VATC1_HUMAN
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 03-AUG-2022, entry version 197.
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 PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR AlphaFoldDB; P21283; -.
DR SMR; P21283; -.
DR BioGRID; 107011; 88.
DR IntAct; P21283; 17.
DR STRING; 9606.ENSP00000379203; -.
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 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; P21283; -.
DR PeptideAtlas; P21283; -.
DR PRIDE; P21283; -.
DR ProteomicsDB; 53857; -.
DR Antibodypedia; 4022; 124 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 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; GEYWLIS; -.
DR OrthoDB; 1016088at2759; -.
DR PhylomeDB; P21283; -.
DR TreeFam; TF314912; -.
DR BioCyc; MetaCyc:HS08030-MON; -.
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; 604 hits in 1093 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 205 other tissues.
DR ExpressionAtlas; P21283; baseline and differential.
DR Genevisible; P21283; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
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 CDD; cd14785; V-ATPase_C; 1.
DR InterPro; IPR004907; ATPase_V1-cplx_csu.
DR InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 1.
DR SUPFAM; SSF118203; SSF118203; 1.
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
