Full text data of ATP5F1
ATP5F1
[Confidence: low (only semi-automatic identification from reviews)]
ATP synthase F(0) complex subunit B1, mitochondrial (ATP synthase proton-transporting mitochondrial F(0) complex subunit B1; ATP synthase subunit b; ATPase subunit b; Flags: Precursor)
ATP synthase F(0) complex subunit B1, mitochondrial (ATP synthase proton-transporting mitochondrial F(0) complex subunit B1; ATP synthase subunit b; ATPase subunit b; Flags: Precursor)
UniProt
P24539
ID AT5F1_HUMAN Reviewed; 256 AA.
AC P24539; Q9BQ68; Q9BRU8;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=ATP synthase F(0) complex subunit B1, mitochondrial;
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit B1;
DE AltName: Full=ATP synthase subunit b;
DE Short=ATPase subunit b;
DE Flags: Precursor;
GN Name=ATP5F1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1831354; DOI=10.1016/0006-291X(91)90993-H;
RA Higuti T., Tsurumi C., Osaka F., Kawamura Y., Tsujita H.,
RA Yoshihara Y., Tani I., Tanaka K., Ichirara A.;
RT "Molecular cloning of cDNA for the import precursor of human subunit B
RT of H(+)-ATP synthase in mitochondria.";
RL Biochem. Biophys. Res. Commun. 178:1014-1020(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-233, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC synthase or Complex V) produces ATP from ADP in the presence of a
CC proton gradient across the membrane which is generated by electron
CC transport complexes of the respiratory chain. F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the
CC membrane proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central
CC stalk subunits to proton translocation. Part of the complex F(0)
CC 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.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC core - and CF(0) - the membrane proton channel. CF(1) has five
CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC has three main subunits: a, b and c. Component of an ATP synthase
CC complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J,
CC ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O,
CC ATP5L, USMG5 and MP68 (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
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CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X60221; CAA42782.1; -; mRNA.
DR EMBL; AL390195; CAC36042.1; -; Genomic_DNA.
DR EMBL; BC005366; AAH05366.1; -; mRNA.
DR EMBL; BC005960; AAH05960.1; -; mRNA.
DR EMBL; BC016350; AAH16350.1; -; mRNA.
DR PIR; JQ1144; JQ1144.
DR RefSeq; NP_001679.2; NM_001688.4.
DR UniGene; Hs.514870; -.
DR ProteinModelPortal; P24539; -.
DR SMR; P24539; 121-249.
DR IntAct; P24539; 17.
DR MINT; MINT-3010280; -.
DR STRING; 9606.ENSP00000358737; -.
DR PhosphoSite; P24539; -.
DR DMDM; 20455474; -.
DR PaxDb; P24539; -.
DR PeptideAtlas; P24539; -.
DR PRIDE; P24539; -.
DR Ensembl; ENST00000369722; ENSP00000358737; ENSG00000116459.
DR GeneID; 515; -.
DR KEGG; hsa:515; -.
DR UCSC; uc001ebc.3; human.
DR CTD; 515; -.
DR GeneCards; GC01P111991; -.
DR HGNC; HGNC:840; ATP5F1.
DR HPA; HPA046067; -.
DR MIM; 603270; gene.
DR neXtProt; NX_P24539; -.
DR PharmGKB; PA25130; -.
DR eggNOG; NOG245616; -.
DR HOGENOM; HOG000007163; -.
DR HOVERGEN; HBG050604; -.
DR InParanoid; P24539; -.
DR KO; K02127; -.
DR OMA; VINHETF; -.
DR OrthoDB; EOG7V4B02; -.
DR PhylomeDB; P24539; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; ATP5F1; -.
DR GenomeRNAi; 515; -.
DR NextBio; 2135; -.
DR PRO; PR:P24539; -.
DR ArrayExpress; P24539; -.
DR Bgee; P24539; -.
DR CleanEx; HS_ATP5F1; -.
