Full text data of ATP5B
ATP5B
(ATPMB, ATPSB)
[Confidence: high (present in two of the MS resources)]
ATP synthase subunit beta, mitochondrial; 3.6.3.14; Flags: Precursor
ATP synthase subunit beta, mitochondrial; 3.6.3.14; Flags: Precursor
hRBCD
IPI00303476
IPI00303476 ATP synthase beta chain, mitochondrial precursor ATP synthase beta chain, mitochondrial precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a 3 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a mitochondrial membrane n/a expected molecular weight found in band 98 kDa and 188 kDa
IPI00303476 ATP synthase beta chain, mitochondrial precursor ATP synthase beta chain, mitochondrial precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a 3 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a mitochondrial membrane n/a expected molecular weight found in band 98 kDa and 188 kDa
UniProt
P06576
ID ATPB_HUMAN Reviewed; 529 AA.
AC P06576; A8K4X0; Q14283;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1990, sequence version 3.
DT 22-JAN-2014, entry version 170.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=3.6.3.14;
DE Flags: Precursor;
GN Name=ATP5B; Synonyms=ATPMB, ATPSB;
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 [GENOMIC DNA].
RX PubMed=2687158; DOI=10.1016/0888-7543(89)90125-0;
RA Neckelmann N., Warner C.K., Chung A., Kudoh J., Minoshima S.,
RA Fukuyama R., Maekawa M., Shimizu Y., Shimizu N., Liu J.D.,
RA Wallace D.C.;
RT "The human ATP synthase beta subunit gene: sequence analysis,
RT chromosome assignment, and differential expression.";
RL Genomics 5:829-843(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-274.
RX PubMed=2900241;
RA Ohta S., Tomura H., Matsuda K., Kagawa Y.;
RT "Gene structure of the human mitochondrial adenosine triphosphate
RT synthase beta subunit.";
RL J. Biol. Chem. 263:11257-11262(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-274.
RX PubMed=2870059;
RA Ohta S., Kagawa Y.;
RT "Human F1-ATPase: molecular cloning of cDNA for the beta subunit.";
RL J. Biochem. 99:135-141(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 48-63.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [8]
RP PROTEIN SEQUENCE OF 95-121; 125-155; 189-198; 202-239; 242-259;
RP 265-279; 282-345; 388-422; 433-456 AND 490-519, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-529.
RX PubMed=2896550; DOI=10.1007/BF00434661;
RA Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A.,
RA Greenberg B.D.;
RT "Sequence analysis of cDNAs for the human and bovine ATP synthase beta
RT subunit: mitochondrial DNA genes sustain seventeen times more
RT mutations.";
RL Curr. Genet. 12:81-90(1987).
RN [10]
RP PROTEIN SEQUENCE OF 95-109; 282-294 AND 311-324.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/BJ20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at
RT the surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [11]
RP PROTEIN SEQUENCE OF 95-121; 125-155; 162-188; 202-239; 242-259;
RP 265-279; 282-345; 407-422 AND 463-480, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-198 AND LYS-426,
RP AND MASS 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 [13]
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. Subunits alpha and beta
CC form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to
CC hydrolysis of ATP in three separate catalytic sites on the beta
CC subunits.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC H(+)(Out).
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. Interacts with PPIF. Interacts with BCL2L1
CC isoform BCL-X(L); the interaction mediates the association of
CC BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0)
CC ATP synthase and enhances neurons metabolic efficency (By
CC similarity).
CC -!- INTERACTION:
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-356231, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC Note=Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
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DR EMBL; M27132; AAA51809.1; -; Genomic_DNA.
DR EMBL; M19483; AAA51808.1; -; Genomic_DNA.
DR EMBL; M19482; AAA51808.1; JOINED; Genomic_DNA.
DR EMBL; X03559; CAA27246.1; -; mRNA.
DR EMBL; D00022; BAA00016.1; -; mRNA.
DR EMBL; AK291085; BAF83774.1; -; mRNA.
DR EMBL; CH471054; EAW96952.1; -; Genomic_DNA.
DR EMBL; BC016512; AAH16512.1; -; mRNA.
