ID   VATC_MANSE              Reviewed;         385 AA.
AC   Q9U5N1;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=V-type proton ATPase subunit C;
DE            Short=V-ATPase subunit C;
DE   AltName: Full=Vacuolar proton pump subunit C;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=11030595; DOI=10.1016/s0005-2736(00)00233-9;
RA   Merzendorfer H., Reineke S., Zhao X.F., Jacobmeier B., Harvey W.R.,
RA   Wieczorek H.;
RT   "The multigene family of the tobacco hornworm V-ATPase: novel subunits a,
RT   C, D, H, and putative isoforms.";
RL   Biochim. Biophys. Acta 1467:369-379(2000).
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 (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits VhaAC45 and ATP6AP2 (By similarity).
CC       {ECO:0000250|UniProtKB:P21283}.
CC   -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR   EMBL; AJ249388; CAB55498.1; -; mRNA.
DR   AlphaFoldDB; Q9U5N1; -.
DR   SMR; Q9U5N1; -.
DR   DIP; DIP-61388N; -.
DR   IntAct; Q9U5N1; 1.
DR   BindingDB; Q9U5N1; -.
DR   ChEMBL; CHEMBL2189157; -.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..385
FT                   /note="V-type proton ATPase subunit C"
FT                   /id="PRO_0000209354"
SQ   SEQUENCE   385 AA;  44127 MW;  844F3A3F38C29F3A CRC64;
     MSEYWLISAP GDKTCQQTWE ALNQATKANN LSLNYKFPIP DLKVGTLDQL VGLSDDLGKL
     DTFVEGVTRK VAQYLGEVLE DQRDKLHENL TANNDDLPHY LTRFQWDMAK YPIKQSLRNI
     ADIISKQVGQ IDADLKVKSS AYNALKGNLQ NLEKKQTGSL LTRNLADLVK KEHFILDSEY
     LTTLLVIVPK SMFNDWNANY EKITDMIVPR STQLIHQDGD YGLFTVTLFK KVVDEFKLHA
     RERKFVVREF AYNEADLVAG KNEITKLLTD KKKQFGPLVR WLKVNFSECF CAWIHVKALR
     VFVESVLRYG LPVNFQAALL VPSRRSARRL RDTLHALYAH LDHSAHHHAN AQQDSVELAG
     LGFGQSEYYP YVFYKINIDM IEKAA