ID E3Q7D6_COLGM Unreviewed; 164 AA.
AC E3Q7D6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=V-type proton ATPase proteolipid subunit {ECO:0000256|RuleBase:RU363060};
GN ORFNames=GLRG_02594 {ECO:0000313|EMBL:EFQ26774.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004128, ECO:0000256|RuleBase:RU363060}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004128,
CC ECO:0000256|RuleBase:RU363060}.
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; GG697335; EFQ26774.1; -; Genomic_DNA.
DR RefSeq; XP_008090794.1; XM_008092603.1.
DR AlphaFoldDB; E3Q7D6; -.
DR STRING; 645133.E3Q7D6; -.
DR EnsemblFungi; EFQ26774; EFQ26774; GLRG_02594.
DR GeneID; 24407959; -.
DR VEuPathDB; FungiDB:GLRG_02594; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_1_1; -.
DR OrthoDB; 168305at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:EnsemblFungi.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18175; ATP-synt_Vo_c_ATP6C_rpt1; 1.
DR CDD; cd18176; ATP-synt_Vo_c_ATP6C_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; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR NCBIfam; TIGR01100; V_ATP_synt_C; 1.
DR PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR PANTHER; PTHR10263:SF8; V-TYPE PROTON ATPASE SUBUNIT C; 1.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU363060};
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:UP000008782};
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};
KW Vacuole {ECO:0000256|RuleBase:RU363060}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 97..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 133..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT DOMAIN 19..77
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 99..158
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 164 AA; 16782 MW; 2F47F0924A051FE9 CRC64;
MAEDSVLAPK FAPFIGMAGI AAAMIFGCIG AAYGTAKSGI GIAGVGTFRP DLIMKCLIPV
VMSGIIAVYS LVISVLIAQD LTPPGAGSNY SLFNGFMHLA CGLSVGLTGL AAGYTIGIVG
DKGVRSYMEQ SRIFVGMVLI LIFGEVLGLY GLIVALILNT KSKG
//