DR EMBL; X05606; CAA29095.1; -; mRNA.
DR PIR; A33370; A33370.
DR RefSeq; NP_001677.2; NM_001686.3.
DR UniGene; Hs.406510; -.
DR ProteinModelPortal; P06576; -.
DR SMR; P06576; 60-525.
DR IntAct; P06576; 37.
DR MINT; MINT-5004016; -.
DR STRING; 9606.ENSP00000262030; -.
DR ChEMBL; CHEMBL2062350; -.
DR PhosphoSite; P06576; -.
DR DMDM; 114549; -.
DR DOSAC-COBS-2DPAGE; P06576; -.
DR OGP; P06576; -.
DR REPRODUCTION-2DPAGE; IPI00303476; -.
DR REPRODUCTION-2DPAGE; P06576; -.
DR SWISS-2DPAGE; P06576; -.
DR UCD-2DPAGE; P06576; -.
DR PaxDb; P06576; -.
DR PRIDE; P06576; -.
DR DNASU; 506; -.
DR Ensembl; ENST00000262030; ENSP00000262030; ENSG00000110955.
DR GeneID; 506; -.
DR KEGG; hsa:506; -.
DR UCSC; uc001slr.3; human.
DR CTD; 506; -.
DR GeneCards; GC12M057031; -.
DR HGNC; HGNC:830; ATP5B.
DR HPA; CAB017527; -.
DR HPA; HPA001520; -.
DR HPA; HPA001528; -.
DR MIM; 102910; gene.
DR neXtProt; NX_P06576; -.
DR PharmGKB; PA25122; -.
DR eggNOG; COG0055; -.
DR HOGENOM; HOG000009605; -.
DR HOVERGEN; HBG004307; -.
DR InParanoid; P06576; -.
DR KO; K02133; -.
DR OMA; EPYAKGG; -.
DR OrthoDB; EOG73V6K6; -.
DR PhylomeDB; P06576; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; ATP5B; human.
DR GeneWiki; ATP5B; -.
DR GenomeRNAi; 506; -.
DR NextBio; 2109; -.
DR PRO; PR:P06576; -.
DR ArrayExpress; P06576; -.
DR Bgee; P06576; -.
DR CleanEx; HS_ATP5B; -.
DR Genevestigator; P06576; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR Gene3D; 1.10.1140.10; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR005722; ATPase_F1-cplx_bsu.
DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR004100; ATPase_F1_a/bsu_N.
DR InterPro; IPR024034; ATPase_F1_bsu/V1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR15184:SF8; PTHR15184:SF8; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; SSF47917; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; ATP-binding; CF(1); Complete proteome;
KW Direct protein sequencing; Hydrogen ion transport; Hydrolase;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1 47 Mitochondrion.
FT CHAIN 48 529 ATP synthase subunit beta, mitochondrial.
FT /FTId=PRO_0000002443.
FT NP_BIND 206 213 ATP (By similarity).
FT MOD_RES 124 124 N6-acetyllysine (By similarity).
FT MOD_RES 133 133 N6-acetyllysine.
FT MOD_RES 161 161 N6-acetyllysine (By similarity).
FT MOD_RES 198 198 N6-acetyllysine.
FT MOD_RES 259 259 N6-acetyllysine (By similarity).
FT MOD_RES 264 264 N6-acetyllysine (By similarity).
FT MOD_RES 426 426 N6-acetyllysine.
FT MOD_RES 480 480 N6-acetyllysine (By similarity).
FT MOD_RES 485 485 N6-acetyllysine (By similarity).
FT MOD_RES 522 522 N6-acetyllysine (By similarity).
FT MOD_RES 529 529 Phosphoserine (By similarity).
FT VARIANT 274 274 E -> Q (in dbSNP:rs1042001).
FT /FTId=VAR_048371.
FT CONFLICT 1 6 MLGFVG -> MTSLWGKGTGCKLFKF (in Ref. 3;
FT BAA00016/CAA27246).
FT CONFLICT 36 40 APTAV -> VRRRF (in Ref. 2; AAA51808).
