ID   VATL_TORMA              Reviewed;         154 AA.
AC   Q03105;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=15 kDa mediatophore protein;
DE   AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 63-79.
RC   TISSUE=Electric lobe;
RX   PubMed=2155824; DOI=10.1016/0014-5793(90)80577-6;
RA   Birman S., Meunier F.-M., Lesbats B., le Caer J.-P., Rossier J., Israel M.;
RT   "A 15 kDa proteolipid found in mediatophore preparations from Torpedo
RT   electric organ presents high sequence homology with the bovine chromaffin
RT   granule protonophore.";
RL   FEBS Lett. 261:303-306(1990).
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:P23956,
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 two accessory subunits (By similarity).
CC       {ECO:0000250|UniProtKB:P27449}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X52002; CAA36253.1; -; mRNA.
DR   PIR; S08261; S08261.
DR   AlphaFoldDB; Q03105; -.
DR   SMR; Q03105; -.
DR   TCDB; 9.B.16.1.2; the putative ductin channel (ductin) family.
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:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..154
FT                   /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT                   /id="PRO_0000071747"
FT   TOPO_DOM        1..9
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..91
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        152..154
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   SITE            138
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250|UniProtKB:P63081"
SQ   SEQUENCE   154 AA;  15512 MW;  E01943883AF23B9B CRC64;
     MSTPGAPEYS AFFGVIGASA AMVFSALGAA YGTAKSGTGI AAMSVMRPEL IMKSIIPVVM
     AGIIAIYGLV VAVLIANSLT EDISLFKSFL QLGAGLSVGL SGLAAGFAIG IVGDAGVRGT
     AQQPRLFVGM ILILIFAEVL GLYGLIVALI LSTK