ID   VATL_HELVI              Reviewed;         156 AA.
AC   P55277;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE            Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE   AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN   Name=VHA16;
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=8353524; DOI=10.1016/0965-1748(93)90041-p;
RA   Pietrantonio P.V., Gill S.S.;
RT   "Sequence of a 17 kDa vacuolar H(+)-ATPase proteolipid subunit from insect
RT   midgut and Malpighian tubules.";
RL   Insect Biochem. Mol. Biol. 23:675-680(1993).
CC   -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC       vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC       peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC       complex (V0) that translocates protons (By similarity). V-ATPase is
CC       responsible for acidifying and maintaining the pH of intracellular
CC       compartments and in some cell types, is targeted to the plasma
CC       membrane, where it is responsible for acidifying the extracellular
CC       environment (By similarity). {ECO:0000250|UniProtKB:P23380,
CC       ECO:0000250|UniProtKB:P27449}.
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:P27449}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; L16884; AAC37176.1; -; mRNA.
DR   PIR; A56680; A56680.
DR   AlphaFoldDB; P55277; -.
DR   SMR; P55277; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 1.20.120.610; -; 1.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR000245; ATPase_proteolipid_csu.
DR   InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; SSF81333; 2.
DR   TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..156
FT                   /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT                   /id="PRO_0000071751"
FT   TOPO_DOM        1..7
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..92
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..126
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..156
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   SITE            139
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250|UniProtKB:P63081"
SQ   SEQUENCE   156 AA;  15934 MW;  E8DB1065B896E4B5 CRC64;
     MAENPIYGPF FGVMGAASAI IFSALGAAYG TAKSGTGIAA MSVMRPELIM KSIIPVVMAG
     IIAIYGLVVA VLIAGSLDAP SNNYTLYKGF IHLGAGLAVG FSGLAAGFAI GIVGDAGVRG
     TAQQPRLFVG MILILIFAEV LGLYGLIVAI YLYTKQ