FT CONFLICT 36 40 APTAV -> VRRRS (in Ref. 3; BAA00016/
FT CAA27246).
FT CONFLICT 130 132 API -> DQL (in Ref. 2; AAA51808).
FT CONFLICT 378 378 H -> D (in Ref. 2; AAA51808).
FT CONFLICT 435 435 Q -> H (in Ref. 2; AAA51808).
SQ SEQUENCE 529 AA; 56560 MW; 960C616A2252B91A CRC64;
MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT SPSPKAGAAT
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV
RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHSS
//
ID ATPB_HUMAN Reviewed; 529 AA.
AC P06576; A8K4X0; Q14283;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1990, sequence version 3.
DT 22-JAN-2014, entry version 170.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=3.6.3.14;
DE Flags: Precursor;
GN Name=ATP5B; Synonyms=ATPMB, ATPSB;
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 [GENOMIC DNA].
RX PubMed=2687158; DOI=10.1016/0888-7543(89)90125-0;
RA Neckelmann N., Warner C.K., Chung A., Kudoh J., Minoshima S.,
RA Fukuyama R., Maekawa M., Shimizu Y., Shimizu N., Liu J.D.,
RA Wallace D.C.;
RT "The human ATP synthase beta subunit gene: sequence analysis,
RT chromosome assignment, and differential expression.";
RL Genomics 5:829-843(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-274.
RX PubMed=2900241;
RA Ohta S., Tomura H., Matsuda K., Kagawa Y.;
RT "Gene structure of the human mitochondrial adenosine triphosphate
RT synthase beta subunit.";
RL J. Biol. Chem. 263:11257-11262(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-274.
RX PubMed=2870059;
RA Ohta S., Kagawa Y.;
RT "Human F1-ATPase: molecular cloning of cDNA for the beta subunit.";
RL J. Biochem. 99:135-141(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 48-63.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [8]
RP PROTEIN SEQUENCE OF 95-121; 125-155; 189-198; 202-239; 242-259;
RP 265-279; 282-345; 388-422; 433-456 AND 490-519, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-529.
RX PubMed=2896550; DOI=10.1007/BF00434661;
RA Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A.,
RA Greenberg B.D.;
RT "Sequence analysis of cDNAs for the human and bovine ATP synthase beta
RT subunit: mitochondrial DNA genes sustain seventeen times more
RT mutations.";
RL Curr. Genet. 12:81-90(1987).
RN [10]
RP PROTEIN SEQUENCE OF 95-109; 282-294 AND 311-324.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/BJ20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at
RT the surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [11]
RP PROTEIN SEQUENCE OF 95-121; 125-155; 162-188; 202-239; 242-259;
RP 265-279; 282-345; 407-422 AND 463-480, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-198 AND LYS-426,
RP AND MASS 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 [13]
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. Subunits alpha and beta
CC form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to
CC hydrolysis of ATP in three separate catalytic sites on the beta
CC subunits.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC H(+)(Out).
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. Interacts with PPIF. Interacts with BCL2L1
CC isoform BCL-X(L); the interaction mediates the association of
CC BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0)
CC ATP synthase and enhances neurons metabolic efficency (By
CC similarity).
CC -!- INTERACTION:
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-356231, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC Note=Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
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DR EMBL; M27132; AAA51809.1; -; Genomic_DNA.
DR EMBL; M19483; AAA51808.1; -; Genomic_DNA.
DR EMBL; M19482; AAA51808.1; JOINED; Genomic_DNA.
DR EMBL; X03559; CAA27246.1; -; mRNA.
DR EMBL; D00022; BAA00016.1; -; mRNA.
DR EMBL; AK291085; BAF83774.1; -; mRNA.
DR EMBL; CH471054; EAW96952.1; -; Genomic_DNA.
DR EMBL; BC016512; AAH16512.1; -; mRNA.
DR EMBL; X05606; CAA29095.1; -; mRNA.
DR PIR; A33370; A33370.
DR RefSeq; NP_001677.2; NM_001686.3.
DR UniGene; Hs.406510; -.
DR ProteinModelPortal; P06576; -.
