ID A0A3B3YDZ4_9TELE Unreviewed; 141 AA.
AC A0A3B3YDZ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000025569.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000025569.1}
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_014859782.1; XM_015004296.1.
DR AlphaFoldDB; A0A3B3YDZ4; -.
DR STRING; 48701.ENSPMEP00000025569; -.
DR Ensembl; ENSPMET00000004782.1; ENSPMEP00000025569.1; ENSPMEG00000008620.1.
DR GeneID; 106928198; -.
DR KEGG; pmei:106928198; -.
DR OrthoDB; 316029at2759; -.
DR Proteomes; UP000261480; Unplaced.
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:SF53; ATP SYNTHASE F(0) COMPLEX SUBUNIT C3, 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 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 74..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004221"
FT TRANSMEM 112..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004221"
FT DOMAIN 75..137
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 141 AA; 14517 MW; BCC19748089F59C9 CRC64;
MYACAKFVST PSLVRAGSRV LYRPLSAAVV SDSRKAETAS LLAPQSPAAS QQQVAVRGFQ
TSAVSRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII GYARNPSLKQ QLFSYAILGF
ALSEAMGLFC LMVAFLILFA M
//