DR Genevestigator; P24539; -.
DR GO; GO:0005759; C:mitochondrial matrix; NAS:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:RefGenome.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:RefGenome.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR InterPro; IPR008688; ATPase_B_chain/sub_B/MI25.
DR InterPro; IPR013837; ATPase_F0_sub_B/B_chain.
DR PANTHER; PTHR12733; PTHR12733; 1.
DR Pfam; PF05405; Mt_ATP-synt_B; 1.
PE 1: Evidence at protein level;
KW Acetylation; CF(0); Complete proteome; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Polymorphism; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1 42 Mitochondrion.
FT CHAIN 43 256 ATP synthase F(0) complex subunit B1,
FT mitochondrial.
FT /FTId=PRO_0000002513.
FT MOD_RES 139 139 N6-acetyllysine (By similarity).
FT MOD_RES 154 154 N6-acetyllysine (By similarity).
FT MOD_RES 162 162 N6-acetyllysine (By similarity).
FT MOD_RES 221 221 N6-acetyllysine.
FT MOD_RES 233 233 N6-acetyllysine.
FT MOD_RES 244 244 N6-acetyllysine (By similarity).
FT VARIANT 152 152 T -> M (in dbSNP:rs1264895).
FT /FTId=VAR_033534.
FT VARIANT 152 152 T -> N (in dbSNP:rs1264895).
FT /FTId=VAR_013176.
FT CONFLICT 84 84 I -> V (in Ref. 1; CAA42782).
FT CONFLICT 91 91 E -> G (in Ref. 3; AAH05960).
FT CONFLICT 194 194 K -> R (in Ref. 3; AAH05960).
SQ SEQUENCE 256 AA; 28909 MW; 743B1C54BFFEBBBD CRC64;
MLSRVVLSAA ATAAPSLKNA AFLGPGVLQA TRTFHTGQPH LVPVPPLPEY GGKVRYGLIP
EEFFQFLYPK TGVTGPYVLG TGLILYALSK EIYVISAETF TALSVLGVMV YGIKKYGPFV
ADFADKLNEQ KLAQLEEAKQ ASIQHIQNAI DTEKSQQALV QKRHYLFDVQ RNNIAMALEV
TYRERLYRVY KEVKNRLDYH ISVQNMMRRK EQEHMINWVE KHVVQSISTQ QEKETIAKCI
ADLKLLAKKA QAQPVM
//
ID AT5F1_HUMAN Reviewed; 256 AA.
AC P24539; Q9BQ68; Q9BRU8;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=ATP synthase F(0) complex subunit B1, mitochondrial;
DE AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit B1;
DE AltName: Full=ATP synthase subunit b;
DE Short=ATPase subunit b;
DE Flags: Precursor;
GN Name=ATP5F1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1831354; DOI=10.1016/0006-291X(91)90993-H;
RA Higuti T., Tsurumi C., Osaka F., Kawamura Y., Tsujita H.,
RA Yoshihara Y., Tani I., Tanaka K., Ichirara A.;
RT "Molecular cloning of cDNA for the import precursor of human subunit B
RT of H(+)-ATP synthase in mitochondria.";
RL Biochem. Biophys. Res. Commun. 178:1014-1020(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-233, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC synthase or Complex V) produces ATP from ADP in the presence of a
CC proton gradient across the membrane which is generated by electron
CC transport complexes of the respiratory chain. F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the
CC membrane proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central
CC stalk subunits to proton translocation. Part of the complex F(0)
CC 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.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC core - and CF(0) - the membrane proton channel. CF(1) has five
CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC has three main subunits: a, b and c. Component of an ATP synthase
CC complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J,
CC ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O,
CC ATP5L, USMG5 and MP68 (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X60221; CAA42782.1; -; mRNA.
DR EMBL; AL390195; CAC36042.1; -; Genomic_DNA.
