ID   VATC_HORVU              Reviewed;         354 AA.
AC   Q9SCB9;
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;
GN   Name=VATC; Synonyms=ATC;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 143-151 AND 249-263.
RC   STRAIN=cv. Gerbel; TISSUE=Leaf;
RX   PubMed=10452532; DOI=10.1016/s0014-5793(99)00937-0;
RA   Tavakoli N., Eckerskorn C., Golldack D., Dietz K.-J.;
RT   "Subunit C of the vacuolar H+-ATPase of Hordeum vulgare.";
RL   FEBS Lett. 456:68-72(1999).
CC   -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase.
CC       Subunit C is necessary for the assembly of the catalytic sector of the
CC       enzyme and is likely to have a specific function in its catalytic
CC       activity. V-ATPase is responsible for acidifying a variety of
CC       intracellular compartments in eukaryotic cells (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (components A to H) attached to an integral
CC       membrane V0 proton pore complex (components: a, c, c', c'' and d).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane. Note=Tonoplast.
CC   -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR   EMBL; AJ242873; CAB65127.1; -; mRNA.
DR   AlphaFoldDB; Q9SCB9; -.
DR   SMR; Q9SCB9; -.
DR   PRIDE; Q9SCB9; -.
DR   ExpressionAtlas; Q9SCB9; baseline and differential.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW   Transport; Vacuole.
FT   CHAIN           1..354
FT                   /note="V-type proton ATPase subunit C"
FT                   /id="PRO_0000209356"
SQ   SEQUENCE   354 AA;  39985 MW;  BC757FB586A4CD24 CRC64;
     MATRYWIAAL PVADDNVAAG KTALWARLQE AISRHSFDTP LYRFTVPDLR PGTLDSLLAL
     SDDLVKSNIF IEGVSHKIRR QIEDLERAGG VEPGTLTVDG VPVDSYLTRF VWDEGKYPVN
     APLKETVASI QSQVAKIEDD MKVRVAEYGN VKSQLGAINR KQTGSLAVRD LSNLIKPEDM
     VTSEHLVTLL SIVPKYSQKD WLASYESLDT FVVPRSSKKL YEDNEYALYT VTLFAKVVDN
     FKVHAREKGF QIRDFEYSPE AQESRKQELE KLLQDQEVMR TSPIAMGAML ATVRVFSSWD
     AFSSAVRVFV ESILRYGSAC TVPVCCPSTI YKEREKSKEH LGRAMRQYQQ LLEI