(data stored in ACNUC7421 zone)

SWISSPROT: ATPF_ASHGO

ID   ATPF_ASHGO              Reviewed;         236 AA.
AC   Q758L2;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 88.
DE   RecName: Full=ATP synthase subunit 4, mitochondrial;
DE   Flags: Precursor;
GN   Name=ATP4; OrderedLocusNames=AEL251C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 189; 194; 196; 198 AND
RP   C-TERMINUS.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements (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. In yeast, the dimeric form
CC       of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC       epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC       and k (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC       membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase subunit B family.
CC       {ECO:0000305}.
DR   EMBL; AE016818; AAS52434.2; -; Genomic_DNA.
DR   RefSeq; NP_984610.2; NM_209963.2.
DR   SMR; Q758L2; -.
DR   STRING; 33169.AAS52434; -.
DR   PRIDE; Q758L2; -.
DR   EnsemblFungi; AAS52434; AAS52434; AGOS_AEL251C.
DR   GeneID; 4620792; -.
DR   KEGG; ago:AGOS_AEL251C; -.
DR   HOGENOM; HOG000158315; -.
DR   InParanoid; Q758L2; -.
DR   KO; K02127; -.
DR   OMA; WVRYEAS; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IEA:EnsemblFungi.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:EnsemblFungi.
DR   InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR   InterPro; IPR013837; ATP_synth_F0_suB.
DR   PANTHER; PTHR12733; PTHR12733; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758L2.
DR   SWISS-2DPAGE; Q758L2.
KW   CF(0); Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..236
FT                   /note="ATP synthase subunit 4, mitochondrial"
FT                   /id="PRO_0000002518"
SQ   SEQUENCE   236 AA;  25617 MW;  067BBD766A132C88 CRC64;
     MAFRALTTKA AARPLLALGP RSVAMGARYM STPAPQDPKS KAAAILDSLP GSTALSKTGI
     LATSAAAAIY AISNELYVLN AETILLCTFT GFSFLIAKLV APAYKEYADK RMQHVSGILN
     SSRNKHVAAV KERIESVSEL KNVTETTKVL FEVSKETLEL EAKAFELKQK VDLATEAKAV
     LDSWVRYEAS VRQLQQKQIA ESVIGKVQAE LANPKFQDKV LQQSVADVEK LFASLK
//

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