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ATP6_DICDI
ID   ATP6_DICDI              Reviewed;         244 AA.
AC   Q27559; Q9XPJ7;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=atp6; ORFNames=DDB_G0294014;
OS   Dictyostelium discoideum (Slime mold).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=10821186; DOI=10.1007/pl00008685;
RA   Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K.,
RA   Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT   "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene
RT   content and genome organization.";
RL   Mol. Gen. Genet. 263:514-519(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-244.
RC   STRAIN=AX3;
RX   PubMed=9560439; DOI=10.1007/s002940050341;
RA   Iwamoto M., Pi M., Kurihara M., Morio T., Tanaka Y.;
RT   "A ribosomal protein gene cluster is encoded in the mitochondrial DNA of
RT   Dictyostelium discoideum: UGA termination codons and similarity of gene
RT   order to Acanthamoeba castellanii.";
RL   Curr. Genet. 33:304-310(1998).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR   EMBL; AB000109; BAA78068.1; -; Genomic_DNA.
DR   EMBL; D21196; BAA04732.1; -; Genomic_DNA.
DR   PIR; T43764; T43764.
DR   RefSeq; NP_050086.1; NC_000895.1.
DR   AlphaFoldDB; Q27559; -.
DR   SMR; Q27559; -.
DR   GeneID; 2193914; -.
DR   KEGG; ddi:DidioMp19; -.
DR   dictyBase; DDB_G0294014; atp6.
DR   InParanoid; Q27559; -.
DR   OMA; FFDQFMS; -.
DR   PhylomeDB; Q27559; -.
DR   PRO; PR:Q27559; -.
DR   Proteomes; UP000002195; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR   Gene3D; 1.20.120.220; -; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 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..244
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000312373"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   244 AA;  27802 MW;  E3A436C7E88F3A96 CRC64;
     MKSLFEQFEI DLYCIIITRF FDISITTITV YLGLLMVIVI GMYKVSLYKA TIIGGNNWQH
     IGEMIYEFVV DLIIEQVGKP GILFFPFIMS LFLFVLTLNV MGLIPLSFTV TGQLLVTFTL
     AITIMIGITI WGFRIHGIKF LNIFVPSGIE PWLLPLLVFI EIMSYVLRPI SLAVRLFANM
     LAGHLLIHII GVAAIYLMQF YFIGILPWIC VIAFMFLELG IAFLQAYVFV LLTLIYIANI
     INLH
 
 
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