ID G1KXN4_ANOCA Unreviewed; 135 AA.
AC G1KXN4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000020235.1, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000020235.1, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000020235.1,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000020235.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU004221}.
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DR AlphaFoldDB; G1KXN4; -.
DR STRING; 28377.ENSACAP00000020235; -.
DR Ensembl; ENSACAT00000024951.1; ENSACAP00000020235.1; ENSACAG00000022716.1.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000159720; -.
DR HOGENOM; CLU_116822_1_0_1; -.
DR InParanoid; G1KXN4; -.
DR TreeFam; TF300140; -.
DR Proteomes; UP000001646; Chromosome 4.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1.
DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
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:SF55; ATP SYNTHASE F(0) COMPLEX SUBUNIT C2, 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.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU004221};
KW Ion transport {ECO:0000256|RuleBase:RU004221};
KW Lipid-binding {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:UP000001646};
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}; Transport {ECO:0000256|RuleBase:RU004221}.
FT TRANSMEM 106..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004221"
FT DOMAIN 70..131
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 135 AA; 14116 MW; 852595516CB377DD CRC64;
APLALMASPA LLHCCSQALT SPTSLSILSR PETQTVQPFG ISNHQLVQRE FQTSVISCDI
DAAAKFIGAG AGTATVGVAD SGAGTGTVFG SLIISYAKNP SLNQQLFFYA ILGFALSETM
GLFCLMVAFL IFFTM
//
