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Database: UniProt
Entry: A0A0L8H161_OCTBM
LinkDB: A0A0L8H161_OCTBM
Original site: A0A0L8H161_OCTBM 
ID   A0A0L8H161_OCTBM        Unreviewed;       151 AA.
AC   A0A0L8H161;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=ATPase protein 9 {ECO:0000256|ARBA:ARBA00033111};
DE   AltName: Full=ATPase subunit c {ECO:0000256|ARBA:ARBA00029852};
GN   ORFNames=OCBIM_22024498mg {ECO:0000313|EMBL:KOF83021.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF83021.1};
RN   [1] {ECO:0000313|EMBL:KOF83021.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF83021.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF83021.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) 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}.
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DR   EMBL; KQ419590; KOF83021.1; -; Genomic_DNA.
DR   RefSeq; XP_014776261.1; XM_014920775.1.
DR   AlphaFoldDB; A0A0L8H161; -.
DR   STRING; 37653.A0A0L8H161; -.
DR   EnsemblMetazoa; Ocbimv22024498m; Ocbimv22024498m.p; Ocbimv22024498m.g.
DR   EnsemblMetazoa; XM_014920775.1; XP_014776261.1; LOC106873419.
DR   GeneID; 106873419; -.
DR   KEGG; obi:106873419; -.
DR   OMA; IPSATRC; -.
DR   OrthoDB; 316029at2759; -.
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   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        84..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004221"
FT   TRANSMEM        122..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004221"
FT   DOMAIN          85..147
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   151 AA;  16077 MW;  15087D82EA377064 CRC64;
     MYACTRYIPS ATRCMLTSSR SALRPLGSTV IPMQENSQSQ SLVPLASCTS FSISQSQMLS
     LIQNQVRFFQ TSSVRNDIDQ AAKYIGAGAA TVGAAGSGAG IGSVFGNLVI GYARNPSLKQ
     QLFSYAILGF ALSEAMGLFC LMMAFLILFA F
//
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