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Database: UniProt
Entry: A0A226N7Q0_CALSU
LinkDB: A0A226N7Q0_CALSU
Original site: A0A226N7Q0_CALSU 
ID   A0A226N7Q0_CALSU        Unreviewed;       134 AA.
AC   A0A226N7Q0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   22-FEB-2023, entry version 18.
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};
GN   ORFNames=ASZ78_008919 {ECO:0000313|EMBL:OXB63604.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB63604.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB63604.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB63604.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB63604.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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: 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:OXB63604.1}.
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DR   EMBL; MCFN01000151; OXB63604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226N7Q0; -.
DR   STRING; 9009.A0A226N7Q0; -.
DR   Proteomes; UP000198323; 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:SF45; ATP SYNTHASE LIPID-BINDING PROTEIN; 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:UP000198323};
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        67..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004221"
FT   TRANSMEM        105..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004221"
FT   DOMAIN          68..130
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   134 AA;  14109 MW;  FCAA0E6AECAFFB99 CRC64;
     MGRADVVPVC RCRSQSARRT LGDTARALAR PVSVSVFSRP EAQTVQLTRR EFQTSAVSRD
     IDTAAKFIGA GAATVGVAGS GAGIGTVFGS LIIGYARNPS LKQQLFSYAI LGFALSEAMG
     LFCLMVAFLI LFAM
//
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