DR SMR; P06576; 60-525.
DR IntAct; P06576; 37.
DR MINT; MINT-5004016; -.
DR STRING; 9606.ENSP00000262030; -.
DR ChEMBL; CHEMBL2062350; -.
DR PhosphoSite; P06576; -.
DR DMDM; 114549; -.
DR DOSAC-COBS-2DPAGE; P06576; -.
DR OGP; P06576; -.
DR REPRODUCTION-2DPAGE; IPI00303476; -.
DR REPRODUCTION-2DPAGE; P06576; -.
DR SWISS-2DPAGE; P06576; -.
DR UCD-2DPAGE; P06576; -.
DR PaxDb; P06576; -.
DR PRIDE; P06576; -.
DR DNASU; 506; -.
DR Ensembl; ENST00000262030; ENSP00000262030; ENSG00000110955.
DR GeneID; 506; -.
DR KEGG; hsa:506; -.
DR UCSC; uc001slr.3; human.
DR CTD; 506; -.
DR GeneCards; GC12M057031; -.
DR HGNC; HGNC:830; ATP5B.
DR HPA; CAB017527; -.
DR HPA; HPA001520; -.
DR HPA; HPA001528; -.
DR MIM; 102910; gene.
DR neXtProt; NX_P06576; -.
DR PharmGKB; PA25122; -.
DR eggNOG; COG0055; -.
DR HOGENOM; HOG000009605; -.
DR HOVERGEN; HBG004307; -.
DR InParanoid; P06576; -.
DR KO; K02133; -.
DR OMA; EPYAKGG; -.
DR OrthoDB; EOG73V6K6; -.
DR PhylomeDB; P06576; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; ATP5B; human.
DR GeneWiki; ATP5B; -.
DR GenomeRNAi; 506; -.
DR NextBio; 2109; -.
DR PRO; PR:P06576; -.
DR ArrayExpress; P06576; -.
DR Bgee; P06576; -.
DR CleanEx; HS_ATP5B; -.
DR Genevestigator; P06576; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR Gene3D; 1.10.1140.10; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR005722; ATPase_F1-cplx_bsu.
DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR004100; ATPase_F1_a/bsu_N.
DR InterPro; IPR024034; ATPase_F1_bsu/V1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR15184:SF8; PTHR15184:SF8; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; SSF47917; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; ATP-binding; CF(1); Complete proteome;
KW Direct protein sequencing; Hydrogen ion transport; Hydrolase;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1 47 Mitochondrion.
FT CHAIN 48 529 ATP synthase subunit beta, mitochondrial.
FT /FTId=PRO_0000002443.
FT NP_BIND 206 213 ATP (By similarity).
FT MOD_RES 124 124 N6-acetyllysine (By similarity).
FT MOD_RES 133 133 N6-acetyllysine.
FT MOD_RES 161 161 N6-acetyllysine (By similarity).
FT MOD_RES 198 198 N6-acetyllysine.
FT MOD_RES 259 259 N6-acetyllysine (By similarity).
FT MOD_RES 264 264 N6-acetyllysine (By similarity).
FT MOD_RES 426 426 N6-acetyllysine.
FT MOD_RES 480 480 N6-acetyllysine (By similarity).
FT MOD_RES 485 485 N6-acetyllysine (By similarity).
FT MOD_RES 522 522 N6-acetyllysine (By similarity).
FT MOD_RES 529 529 Phosphoserine (By similarity).
FT VARIANT 274 274 E -> Q (in dbSNP:rs1042001).
FT /FTId=VAR_048371.
FT CONFLICT 1 6 MLGFVG -> MTSLWGKGTGCKLFKF (in Ref. 3;
FT BAA00016/CAA27246).
FT CONFLICT 36 40 APTAV -> VRRRF (in Ref. 2; AAA51808).
FT CONFLICT 36 40 APTAV -> VRRRS (in Ref. 3; BAA00016/
FT CAA27246).
FT CONFLICT 130 132 API -> DQL (in Ref. 2; AAA51808).
FT CONFLICT 378 378 H -> D (in Ref. 2; AAA51808).
