ID A0A3P8VZM9_CYNSE Unreviewed; 137 AA.
AC A0A3P8VZM9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP synthase lipid-binding protein {ECO:0000256|ARBA:ARBA00032304};
DE AltName: Full=ATPase protein 9 {ECO:0000256|ARBA:ARBA00033111};
DE AltName: Full=ATPase subunit c {ECO:0000256|ARBA:ARBA00029852};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000019769.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000019769.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000019769.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. A homomeric c-ring of probably 10 subunits is part of the
CC complex rotary element. {ECO:0000256|ARBA:ARBA00003897}.
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 RefSeq; XP_008328769.1; XM_008330547.2.
DR AlphaFoldDB; A0A3P8VZM9; -.
DR Ensembl; ENSCSET00000020008.1; ENSCSEP00000019769.1; ENSCSEG00000012587.1.
DR GeneID; 103393548; -.
DR KEGG; csem:103393548; -.
DR CTD; 516; -.
DR GeneTree; ENSGT00940000157981; -.
DR OMA; SAISCDI; -.
DR OrthoDB; 316029at2759; -.
DR Proteomes; UP000265120; Chromosome 17.
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:SF32; ATP SYNTHASE F(0) COMPLEX SUBUNIT C1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10031; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 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:UP000265120};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
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 70..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004221"
FT TRANSMEM 108..136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004221"
FT DOMAIN 71..133
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 137 AA; 14270 MW; 8EB9B616C6185D28 CRC64;
MYACAKFITS PAVLRGGSRV LARPVSVSLF NRPEATVEQQ ALLPLSQSVV LSRSFQTSAV
SRDIDTAAKF IGAGAATVGV AGSGAGIGTV FGSLIIGYAR NPSLKQQLFS YAILGFALSE
AMGLFCLMVA FLILFAM
//
