ID ATPB_MOUSE Reviewed; 529 AA.
AC P56480; Q0QEP4; Q3TFD7; Q3TIP9; Q3TK44; Q3TWD5; Q3TX28; Q3U6U4; Q3U774;
AC Q3UB69; Q3UF69; Q8CI65; Q8VEJ5; Q9CTI7; Q9CWX7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 27-NOV-2024, entry version 220.
DE RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000305};
DE EC=7.1.2.2;
DE AltName: Full=ATP synthase F1 subunit beta {ECO:0000250|UniProtKB:P06576};
DE Flags: Precursor;
GN Name=Atp5f1b {ECO:0000250|UniProtKB:P06576}; Synonyms=Atp5b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=10657236; DOI=10.1042/bj3460033;
RA Andersson U., Antonicka H., Houstek J., Cannon B.;
RT "A novel principle for conferring selectivity to poly(A)-binding proteins:
RT interdependence of two ATP synthase beta-subunit mRNA-binding proteins.";
RL Biochem. J. 346:33-39(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Amnion, Bone marrow, Embryonic stem cell, Heart, Kidney, Liver,
RC Spinal ganglion, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N;
RC TISSUE=Mammary tumor, Retina, and Salivary gland;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 65-509.
RC TISSUE=Liver;
RX PubMed=16751257; DOI=10.1093/molbev/msl027;
RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL Mol. Biol. Evol. 23:1493-1503(2006).
RN [5]
RP PROTEIN SEQUENCE OF 95-121; 125-155; 162-198; 202-239; 242-259; 265-279;
RP 282-345; 352-422; 433-456 AND 463-489, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH S100A1, AND FUNCTION.
RX PubMed=17438143; DOI=10.1128/mcb.02045-06;
RA Boerries M., Most P., Gledhill J.R., Walker J.E., Katus H.A., Koch W.J.,
RA Aebi U., Schoenenberger C.A.;
RT "Ca2+ -dependent interaction of S100A1 with F1-ATPase leads to an increased
RT ATP content in cardiomyocytes.";
RL Mol. Cell. Biol. 27:4365-4373(2007).
RN [8]
RP INTERACTION WITH CLN5 AND PPT1.
RX PubMed=19941651; DOI=10.1186/1471-2121-10-83;
RA Lyly A., von Schantz C., Heine C., Schmiedt M.L., Sipilae T., Jalanko A.,
RA Kyttaelae A.;
RT "Novel interactions of CLN5 support molecular networking between neuronal
RT ceroid lipofuscinosis proteins.";
RL BMC Cell Biol. 10:83-83(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-312, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH PPIF, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21281446; DOI=10.1111/j.1742-4658.2011.08026.x;
RA Chinopoulos C., Konrad C., Kiss G., Metelkin E., Torocsik B., Zhang S.F.,
RA Starkov A.A.;
RT "Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix
RT adenine nucleotide levels.";
RL FEBS J. 278:1112-1125(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-522, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-124; LYS-133; LYS-161; LYS-259; LYS-264 AND LYS-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124; LYS-133; LYS-161; LYS-198;
RP LYS-259; LYS-264; LYS-426; LYS-480; LYS-485 AND LYS-522, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(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. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits.
CC {ECO:0000269|PubMed:17438143, ECO:0000269|PubMed:21281446}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out);
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000269|PubMed:21281446};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57722;
CC Evidence={ECO:0000305|PubMed:21281446};
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 PPIF (PubMed:21281446).
CC Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the
CC association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane
CC F(1)F(0) ATP synthase and enhances neurons metabolic efficiency (By
CC similarity). Interacts with CLN5 and PPT1 (PubMed:19941651). Interacts
CC with S100A1; this interaction increases F1-ATPase activity
CC (PubMed:17438143). Interacts with MTLN (By similarity). Interacts with
CC TTC5/STRAP; the interaction results in decreased mitochondrial ATP
CC production (By similarity). {ECO:0000250|UniProtKB:P00829,
CC ECO:0000250|UniProtKB:P06576, ECO:0000250|UniProtKB:P10719,
CC ECO:0000269|PubMed:17438143, ECO:0000269|PubMed:19941651,
CC ECO:0000269|PubMed:21281446}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17438143}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17438143}; Matrix side
CC {ECO:0000250|UniProtKB:P00829}.
CC -!- PTM: Acetylation of Lys-133 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37127.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF030559; AAB86421.1; -; mRNA.
DR EMBL; AK003460; BAB22802.1; -; mRNA.
DR EMBL; AK010314; BAB26846.1; -; mRNA.
DR EMBL; AK084009; BAC39095.1; -; mRNA.
DR EMBL; AK145684; BAE26587.1; -; mRNA.
DR EMBL; AK148891; BAE28692.1; -; mRNA.
DR EMBL; AK150599; BAE29691.1; -; mRNA.
DR EMBL; AK151081; BAE30095.1; -; mRNA.
DR EMBL; AK151600; BAE30540.1; -; mRNA.
DR EMBL; AK152788; BAE31497.1; -; mRNA.
DR EMBL; AK152976; BAE31630.1; -; mRNA.
DR EMBL; AK153099; BAE31720.1; -; mRNA.
DR EMBL; AK159444; BAE35088.1; -; mRNA.
DR EMBL; AK159737; BAE35331.1; -; mRNA.
