ATP6_CANLU
ID ATP6_CANLU Reviewed; 226 AA.
AC Q1HKB1; Q1HK98; Q1HKF0; Q3L6Z4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS Canis lupus (Gray wolf).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9612;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-187.
RX PubMed=15964215; DOI=10.1016/j.ympev.2005.04.025;
RA Delisle I., Strobeck C.;
RT "A phylogeny of the Caniformia (order Carnivora) based on 12 complete
RT protein-coding mitochondrial genes.";
RL Mol. Phylogenet. Evol. 37:192-201(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-66; ILE-143; ILE-187
RP AND THR-201.
RX PubMed=16809672; DOI=10.1101/gr.5117706;
RA Bjornerfeldt S., Webster M.T., Vila C.;
RT "Relaxation of selective constraint on dog mitochondrial DNA following
RT domestication.";
RL Genome Res. 16:990-994(2006).
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. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct
CC (By similarity). {ECO:0000250|UniProtKB:P00846,
CC ECO:0000250|UniProtKB:P00847}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR EMBL; AY598494; AAU00440.1; -; Genomic_DNA.
DR EMBL; DQ480503; ABE48160.1; -; Genomic_DNA.
DR EMBL; DQ480504; ABE48173.1; -; Genomic_DNA.
DR EMBL; DQ480505; ABE48186.1; -; Genomic_DNA.
DR EMBL; DQ480506; ABE48199.1; -; Genomic_DNA.
DR EMBL; DQ480507; ABE48212.1; -; Genomic_DNA.
DR EMBL; DQ480508; ABE48225.1; -; Genomic_DNA.
DR RefSeq; YP_626733.1; NC_008092.1.
DR AlphaFoldDB; Q1HKB1; -.
DR SMR; Q1HKB1; -.
DR GeneID; 4097769; -.
DR CTD; 4508; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); 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 Gene3D; 1.20.120.220; -; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..226
FT /note="ATP synthase subunit a"
FT /id="PRO_0000269706"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 66
FT /note="R -> Q"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 143
FT /note="V -> I"
FT /evidence="ECO:0000269|PubMed:16809672"
FT VARIANT 187
FT /note="T -> I"
FT /evidence="ECO:0000269|PubMed:15964215,
FT ECO:0000269|PubMed:16809672"
FT VARIANT 201
FT /note="I -> T"
FT /evidence="ECO:0000269|PubMed:16809672"
SQ SEQUENCE 226 AA; 24789 MW; 9A4C7B4590575007 CRC64;
MNENLFASFA APSMMGLPIV VLIVMFPSIL FPTPSRLINN RLISIQQWLI QLTSKQMLAI
HNQKGRTWAL MLMSLILFIG STNLLGLLPH SFTPTTQLSM NLGMAIPLWA GTVITGFRYK
TKASLAHFLP QGTPLPLIPM LVVIETISLF IQPMALAVRL TANITAGHLL IHLIGGATLA
LINISATTAF ITFIILILLT ILEFAVALIQ AYVFTLLVSL YLHDNT
