|PubMed:33065002}.
CC   -!- INTERACTION:
CC       P21283; P62330: ARF6; NbExp=4; IntAct=EBI-988663, EBI-638181;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:Q5FVI6}; Peripheral membrane
CC       protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250|UniProtKB:Q5FVI6}; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384298}.
CC   -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR   EMBL; X69151; CAA48903.1; -; mRNA.
DR   EMBL; AF363578; AAL50383.1; -; Genomic_DNA.
DR   EMBL; BC010960; AAH10960.1; -; mRNA.
DR   EMBL; J05682; AAA36803.1; -; mRNA.
DR   CCDS; CCDS6296.1; -.
DR   PIR; JN0907; JN0907.
DR   RefSeq; NP_001686.1; NM_001695.4.
DR   PDB; 6WM2; EM; 3.10 A; O=1-382.
DR   PDB; 6WM3; EM; 3.40 A; O=1-382.
DR   PDB; 6WM4; EM; 3.60 A; O=1-382.
DR   PDB; 7U4T; EM; 3.60 A; O=1-382.
DR   PDB; 7UNF; EM; 4.08 A; C=1-382.
DR   PDBsum; 6WM2; -.
DR   PDBsum; 6WM3; -.
DR   PDBsum; 6WM4; -.
DR   PDBsum; 7U4T; -.
DR   PDBsum; 7UNF; -.
DR   AlphaFoldDB; P21283; -.
DR   EMDB; EMD-21847; -.
DR   EMDB; EMD-21848; -.
DR   EMDB; EMD-21849; -.
DR   EMDB; EMD-26334; -.
DR   EMDB; EMD-26623; -.
DR   SMR; P21283; -.
DR   BioGRID; 107011; 104.
DR   IntAct; P21283; 17.
DR   STRING; 9606.ENSP00000430282; -.
DR   DrugBank; DB01694; D-tartaric acid.
DR   DrugBank; DB09552; Thonzonium.
DR   DrugBank; DB01133; Tiludronic acid.
DR   TCDB; 3.A.2.2.4; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   GlyGen; P21283; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P21283; -.
DR   PhosphoSitePlus; P21283; -.
DR   SwissPalm; P21283; -.
DR   BioMuta; ATP6V1C1; -.
DR   DMDM; 401329; -.
DR   CPTAC; CPTAC-173; -.
DR   EPD; P21283; -.
DR   jPOST; P21283; -.
DR   MassIVE; P21283; -.
DR   MaxQB; P21283; -.
DR   PaxDb; 9606-ENSP00000379203; -.
DR   PeptideAtlas; P21283; -.
DR   ProteomicsDB; 53857; -.
DR   Pumba; P21283; -.
DR   Antibodypedia; 4022; 144 antibodies from 24 providers.
DR   DNASU; 528; -.
DR   Ensembl; ENST00000395862.7; ENSP00000379203.3; ENSG00000155097.12.
DR   Ensembl; ENST00000518738.2; ENSP00000430282.1; ENSG00000155097.12.
DR   GeneID; 528; -.
DR   KEGG; hsa:528; -.
DR   MANE-Select; ENST00000518738.2; ENSP00000430282.1; NM_001695.5; NP_001686.1.
DR   UCSC; uc003ykz.5; human.
DR   AGR; HGNC:856; -.
DR   CTD; 528; -.
DR   DisGeNET; 528; -.
DR   GeneCards; ATP6V1C1; -.
DR   HGNC; HGNC:856; ATP6V1C1.
DR   HPA; ENSG00000155097; Low tissue specificity.
DR   MIM; 603097; gene.
DR   neXtProt; NX_P21283; -.
DR   OpenTargets; ENSG00000155097; -.
DR   PharmGKB; PA25156; -.
DR   VEuPathDB; HostDB:ENSG00000155097; -.
DR   eggNOG; KOG2909; Eukaryota.
DR   GeneTree; ENSGT00390000004263; -.
DR   InParanoid; P21283; -.
DR   OMA; VMIWIHV; -.
DR   OrthoDB; 166742at2759; -.
DR   PhylomeDB; P21283; -.
DR   TreeFam; TF314912; -.
DR   BioCyc; MetaCyc:HS08030-MONOMER; -.
DR   PathwayCommons; P21283; -.
DR   Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
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; P21283; -.
DR   BioGRID-ORCS; 528; 631 hits in 1182 CRISPR screens.
DR   ChiTaRS; ATP6V1C1; human.
DR   GeneWiki; ATP6V1C1; -.
DR   GenomeRNAi; 528; -.
DR   Pharos; P21283; Tbio.
DR   PRO; PR:P21283; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P21283; Protein.
DR   Bgee; ENSG00000155097; Expressed in sperm and 207 other cell types or tissues.
DR   ExpressionAtlas; P21283; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016469; C:proton-transporting two-sector ATPase complex; TAS:ProtInc.
DR   GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:1902600; P:proton transmembrane transport; TAS:ProtInc.
DR   GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl.
DR   CDD; cd14785; V-ATPase_C; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 1.20.1460.10; subunit c (vma5p) of the yeast v-atpase, domain 2; 1.
DR   InterPro; IPR004907; ATPase_V1-cplx_csu.
DR   InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR   PANTHER; PTHR10137; V-TYPE PROTON ATPASE SUBUNIT C; 1.
DR   PANTHER; PTHR10137:SF5; V-TYPE PROTON ATPASE SUBUNIT C 1; 1.
DR   Pfam; PF03223; V-ATPase_C; 1.
DR   SUPFAM; SSF118203; Vacuolar ATP synthase subunit C; 1.
DR   Genevisible; P21283; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasmic vesicle; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Synapse; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:25944712"
FT   CHAIN           2..382
FT                   /note="V-type proton ATPase subunit C 1"
FT                   /id="PRO_0000209348"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:25944712"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   TURN            24..26
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   TURN            28..32
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           48..79
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           98..103
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           118..156
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          180..190
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   TURN            191..193
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           194..200
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          214..218
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          220..230
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           234..243
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           255..309
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          317..322
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   HELIX           328..339
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:6WM2"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:6WM3"
FT   STRAND          359..361
FT                   /evidence="ECO:0007829|PDB:6WM3"
FT   STRAND          368..374
FT                   /evidence="ECO:0007829|PDB:6WM2"
SQ   SEQUENCE   382 AA;  43942 MW;  5626E2AB2BD66BA7 CRC64;
     MTEFWLISAP GEKTCQQTWE KLHAATSKNN NLAVTSKFNI PDLKVGTLDV LVGLSDELAK
     LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLANGVDLVT YITRFQWDMA KYPIKQSLKN
     ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL QNLERKNAGS LLTRSLAEIV KKDDFVLDSE
     YLVTLLVVVP KLNHNDWIKQ YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK
     ARENKFIVRD FQYNEEEMKA DKEEMNRLST DKKKQFGPLV RWLKVNFSEA FIAWIHVKAL
     RVFVESVLRY GLPVNFQAML LQPNKKTLKK LREVLHELYK HLDSSAAAII DAPMDIPGLN
     LSQQEYYPYV YYKIDCNLLE FK
//