VATC2_MOUSE
ID VATC2_MOUSE Reviewed; 427 AA.
AC Q99L60; Q6PHA4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
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; Synonyms=Atp6c2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RX PubMed=12527205; DOI=10.1016/s0378-1119(02)01099-5;
RA Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.;
RT "Diversity of mouse proton-translocating ATPase: presence of multiple
RT isoforms of the C, d and G subunits.";
RL Gene 302:147-153(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
RX PubMed=12947086; DOI=10.1074/jbc.m307197200;
RA Sun-Wada G.H., Murata Y., Namba M., Yamamoto A., Wada Y., Futai M.;
RT "Mouse proton pump ATPase C subunit isoforms (C2-a and C2-b) specifically
RT expressed in kidney and lung.";
RL J. Biol. Chem. 278:44843-44851(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=C2-a;
CC IsoId=Q99L60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99L60-2; Sequence=VSP_024884;
CC Name=3; Synonyms=C2-b;
CC IsoId=Q99L60-3; Sequence=VSP_024885;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the lung and kidney.
CC Isoform 1 is lung-specific while isoform 3 is a kidney-specific
CC isoform. Isoform 1 is localized in the lamellar bodies of type II
CC alveolar cells. Isoform 2 is strongly expressed in the cortical and
CC medulla collecting ducts and is found in the plasma membranes of renal
CC alpha and beta intercalated cells. {ECO:0000269|PubMed:12527205,
CC ECO:0000269|PubMed:12947086}.
CC -!- DEVELOPMENTAL STAGE: Significant expression seen at 17 dpc and not
CC earlier. {ECO:0000269|PubMed:12527205}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR EMBL; AB088357; BAC57950.1; -; mRNA.
DR EMBL; BC003810; AAH03810.1; -; mRNA.
DR EMBL; BC056636; AAH56636.1; -; mRNA.
DR CCDS; CCDS25827.1; -. [Q99L60-1]
DR CCDS; CCDS49034.1; -. [Q99L60-2]
DR RefSeq; NP_001153104.1; NM_001159632.1. [Q99L60-2]
DR RefSeq; NP_598460.1; NM_133699.2. [Q99L60-1]
DR RefSeq; XP_006515259.1; XM_006515196.3. [Q99L60-2]
DR RefSeq; XP_006515262.1; XM_006515199.3. [Q99L60-3]
DR AlphaFoldDB; Q99L60; -.
DR SMR; Q99L60; -.
DR BioGRID; 213044; 1.
DR STRING; 10090.ENSMUSP00000020884; -.
DR TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; Q99L60; -.
DR PhosphoSitePlus; Q99L60; -.
DR jPOST; Q99L60; -.
DR MaxQB; Q99L60; -.
DR PaxDb; Q99L60; -.
DR PRIDE; Q99L60; -.
DR ProteomicsDB; 297536; -. [Q99L60-1]
DR ProteomicsDB; 297537; -. [Q99L60-2]
DR ProteomicsDB; 297538; -. [Q99L60-3]
DR Antibodypedia; 26729; 313 antibodies from 30 providers.
DR DNASU; 68775; -.
DR Ensembl; ENSMUST00000020884; ENSMUSP00000020884; ENSMUSG00000020566. [Q99L60-2]
DR Ensembl; ENSMUST00000095820; ENSMUSP00000093500; ENSMUSG00000020566. [Q99L60-1]
DR Ensembl; ENSMUST00000221129; ENSMUSP00000152515; ENSMUSG00000020566. [Q99L60-3]
DR GeneID; 68775; -.
DR KEGG; mmu:68775; -.
DR UCSC; uc007ncq.1; mouse. [Q99L60-1]
DR UCSC; uc007ncs.2; mouse. [Q99L60-2]
DR CTD; 245973; -.
DR MGI; MGI:1916025; Atp6v1c2.
DR VEuPathDB; HostDB:ENSMUSG00000020566; -.
DR eggNOG; KOG2909; Eukaryota.
DR GeneTree; ENSGT00390000004263; -.
DR InParanoid; Q99L60; -.
DR OMA; VDTLAKX; -.
DR OrthoDB; 1016088at2759; -.
DR PhylomeDB; Q99L60; -.
DR TreeFam; TF314912; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-77387; Insulin receptor recycling.
DR Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR Reactome; R-MMU-983712; Ion channel transport.
DR BioGRID-ORCS; 68775; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Atp6v1c2; mouse.
DR PRO; PR:Q99L60; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q99L60; protein.
DR Bgee; ENSMUSG00000020566; Expressed in prostate gland ventral lobe and 62 other tissues.
DR ExpressionAtlas; Q99L60; baseline and differential.
DR Genevisible; Q99L60; MM.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IDA:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:MGI.
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_0000285670"
FT REGION 298..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 95
FT /note="V -> GLKEKMKCLKI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024884"
FT VAR_SEQ 276..321
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12527205,
FT ECO:0000303|PubMed:12947086"
FT /id="VSP_024885"
FT CONFLICT 125
FT /note="A -> T (in Ref. 3; AAH56636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 48350 MW; 5D7146D9BC7F03F7 CRC64;
MSEFWLISAP GDKENLQALE RMNNVTSKSN LSHNTKFAIP DFKVGTLDSL VGLSDELGKL
DTFAESLIKR MAQSVVEVME DSKGKAHETL LANGVDLTSF VTHFEWDMAK YPAKQPLVSV
VDTLAKQLAQ IETDLKSRTA AYSVLKANLE NLEKRSTGNL FTRTLSDIVS KEDFVLDSEY
LITLLVIVPK SSFAQWQKTY ESLSDMVVPR STKLIAEDNE GGLFTVTLFR KVIEDFKVKA
KENKFIVREF YYDEKEIKRE REEMTRLLSD KKQQYPTSCV ALKKGSATYR DHKVKVAPLG
NPARPAAGQT DRDRESEGEG EGPLLRWLKV NFSEAFIAWI HIKALRVFVE SVLRYGLPVN
FQAVLLQPHK KSATKRLREV LNSVFRHLDE VAAASILDAS VEIPGLQLSN QDYFPYVYFH
IDLSLLD
