VATC2_HUMAN
ID VATC2_HUMAN Reviewed; 427 AA.
AC Q8NEY4; Q96EL8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=V-type proton ATPase subunit C 2;
DE Short=V-ATPase subunit C 2;
DE AltName: Full=Vacuolar proton pump subunit C 2;
GN Name=ATP6V1C2;
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] (ISOFORM 2), ALTERNATIVE SPLICING, AND TISSUE
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASP-143.
RC TISSUE=Eye;
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).
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 (By similarity). 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:P21283, ECO:0000250|UniProtKB:P31412}.
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. The V1 complex consists of three catalytic AB heterodimers
CC that form a heterohexamer, three peripheral stalks each consisting of
CC EG heterodimers, one central rotor including subunits D and F, and the
CC regulatory subunits C and H. The proton translocation complex V0
CC consists of the proton transport subunit a, a ring of proteolipid
CC subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC subunits ATP6AP1/Ac45 and ATP6AP2/PRR. {ECO:0000250|UniProtKB:P21283}.
CC -!- INTERACTION:
CC Q8NEY4-2; Q08379: GOLGA2; NbExp=6; IntAct=EBI-10270867, EBI-618309;
CC Q8NEY4-2; Q6TFL4: KLHL24; NbExp=3; IntAct=EBI-10270867, EBI-2510117;
CC Q8NEY4-2; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-10270867, EBI-10176379;
CC Q8NEY4-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10270867, EBI-16439278;
CC Q8NEY4-2; P26367: PAX6; NbExp=3; IntAct=EBI-10270867, EBI-747278;
CC Q8NEY4-2; Q04864-2: REL; NbExp=3; IntAct=EBI-10270867, EBI-10829018;
CC Q8NEY4-2; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-10270867, EBI-12037215;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NEY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEY4-2; Sequence=VSP_024883;
CC -!- TISSUE SPECIFICITY: Kidney and placenta. {ECO:0000269|PubMed:12384298}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY24069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY039759; AAK83464.1; -; mRNA.
DR EMBL; AC092687; AAY24069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC012142; AAH12142.1; -; mRNA.
DR CCDS; CCDS1674.1; -. [Q8NEY4-2]
DR CCDS; CCDS42653.1; -. [Q8NEY4-1]
DR RefSeq; NP_001034451.1; NM_001039362.1. [Q8NEY4-1]
DR RefSeq; NP_653184.2; NM_144583.3. [Q8NEY4-2]
DR RefSeq; XP_016859234.1; XM_017003745.1. [Q8NEY4-1]
DR AlphaFoldDB; Q8NEY4; -.
DR SMR; Q8NEY4; -.
DR BioGRID; 128859; 50.
DR IntAct; Q8NEY4; 30.
DR MINT; Q8NEY4; -.
DR STRING; 9606.ENSP00000272238; -.
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; Q8NEY4; -.
DR PhosphoSitePlus; Q8NEY4; -.
DR BioMuta; ATP6V1C2; -.
DR DMDM; 146325814; -.
DR EPD; Q8NEY4; -.
DR jPOST; Q8NEY4; -.
DR MassIVE; Q8NEY4; -.
DR MaxQB; Q8NEY4; -.
DR PaxDb; Q8NEY4; -.
DR PeptideAtlas; Q8NEY4; -.
DR PRIDE; Q8NEY4; -.
DR ProteomicsDB; 73238; -. [Q8NEY4-1]
DR ProteomicsDB; 73239; -. [Q8NEY4-2]
DR Antibodypedia; 26729; 313 antibodies from 30 providers.
DR DNASU; 245973; -.
DR Ensembl; ENST00000272238.9; ENSP00000272238.4; ENSG00000143882.12. [Q8NEY4-1]
DR Ensembl; ENST00000381661.3; ENSP00000371077.3; ENSG00000143882.12. [Q8NEY4-2]
DR GeneID; 245973; -.
DR KEGG; hsa:245973; -.
DR MANE-Select; ENST00000272238.9; ENSP00000272238.4; NM_001039362.2; NP_001034451.1.
DR UCSC; uc002ras.4; human. [Q8NEY4-1]
DR CTD; 245973; -.
DR DisGeNET; 245973; -.
DR GeneCards; ATP6V1C2; -.
DR HGNC; HGNC:18264; ATP6V1C2.
DR HPA; ENSG00000143882; Tissue enhanced (epididymis, salivary gland, skin).
DR MIM; 618070; gene.
DR neXtProt; NX_Q8NEY4; -.
DR OpenTargets; ENSG00000143882; -.
DR PharmGKB; PA38514; -.
DR VEuPathDB; HostDB:ENSG00000143882; -.
DR eggNOG; KOG2909; Eukaryota.
DR GeneTree; ENSGT00390000004263; -.
DR HOGENOM; CLU_017554_3_0_1; -.
DR InParanoid; Q8NEY4; -.
DR OMA; VDTLAKX; -.
DR OrthoDB; 1099604at2759; -.
DR PhylomeDB; Q8NEY4; -.
DR TreeFam; TF314912; -.
DR BioCyc; MetaCyc:HS07123-MON; -.
DR PathwayCommons; Q8NEY4; -.
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; Q8NEY4; -.
DR BioGRID-ORCS; 245973; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; ATP6V1C2; human.
DR GeneWiki; ATP6V1C2; -.
DR GenomeRNAi; 245973; -.
DR Pharos; Q8NEY4; Tbio.
DR PRO; PR:Q8NEY4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NEY4; protein.
DR Bgee; ENSG00000143882; Expressed in skin of abdomen and 116 other tissues.
DR ExpressionAtlas; Q8NEY4; baseline and differential.
DR Genevisible; Q8NEY4; HS.
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:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
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; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrogen ion transport; Ion transport;
KW Reference proteome; Transport.
FT CHAIN 1..427
FT /note="V-type proton ATPase subunit C 2"
FT /id="PRO_0000285669"
FT REGION 292..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 276..321
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12384298,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024883"
FT VARIANT 143
FT /note="N -> D (in dbSNP:rs1198849)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032041"
SQ SEQUENCE 427 AA; 48759 MW; 7ED699EDD49CBC96 CRC64;
MSEFWLISAP GDKENLQALE RMNTVTSKSN LSYNTKFAIP DFKVGTLDSL VGLSDELGKL
DTFAESLIRR MAQSVVEVME DSKGKVQEHL LANGVDLTSF VTHFEWDMAK YPVKQPLVSV
VDTIAKQLAQ IEMDLKSRTA AYNTLKTNLE NLEKKSMGNL FTRTLSDIVS KEDFVLDSEY
LVTLLVIVPK PNYSQWQKTY ESLSDMVVPR STKLITEDKE GGLFTVTLFR KVIEDFKTKA
KENKFTVREF YYDEKEIERE REEMARLLSD KKQQYQTSCV ALKKGSSTFP DHKVKVTPLG
NPDRPAAGQT DRERESEGEG EGPLLRWLKV NFSEAFIAWI HIKALRVFVE SVLRYGLPVN
FQAVLLQPHK KSSTKRLREV LNSVFRHLDE VAATSILDAS VEIPGLQLNN QDYFPYVYFH
IDLSLLD
