ID   VATL_NEPNO              Reviewed;         159 AA.
AC   Q26250;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-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};
OS   Nephrops norvegicus (Norway lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Nephropoidea; Nephropidae; Nephrops.
OX   NCBI_TaxID=6829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1378613; DOI=10.1093/protein/5.1.7;
RA   Finbow M.E., Eliopoulos E.E., Jackson P.J., Keen J.N., Meagher L.,
RA   Thompson P., Jones P., Findlay J.B.;
RT   "Structure of a 16 kDa integral membrane protein that has identity to the
RT   putative proton channel of the vacuolar H(+)-ATPase.";
RL   Protein Eng. 5:7-15(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 153-159, AND FUNCTION.
RX   PubMed=8168500; DOI=10.1111/j.1432-1033.1994.tb18719.x;
RA   Harrison M.A., Jones P.C., Kim Y.I., Finbow M.E., Findlay J.B.;
RT   "Functional properties of a hybrid vacuolar H(+)-ATPase in Saccharomyces
RT   cells expressing the Nephrops 16-kDa proteolipid.";
RL   Eur. J. Biochem. 221:111-120(1994).
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 (PubMed:8168500). 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 (PubMed:8168500). {ECO:0000269|PubMed:8168500}.
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   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; S40059; AAB22508.1; -; mRNA.
DR   PIR; S32544; S32544.
DR   AlphaFoldDB; Q26250; -.
DR   SMR; Q26250; -.
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   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..159
FT                   /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT                   /id="PRO_0000071756"
FT   TOPO_DOM        1..11
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..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..93
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        154..159
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   SITE            140
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250|UniProtKB:P63081"
SQ   SEQUENCE   159 AA;  16280 MW;  9E34590CDE4C21B9 CRC64;
     MSEEGSPMYS PFFGVMGAAS AMVFSALGAA YGTAKSGVGI SAMSVMRPEL IMKCIIPVVM
     AGIIAIYGLV VAVLIAGKLD EAPTYTLYQG FVHMGAGLSV GLSGLAAGFA IGIVGDAGVR
     GTAQQPRLYV GMILILIFAE VLGLYGLIVA IFLYTKTSS