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ATP6_LOXAF
ID   ATP6_LOXAF              Reviewed;         222 AA.
AC   Q9TA24; Q2I3F6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS   Loxodonta africana (African elephant).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RA   Hauf J., Waddell P.J., Chalwatzis N., Joger U., Zimmermann F.K.;
RT   "The complete mitochondrial genome sequence of the African elephant
RT   (Loxodonta africana), phylogenetic relationships of Proboscidea to other
RT   mammals and D-loop heteroplasmy.";
RL   Zoology 102:184-195(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=16448217; DOI=10.1371/journal.pbio.0040073;
RA   Rogaev E.I., Moliaka Y.K., Malyarchuk B.A., Kondrashov F.A., Derenko M.V.,
RA   Chumakov I., Grigorenko A.P.;
RT   "Complete mitochondrial genome and phylogeny of Pleistocene mammoth
RT   Mammuthus primigenius.";
RL   PLoS Biol. 4:403-410(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA12143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ224821; CAA12143.1; ALT_INIT; Genomic_DNA.
DR   EMBL; DQ316069; ABC17909.1; -; Genomic_DNA.
DR   PIR; T45555; T45555.
DR   RefSeq; NP_009284.2; NC_000934.1.
DR   AlphaFoldDB; Q9TA24; -.
DR   SMR; Q9TA24; -.
DR   STRING; 9785.ENSLAFP00000029496; -.
DR   GeneID; 808788; -.
DR   KEGG; lav:808788; -.
DR   CTD; 4508; -.
DR   eggNOG; KOG4665; Eukaryota.
DR   InParanoid; Q9TA24; -.
DR   OrthoDB; 1095315at2759; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..222
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082133"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        111
FT                   /note="P -> L (in Ref. 2; ABC17909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="S -> L (in Ref. 2; ABC17909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   222 AA;  24576 MW;  5D93F1EEDCF7D6EC CRC64;
     MNEELSTFFY VPVGTMMLAI AFPAILLPTP NRLITNRWIT IQQWLIQLIM KQLLSIHNTK
     GLSWSLMLIT LTLFIGLTNL LGLLPYSFAP TTQLTVNLSM AIPLWTGTVV PGFRYKTKIS
     LAHLLPQGTP MFLIPMIIII ETISLLIRPV TLAVRLTANI TAGHSLIHLT GTATLTLSSI
     HSMTITVTFV TVILLTILEL AVALIQAYVF ALLISLYLHE NA
 
 
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