VATC2_RAT
ID VATC2_RAT Reviewed; 425 AA.
AC Q6AYE4; Q53B80;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=16283434; DOI=10.1007/s11373-005-9020-3;
RA Feng N.-H., Lin H.-I., Wang J.-S., Chou S.-T., Ma H.-K., Rooney S.A.,
RA Lu J.-F.;
RT "Differential expression of a V-type ATPase C subunit gene, Atp6v1c2,
RT during culture of rat lung type II pneumocytes.";
RL J. Biomed. Sci. 12:899-911(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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. V-ATPase is responsible for acidifying and maintaining the pH
CC of intracellular compartments and in some cell types, is targeted to
CC the plasma membrane, where it is responsible for acidifying the
CC extracellular environment (By similarity). Subunit C is necessary for
CC the assembly of the catalytic sector of the enzyme and is likely to
CC have a specific function in its catalytic activity (By similarity).
CC {ECO:0000250|UniProtKB:P31412, ECO:0000250|UniProtKB:Q5FVI6}.
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:Q5FVI6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=C2-a;
CC IsoId=Q6AYE4-1; Sequence=Displayed;
CC Name=2; Synonyms=C2-b;
CC IsoId=Q6AYE4-2; Sequence=VSP_024886;
CC -!- TISSUE SPECIFICITY: Lung, kidney and testis. Expressed in both
CC bronchiolar and alveolar lung epithelial cells. Isoform 1 is
CC predominantly expressed in the lung while isoform 2 is strongly
CC expressed in the kidney and testis. {ECO:0000269|PubMed:16283434}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR EMBL; AY594319; AAT44904.1; -; mRNA.
DR EMBL; BC079083; AAH79083.1; -; mRNA.
DR RefSeq; NP_001014221.1; NM_001014199.1. [Q6AYE4-1]
DR AlphaFoldDB; Q6AYE4; -.
DR SMR; Q6AYE4; -.
DR STRING; 10116.ENSRNOP00000066981; -.
DR PRIDE; Q6AYE4; -.
DR Ensembl; ENSRNOT00000071977; ENSRNOP00000066981; ENSRNOG00000050553. [Q6AYE4-1]
DR Ensembl; ENSRNOT00000099858; ENSRNOP00000093823; ENSRNOG00000050553. [Q6AYE4-2]
DR GeneID; 362802; -.
DR KEGG; rno:362802; -.
DR CTD; 245973; -.
DR RGD; 1359430; Atp6v1c2.
DR GeneTree; ENSGT00390000004263; -.
DR InParanoid; Q6AYE4; -.
DR OrthoDB; 1016088at2759; -.
DR PhylomeDB; Q6AYE4; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-77387; Insulin receptor recycling.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR Reactome; R-RNO-983712; Ion channel transport.
DR PRO; PR:Q6AYE4; -.
DR Proteomes; UP000002494; Chromosome 6.
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:RGD.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISO:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; Hydrogen ion transport; Ion transport;
KW Reference proteome; Transport.
FT CHAIN 1..425
FT /note="V-type proton ATPase subunit C 2"
FT /id="PRO_0000285671"
FT REGION 295..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 276..319
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16283434"
FT /id="VSP_024886"
FT CONFLICT 49
FT /note="S -> P (in Ref. 1; AAT44904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 48243 MW; 698606392087372D CRC64;
MSEFWLISAP GDKENLQALE RMNSVTSKSN LSHNTKFAIP DFKVGTLDSL VGLSDELGKL
DTFAESLIKR MAQSVVEVME DSKGKVHENL LANGVDLTSF VTHFEWDMAK YPAKQPLVSV
VDTLAKQLAQ IETDLKSRTA AYSVLKANLE NLEKKSTGNL FTRTLSDIVS KEDFVLDSEY
LITLLVIVPK SSYVQWQKTY ESLSDMVVPR STKLIAEDNE GGLFTVTLFR KVIEDFKVKA
KENKFIVREF YYDEKEIKRE REEMTRLLSD KKQQYQTSCV ALKKGSATYR DHKVKVTPLG
NPTRPTAGQN DRESEGEGEG PLLRWLKVNF SEAFIAWIHI KALRVFVESV LRYGLPVNFQ
AVLLQPHKKS ATKRLREVLN SVFRHLDEVA AASILDASVE IPGLQLSNQD YFPYVYFHID
LSLLD