FT CONFLICT 435 435 Q -> H (in Ref. 2; AAA51808).
SQ SEQUENCE 529 AA; 56560 MW; 960C616A2252B91A CRC64;
MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT SPSPKAGAAT
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV
RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHSS
//
MIM
102910
*RECORD*
*FIELD* NO
102910
*FIELD* TI
*102910 ATP SYNTHASE, H+ TRANSPORTING, MITOCHONDRIAL F1 COMPLEX, BETA SUBUNIT;
ATP5B
read more;;MITOCHONDRIAL ATP SYNTHASE, BETA SUBUNIT; ATPMB;;
ATPSB
*FIELD* TX
DESCRIPTION
Mitochondrial ATP synthase catalyzes ATP formation, using the energy of
proton flux through the inner membrane during oxidative phosphorylation.
Two subunits of the enzyme are encoded by mitochondrial genes and the
others by nuclear genes. The beta subunit of mitochondrial ATP synthase
is encoded by a nuclear gene (summary by Ohta et al., 1988).
CLONING
Ohta et al. (1988) cloned a cDNA of the human beta subunit of ATP
synthase.
Neckelmann et al. (1989, 1989) sequenced the human ATP synthase
beta-subunit gene and demonstrated that it is preferentially expressed
in heart and skeletal muscle. The gene encodes a leader peptide of 49
amino acids and a mature protein of 480 amino acids.
GENE STRUCTURE
Ohta et al. (1988) determined that the ATP5B gene contains 10 exons,
with the first exon corresponding to the noncoding region and most of
the presequence that targets this protein to the mitochondria.
MAPPING
Kudoh et al. (1989) assigned the ATPMB locus to the p13-qter region of
human chromosome 12 by analysis of human-mouse somatic cell hybrid DNA
and by use of flow-sorted chromosomes. They assigned 2 related
sequences, ATPMBL1 and ATPMBL2, to chromosome 2 and 17, respectively.
GENE FUNCTION
Martinez et al. (2003) identified ATP5B as a high affinity HDL receptor
for apolipoprotein A1 (107680). They used a variety of experimental
approaches to confirm this ectopic localization of components of the ATP
synthase complex and the presence of ATP hydrolase activity at the
hepatocyte cell surface. Receptor stimulation by apoA-I triggers the
endocytosis of holo-HDL particles (protein plus lipid) by a mechanism
that depends strictly on the generation of ADP. Martinez et al. (2003)
confirmed this effect on endocytosis in perfused rat liver ex vivo by
using a specific inhibitor of ATP synthase. Thus, Martinez et al. (2003)
concluded that membrane-bound ATP synthase has a previously unsuspected
role in modulating the concentrations of extracellular ADP and is
regulated by a principal plasma apolipoprotein.
ANIMAL MODEL
Kim et al. (2012) found that the Gsto1a isoform of Drosophila Gsto1
(605482) modified Atp5b by glutathionylation and enhanced mitochondrial
ATPase synthase assembly and activity. Parkin (PARK2; 602544) mutant
flies showed reduced expression of both Gsto1 and Atp5b and reduced
ATPase function compared with controls. Overexpression of Gsto1 enhanced
mitochondrial ATPase function and partially reversed the phenotype of
parkin mutant flies, including degeneration of dopaminergic neurons and
muscle, cellular tubulin (see 602529) accumulation, and endoplasmic
reticulum stress. Knockdown of Atp5b in flies via RNA interference
induced some of the parkin mutant phenotype.
*FIELD* RF
1. Kim, K.; Kim, S.-H.; Kim, J.; Kim, H.; Yim, J.: Glutathione S-transferase
omega 1 activity is sufficient to suppress neurodegeneration in a
Drosophila model of Parkinson disease. J. Biol. Chem. 287: 6628-6641,
2012.
2. Kudoh, J.; Minoshima, S.; Fukuyama, R.; Maekawa, M.; Neckelmann,
N.; Wallace, D. C.; Shimizu, Y.; Shimizu, N.: Assignment of ATP synthase
beta subunit (ATPMB) gene to the p13-qter region of human chromosome
12. (Abstract) Cytogenet. Cell Genet. 51: 1026 only, 1989.