DR EMBL; BC005366; AAH05366.1; -; mRNA.
DR EMBL; BC005960; AAH05960.1; -; mRNA.
DR EMBL; BC016350; AAH16350.1; -; mRNA.
DR PIR; JQ1144; JQ1144.
DR RefSeq; NP_001679.2; NM_001688.4.
DR UniGene; Hs.514870; -.
DR ProteinModelPortal; P24539; -.
DR SMR; P24539; 121-249.
DR IntAct; P24539; 17.
DR MINT; MINT-3010280; -.
DR STRING; 9606.ENSP00000358737; -.
DR PhosphoSite; P24539; -.
DR DMDM; 20455474; -.
DR PaxDb; P24539; -.
DR PeptideAtlas; P24539; -.
DR PRIDE; P24539; -.
DR Ensembl; ENST00000369722; ENSP00000358737; ENSG00000116459.
DR GeneID; 515; -.
DR KEGG; hsa:515; -.
DR UCSC; uc001ebc.3; human.
DR CTD; 515; -.
DR GeneCards; GC01P111991; -.
DR HGNC; HGNC:840; ATP5F1.
DR HPA; HPA046067; -.
DR MIM; 603270; gene.
DR neXtProt; NX_P24539; -.
DR PharmGKB; PA25130; -.
DR eggNOG; NOG245616; -.
DR HOGENOM; HOG000007163; -.
DR HOVERGEN; HBG050604; -.
DR InParanoid; P24539; -.
DR KO; K02127; -.
DR OMA; VINHETF; -.
DR OrthoDB; EOG7V4B02; -.
DR PhylomeDB; P24539; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; ATP5F1; -.
DR GenomeRNAi; 515; -.
DR NextBio; 2135; -.
DR PRO; PR:P24539; -.
DR ArrayExpress; P24539; -.
DR Bgee; P24539; -.
DR CleanEx; HS_ATP5F1; -.
DR Genevestigator; P24539; -.
DR GO; GO:0005759; C:mitochondrial matrix; NAS:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:RefGenome.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:RefGenome.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR InterPro; IPR008688; ATPase_B_chain/sub_B/MI25.
DR InterPro; IPR013837; ATPase_F0_sub_B/B_chain.
DR PANTHER; PTHR12733; PTHR12733; 1.
DR Pfam; PF05405; Mt_ATP-synt_B; 1.
PE 1: Evidence at protein level;
KW Acetylation; CF(0); Complete proteome; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Polymorphism; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1 42 Mitochondrion.
FT CHAIN 43 256 ATP synthase F(0) complex subunit B1,
FT mitochondrial.
FT /FTId=PRO_0000002513.
FT MOD_RES 139 139 N6-acetyllysine (By similarity).
FT MOD_RES 154 154 N6-acetyllysine (By similarity).
FT MOD_RES 162 162 N6-acetyllysine (By similarity).
FT MOD_RES 221 221 N6-acetyllysine.
FT MOD_RES 233 233 N6-acetyllysine.
FT MOD_RES 244 244 N6-acetyllysine (By similarity).
FT VARIANT 152 152 T -> M (in dbSNP:rs1264895).
FT /FTId=VAR_033534.
FT VARIANT 152 152 T -> N (in dbSNP:rs1264895).
FT /FTId=VAR_013176.
FT CONFLICT 84 84 I -> V (in Ref. 1; CAA42782).
FT CONFLICT 91 91 E -> G (in Ref. 3; AAH05960).
FT CONFLICT 194 194 K -> R (in Ref. 3; AAH05960).
