ID   VATC_ASCSS              Reviewed;         384 AA.
AC   Q9NDR5;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=VATC;
OS   Ascidia sydneiensis samea (Vanadium-rich ascidian).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Ascidiidae; Ascidia.
OX   NCBI_TaxID=79730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=14961347; DOI=10.1007/s1012601-0054-x;
RA   Ueki T., Uyama T., Kanamori K., Michibata H.;
RT   "Subunit C of the vacuolar-type ATPase from the vanadium-rich ascidian
RT   Ascidia sydneiensis samea rescued the pH sensitivity of yeast vma5
RT   mutants.";
RL   Mar. Biotechnol. 3:316-321(2001).
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:P31412, ECO:0000250|UniProtKB:Q9XXU9}.
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 vah-19/Ac45 and vah-20/PRR (By similarity).
CC       {ECO:0000250|UniProtKB:P21282}.
CC   -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR   EMBL; AB035809; BAA96746.1; -; mRNA.
DR   AlphaFoldDB; Q9NDR5; -.
DR   SMR; Q9NDR5; -.
DR   PRIDE; Q9NDR5; -.
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..384
FT                   /note="V-type proton ATPase subunit C 2"
FT                   /id="PRO_0000209350"
SQ   SEQUENCE   384 AA;  44105 MW;  16AFF1B6EC2D9068 CRC64;
     MSEFWVISAP GDKTPQQTYE RLQKATMGSG QNLSNCYKFS IPELKVGTLD SLIGLTDDLG
     KLDTFCEGVC RKVASYMGEV LEDQKDKLSS NLSAGEGTLV NFMHRFQWNM AKYPTKQPIK
     SLTEILSKVV TQVDTDLRSK SQAYNNLKSS LQNMERKATG SLLLRNLSQI VKKDDFIDGS
     EYLRTVIVAV PVALFGEWEK NYESLADYVA PKSSRLLTQD EEYGLFATSI FKKVYEEFKY
     NCSRYKFFVR EFNFNEQDSV VRQDQINKIA SEKRKMLGPL LRWLKVNFSE VFTAWIHIKA
     LRVFVESVLR YGLPVNFQAV VLDPPKKNRK RLRDVLNNLY CKLDSTGLTN VDAEDSVPGL
     SLGMQEYYPY VFYKVILDFE SRSF