ID A0A2H3E4S0_ARMGA Unreviewed; 210 AA.
AC A0A2H3E4S0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=V-ATPase proteolipid subunit C-like domain-containing protein {ECO:0000259|Pfam:PF00137};
GN ORFNames=ARMGADRAFT_990573 {ECO:0000313|EMBL:PBK95563.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK95563.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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. V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments.
CC {ECO:0000256|RuleBase:RU363060}.
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'', d, e, f and
CC VOA1). The decameric c-ring forms the proton-conducting pore, and is
CC composed of eight proteolipid subunits c, one subunit c' and one
CC subunit c''. {ECO:0000256|RuleBase:RU363060}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000256|ARBA:ARBA00007296, ECO:0000256|RuleBase:RU363060}.
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DR EMBL; KZ293652; PBK95563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3E4S0; -.
DR STRING; 47427.A0A2H3E4S0; -.
DR InParanoid; A0A2H3E4S0; -.
DR OMA; GWFLENT; -.
DR OrthoDB; 1112183at2759; -.
DR Proteomes; UP000217790; Unassembled WGS sequence.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProt.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18177; ATP-synt_Vo_c_ATP6F_rpt1; 1.
DR CDD; cd18178; ATP-synt_Vo_c_ATP6F_rpt2; 1.
DR Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10263:SF18; V-TYPE PROTON ATPASE 21 KDA PROTEOLIPID SUBUNIT C; 1.
DR PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU363060};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363060};
KW Reference proteome {ECO:0000313|Proteomes:UP000217790};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363060};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363060};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363060}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..210
FT /note="V-ATPase proteolipid subunit C-like domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013641944"
FT TRANSMEM 52..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 127..156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT DOMAIN 47..104
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 131..189
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 210 AA; 21775 MW; 752EBECB1ED6A864 CRC64;
MGYFSYGLPS FLVLVIALYI LLTGSGEAFN VGRFLEETSP YAWAATGIGL DIGLSVLGAG
WGIFVTGSSI LGGGVRAPRI STKNLISIIF CEVVAIYGVI IGIVYSAKIT SVADSVLYTR
ENYYTGFALF WGGLTVGACN LLCGVCVGIT GSTAALSDAA DPNLFVKILV VEVFGSIMGL
FGLITGLLMV SAADDFKGAA VEAVVSPFVH
//