SQ SEQUENCE 256 AA; 28909 MW; 743B1C54BFFEBBBD CRC64;
MLSRVVLSAA ATAAPSLKNA AFLGPGVLQA TRTFHTGQPH LVPVPPLPEY GGKVRYGLIP
EEFFQFLYPK TGVTGPYVLG TGLILYALSK EIYVISAETF TALSVLGVMV YGIKKYGPFV
ADFADKLNEQ KLAQLEEAKQ ASIQHIQNAI DTEKSQQALV QKRHYLFDVQ RNNIAMALEV
TYRERLYRVY KEVKNRLDYH ISVQNMMRRK EQEHMINWVE KHVVQSISTQ QEKETIAKCI
ADLKLLAKKA QAQPVM
//
MIM
603270
*RECORD*
*FIELD* NO
603270
*FIELD* TI
*603270 ATP SYNTHASE, H+ TRANSPORTING, MITOCHONDRIAL FO COMPLEX, SUBUNIT B,
ISOFORM 1; ATP5F1
read more*FIELD* TX
DESCRIPTION
The mitochondrial F1Fo-ATP synthase complex (EC 3.6.1.34) uses energy
derived from a proton gradient to synthesize ATP. The structure of this
complex has been referred to as a 'lollipop,' as the soluble F1
catalytic unit is attached to the mitochondrial inner membrane via the
Fo unit (summary by Walker, 1995).
The ATP5F1 gene encodes subunit B of the mitochondrial ATP synthase Fo
unit (Higuti et al., 1991).
CLONING
Higuti et al. (1991) cloned the human cDNA encoding human Fo subunit B.
The gene encodes a 214-amino acid mature polypeptide with a 42-amino
acid import signal.
*FIELD* RF
1. Higuti, T.; Tsurumi, C.; Osaka, F.; Kawamura, Y.; Tsujita, H.;
Yoshihara, Y.; Tani, I.; Tanaka, K.; Ichihara, A.: Molecular cloning
of cDNA for the import precursor of human subunit B of H(+)-ATP synthase
in mitochondria. Biochem. Biophys. Res. Commun. 178: 1014-1020,
1991.
2. Walker, J. E.: Determination of the structures of respiratory
enzyme complexes from mammalian mitochondria. Biochim. Biophys. Acta 1271:
221-227, 1995.
*FIELD* CD
Jennifer P. Macke: 11/10/1998
*FIELD* ED
carol: 06/14/2011
carol: 6/13/2011
alopez: 5/7/2010
alopez: 11/10/1998
*RECORD*
*FIELD* NO
603270
*FIELD* TI
*603270 ATP SYNTHASE, H+ TRANSPORTING, MITOCHONDRIAL FO COMPLEX, SUBUNIT B,
ISOFORM 1; ATP5F1
read more*FIELD* TX
DESCRIPTION
The mitochondrial F1Fo-ATP synthase complex (EC 3.6.1.34) uses energy
derived from a proton gradient to synthesize ATP. The structure of this
complex has been referred to as a 'lollipop,' as the soluble F1
catalytic unit is attached to the mitochondrial inner membrane via the
Fo unit (summary by Walker, 1995).
The ATP5F1 gene encodes subunit B of the mitochondrial ATP synthase Fo
unit (Higuti et al., 1991).
CLONING
Higuti et al. (1991) cloned the human cDNA encoding human Fo subunit B.
The gene encodes a 214-amino acid mature polypeptide with a 42-amino
acid import signal.
*FIELD* RF
1. Higuti, T.; Tsurumi, C.; Osaka, F.; Kawamura, Y.; Tsujita, H.;
Yoshihara, Y.; Tani, I.; Tanaka, K.; Ichihara, A.: Molecular cloning
of cDNA for the import precursor of human subunit B of H(+)-ATP synthase
in mitochondria. Biochem. Biophys. Res. Commun. 178: 1014-1020,
1991.
2. Walker, J. E.: Determination of the structures of respiratory
enzyme complexes from mammalian mitochondria. Biochim. Biophys. Acta 1271:
221-227, 1995.
*FIELD* CD
Jennifer P. Macke: 11/10/1998
*FIELD* ED
carol: 06/14/2011
carol: 6/13/2011
alopez: 5/7/2010
alopez: 11/10/1998