ID   A0A0B2ULH5_TOXCA        Unreviewed;       116 AA.
AC   A0A0B2ULH5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ATPase protein 9 {ECO:0000256|ARBA:ARBA00033111};
DE   AltName: Full=ATPase subunit c {ECO:0000256|ARBA:ARBA00029852};
GN   Name=Y82E9BR.3 {ECO:0000313|EMBL:KHN71891.1};
GN   ORFNames=Tcan_18700 {ECO:0000313|EMBL:KHN71891.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN71891.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN71891.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN71891.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004225}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC       {ECO:0000256|ARBA:ARBA00006704, ECO:0000256|RuleBase:RU004221}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHN71891.1}.
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DR   EMBL; JPKZ01014295; KHN71891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2ULH5; -.
DR   STRING; 6265.A0A0B2ULH5; -.
DR   OMA; SAISCDI; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1.
DR   Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR   InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   PANTHER; PTHR10031; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10031:SF0; ATPASE PROTEIN 9; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
PE   3: Inferred from homology;
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU004221};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU004221};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121,
KW   ECO:0000256|RuleBase:RU004221};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004221};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU004221};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU004221};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU004221}.
FT   TRANSMEM        49..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004221"
FT   TRANSMEM        87..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004221"
FT   DOMAIN          50..112
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   116 AA;  12357 MW;  112F124FC2B78E5E CRC64;
     MYCQRLMFPL SRTLVQRVPS AVRPECALMM TRCLHKTVAR RDIDSAAKYI GAGAATVGVA
     GSGAGIGNVF GALVIGYARN PSLKAQLFSY AILGFALSEA MGLFCLTMGF MILFAL
//