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Database: UniProt
Entry: H1VU40_COLHI
LinkDB: H1VU40_COLHI
Original site: H1VU40_COLHI 
ID   H1VU40_COLHI            Unreviewed;       200 AA.
AC   H1VU40;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=ATP synthase subunit C {ECO:0000313|EMBL:CCF43748.1};
GN   ORFNames=CH063_03153 {ECO:0000313|EMBL:CCF43748.1}, CH63R_04808
GN   {ECO:0000313|EMBL:OBR12512.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF43748.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|EMBL:CCF43748.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF43748.1};
RA   Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
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).
RN   [3] {ECO:0000313|EMBL:OBR12512.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR12512.1};
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000092177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX   PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA   Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA   Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA   Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA   Thon M.R., O'Connell R.J.;
RT   "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT   structure and association of transposable elements with secondary
RT   metabolite gene clusters.";
RL   BMC Genomics 18:667-667(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}. Vacuole membrane
CC       {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004128}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000256|ARBA:ARBA00007296, ECO:0000256|RuleBase:RU363060}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU363060}.
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DR   EMBL; CACQ02006345; CCF43748.1; -; Genomic_DNA.
DR   EMBL; LTAN01000003; OBR12512.1; -; Genomic_DNA.
DR   RefSeq; XP_018161029.1; XM_018299783.1.
DR   STRING; 759273.H1VU40; -.
DR   EnsemblFungi; CCF43748; CCF43748; CH063_03153.
DR   GeneID; 28863890; -.
DR   KEGG; chig:CH63R_04808; -.
DR   VEuPathDB; FungiDB:CH63R_04808; -.
DR   eggNOG; KOG0233; Eukaryota.
DR   HOGENOM; CLU_085752_0_1_1; -.
DR   OrthoDB; 1112183at2759; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   Proteomes; UP000092177; Chromosome 3.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:EnsemblFungi.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
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   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   TRANSMEM        5..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        43..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        86..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        128..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        165..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   DOMAIN          48..105
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   200 AA;  20472 MW;  3F1D97177BA30C80 CRC64;
     MSLTYGLGGI GSTLLVVGAY MLFTGSGEAF NVGEFLESIS PYAWADTGIA LCIGLSVVGA
     AWGIFITGSS ILGAGVKAPR VRTKNLISII FCEVVAIYGV IMAIVFSAQL ENVQGQTLHD
     GNSYYTGFAL FWAGITVGMC NLICGVAVGI NGSGAALADA ADPTLFVKIL VVEIFSSVLG
     LFGLIVGLLV SGKANAFGKV
//
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