3. Martinez, L. O.; Jacquet, S.; Esteve, J.-P.; Rolland, C.; Cabezon,
E.; Champagne, E.; Pineau, T.; Georgeaud, V.; Walker, J. E.; Terce,
F.; Collet, X.; Perret, B.; Barbaras, R.: Ectopic beta-chain of ATP
synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis. Nature 421:
75-79, 2003.
4. Neckelmann, N.; Warner, C. K.; Chung, A.; Kudoh, J.; Minoshima,
S.; Fukuyama, R.; Maekawa, M.; Shimizu, Y.; Shimizu, N.; Liu, J. D.;
Wallace, D. C.: The human ATP synthase beta subunit gene: sequence
analysis, chromosome assignment, and differential expression. Genomics 5:
829-843, 1989.
5. Neckelmann, N. S.; Chung, A. B.; Warner, C. K.; Hodge, J. A.; Wallace,
D. C.: The human ATP synthase beta subunit gene has been sequenced
and shown to be preferentially expressed in heart and skeletal muscle.
(Abstract) Cytogenet. Cell Genet. 51: 1051 only, 1989.
6. Ohta, S.; Tomura, H.; Matsuda, K.; Kagawa, Y.: Gene structure
of the human mitochondrial adenosine triphosphate synthase beta subunit. J.
Biol. Chem. 263: 11257-11262, 1988.
*FIELD* CN
Patricia A. Hartz - updated: 10/19/2012
Ada Hamosh - updated: 2/3/2003
*FIELD* CD
Victor A. McKusick: 10/10/1988
*FIELD* ED
mgross: 11/09/2012
terry: 10/19/2012
carol: 6/14/2011
alopez: 3/24/2004
terry: 3/23/2004
alopez: 2/4/2003
terry: 2/3/2003
alopez: 10/15/1998
carol: 6/24/1998
psherman: 6/22/1998
alopez: 7/17/1997
jason: 7/29/1994
supermim: 3/16/1992
carol: 2/7/1991
supermim: 3/20/1990
carol: 12/14/1989
ddp: 10/27/1989
*RECORD*
*FIELD* NO
102910
*FIELD* TI
*102910 ATP SYNTHASE, H+ TRANSPORTING, MITOCHONDRIAL F1 COMPLEX, BETA SUBUNIT;
ATP5B
read more;;MITOCHONDRIAL ATP SYNTHASE, BETA SUBUNIT; ATPMB;;
ATPSB
*FIELD* TX
DESCRIPTION
Mitochondrial ATP synthase catalyzes ATP formation, using the energy of
proton flux through the inner membrane during oxidative phosphorylation.
Two subunits of the enzyme are encoded by mitochondrial genes and the
others by nuclear genes. The beta subunit of mitochondrial ATP synthase
is encoded by a nuclear gene (summary by Ohta et al., 1988).
CLONING
Ohta et al. (1988) cloned a cDNA of the human beta subunit of ATP
synthase.
Neckelmann et al. (1989, 1989) sequenced the human ATP synthase
beta-subunit gene and demonstrated that it is preferentially expressed
in heart and skeletal muscle. The gene encodes a leader peptide of 49
amino acids and a mature protein of 480 amino acids.
GENE STRUCTURE
Ohta et al. (1988) determined that the ATP5B gene contains 10 exons,
with the first exon corresponding to the noncoding region and most of
the presequence that targets this protein to the mitochondria.
MAPPING
Kudoh et al. (1989) assigned the ATPMB locus to the p13-qter region of
human chromosome 12 by analysis of human-mouse somatic cell hybrid DNA
and by use of flow-sorted chromosomes. They assigned 2 related
sequences, ATPMBL1 and ATPMBL2, to chromosome 2 and 17, respectively.
GENE FUNCTION
Martinez et al. (2003) identified ATP5B as a high affinity HDL receptor
for apolipoprotein A1 (107680). They used a variety of experimental
approaches to confirm this ectopic localization of components of the ATP
synthase complex and the presence of ATP hydrolase activity at the
hepatocyte cell surface. Receptor stimulation by apoA-I triggers the
endocytosis of holo-HDL particles (protein plus lipid) by a mechanism
that depends strictly on the generation of ADP. Martinez et al. (2003)
confirmed this effect on endocytosis in perfused rat liver ex vivo by
using a specific inhibitor of ATP synthase. Thus, Martinez et al. (2003)
concluded that membrane-bound ATP synthase has a previously unsuspected
role in modulating the concentrations of extracellular ADP and is
regulated by a principal plasma apolipoprotein.
ANIMAL MODEL
Kim et al. (2012) found that the Gsto1a isoform of Drosophila Gsto1
(605482) modified Atp5b by glutathionylation and enhanced mitochondrial
ATPase synthase assembly and activity. Parkin (PARK2; 602544) mutant
flies showed reduced expression of both Gsto1 and Atp5b and reduced
ATPase function compared with controls. Overexpression of Gsto1 enhanced
mitochondrial ATPase function and partially reversed the phenotype of
parkin mutant flies, including degeneration of dopaminergic neurons and
muscle, cellular tubulin (see 602529) accumulation, and endoplasmic
reticulum stress. Knockdown of Atp5b in flies via RNA interference
induced some of the parkin mutant phenotype.
*FIELD* RF
1. Kim, K.; Kim, S.-H.; Kim, J.; Kim, H.; Yim, J.: Glutathione S-transferase
omega 1 activity is sufficient to suppress neurodegeneration in a
Drosophila model of Parkinson disease. J. Biol. Chem. 287: 6628-6641,
2012.
2. Kudoh, J.; Minoshima, S.; Fukuyama, R.; Maekawa, M.; Neckelmann,
N.; Wallace, D. C.; Shimizu, Y.; Shimizu, N.: Assignment of ATP synthase
beta subunit (ATPMB) gene to the p13-qter region of human chromosome
12. (Abstract) Cytogenet. Cell Genet. 51: 1026 only, 1989.
3. Martinez, L. O.; Jacquet, S.; Esteve, J.-P.; Rolland, C.; Cabezon,
E.; Champagne, E.; Pineau, T.; Georgeaud, V.; Walker, J. E.; Terce,
F.; Collet, X.; Perret, B.; Barbaras, R.: Ectopic beta-chain of ATP
synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis. Nature 421:
75-79, 2003.
4. Neckelmann, N.; Warner, C. K.; Chung, A.; Kudoh, J.; Minoshima,
S.; Fukuyama, R.; Maekawa, M.; Shimizu, Y.; Shimizu, N.; Liu, J. D.;
Wallace, D. C.: The human ATP synthase beta subunit gene: sequence
analysis, chromosome assignment, and differential expression. Genomics 5:
829-843, 1989.
5. Neckelmann, N. S.; Chung, A. B.; Warner, C. K.; Hodge, J. A.; Wallace,
D. C.: The human ATP synthase beta subunit gene has been sequenced
and shown to be preferentially expressed in heart and skeletal muscle.
(Abstract) Cytogenet. Cell Genet. 51: 1051 only, 1989.
6. Ohta, S.; Tomura, H.; Matsuda, K.; Kagawa, Y.: Gene structure
of the human mitochondrial adenosine triphosphate synthase beta subunit. J.
Biol. Chem. 263: 11257-11262, 1988.
*FIELD* CN
Patricia A. Hartz - updated: 10/19/2012
Ada Hamosh - updated: 2/3/2003
*FIELD* CD
Victor A. McKusick: 10/10/1988
*FIELD* ED
mgross: 11/09/2012
terry: 10/19/2012
carol: 6/14/2011
alopez: 3/24/2004
terry: 3/23/2004
alopez: 2/4/2003
terry: 2/3/2003
alopez: 10/15/1998
carol: 6/24/1998
psherman: 6/22/1998
alopez: 7/17/1997
jason: 7/29/1994
supermim: 3/16/1992
carol: 2/7/1991
supermim: 3/20/1990
carol: 12/14/1989
ddp: 10/27/1989