DR EMBL; AK159978; BAE35529.1; -; mRNA.
DR EMBL; AK160199; BAE35689.1; -; mRNA.
DR EMBL; AK160608; BAE35911.1; -; mRNA.
DR EMBL; AK164383; BAE37764.1; -; mRNA.
DR EMBL; AK166525; BAE38829.1; -; mRNA.
DR EMBL; AK166603; BAE38888.1; -; mRNA.
DR EMBL; AK166979; BAE39161.1; -; mRNA.
DR EMBL; AK167119; BAE39267.1; -; mRNA.
DR EMBL; AK167160; BAE39301.1; -; mRNA.
DR EMBL; AK167728; BAE39769.1; -; mRNA.
DR EMBL; AK167764; BAE39797.1; -; mRNA.
DR EMBL; AK168692; BAE40537.1; -; mRNA.
DR EMBL; AK168941; BAE40749.1; -; mRNA.
DR EMBL; AK169184; BAE40961.1; -; mRNA.
DR EMBL; BC018392; AAH18392.1; -; mRNA.
DR EMBL; BC037127; AAH37127.1; ALT_INIT; mRNA.
DR EMBL; BC046616; AAH46616.1; -; mRNA.
DR EMBL; DQ403100; ABD77233.1; -; mRNA.
DR CCDS; CCDS24259.1; -.
DR RefSeq; NP_058054.2; NM_016774.3.
DR AlphaFoldDB; P56480; -.
DR SMR; P56480; -.
DR BioGRID; 198254; 66.
DR IntAct; P56480; 37.
DR MINT; P56480; -.
DR STRING; 10090.ENSMUSP00000026459; -.
DR CarbonylDB; P56480; -.
DR GlyCosmos; P56480; 1 site, No reported glycans.
DR GlyGen; P56480; 4 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P56480; -.
DR MetOSite; P56480; -.
DR PhosphoSitePlus; P56480; -.
DR SwissPalm; P56480; -.
DR REPRODUCTION-2DPAGE; IPI00468481; -.
DR REPRODUCTION-2DPAGE; P56480; -.
DR CPTAC; non-CPTAC-3766; -.
DR jPOST; P56480; -.
DR PaxDb; 10090-ENSMUSP00000026459; -.
DR PeptideAtlas; P56480; -.
DR ProteomicsDB; 277217; -.
DR Pumba; P56480; -.
DR TopDownProteomics; P56480; -.
DR Antibodypedia; 877; 559 antibodies from 36 providers.
DR DNASU; 11947; -.
DR Ensembl; ENSMUST00000026459.6; ENSMUSP00000026459.6; ENSMUSG00000025393.13.
DR GeneID; 11947; -.
DR KEGG; mmu:11947; -.
DR UCSC; uc007hle.1; mouse.
DR AGR; MGI:107801; -.
DR CTD; 506; -.
DR MGI; MGI:107801; Atp5f1b.
DR VEuPathDB; HostDB:ENSMUSG00000025393; -.
DR eggNOG; KOG1350; Eukaryota.
DR GeneTree; ENSGT00550000074800; -.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; P56480; -.
DR OMA; VRCIMLA; -.
DR OrthoDB; 3420200at2759; -.
DR PhylomeDB; P56480; -.
DR TreeFam; TF105640; -.
DR Reactome; R-MMU-1268020; Mitochondrial protein import.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR Reactome; R-MMU-9837999; Mitochondrial protein degradation.
DR BioGRID-ORCS; 11947; 31 hits in 81 CRISPR screens.
DR ChiTaRS; Atp5b; mouse.
DR PRO; PR:P56480; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P56480; protein.
DR Bgee; ENSMUSG00000025393; Expressed in right kidney and 266 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0043532; F:angiostatin binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042288; F:MHC class I protein binding; IEA:Ensembl.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IMP:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; IEA:Ensembl.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR FunFam; 1.10.1140.10:FF:000001; ATP synthase subunit beta; 1.
DR FunFam; 2.40.10.170:FF:000004; ATP synthase subunit beta; 1.
DR FunFam; 3.40.50.12240:FF:000006; ATP synthase subunit beta; 1.
DR FunFam; 3.40.50.300:FF:000026; ATP synthase subunit beta; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR055190; ATP-synt_VA_C.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR050053; ATPase_alpha/beta_chains.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF22919; ATP-synt_VA_C; 1.
DR PIRSF; PIRSF039072; ATPase_subunit_beta; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Glycoprotein; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transit peptide; Translocase;
KW Transport.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT CHAIN 47..529
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002444"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 133
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 133
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 161
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 161
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 259
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 264
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 264
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10719"
FT MOD_RES 480
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 485
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 522
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 522
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT CARBOHYD 106
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 25
FT /note="A -> V (in Ref. 1; AAB86421)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="A -> V (in Ref. 2; BAE35088)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="D -> G (in Ref. 2; BAE40961)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="D -> E (in Ref. 1; AAB86421)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="I -> V (in Ref. 2; BAE31497)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="R -> K (in Ref. 1; AAB86421)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="Q -> R (in Ref. 2; BAE38888/BAE39301)"
FT /evidence="ECO:0000305"
FT CONFLICT 279..280
FT /note="RA -> PT (in Ref. 1; AAB86421)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="T -> A (in Ref. 2; BAE31497/BAE31630)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="T -> N (in Ref. 2; BAE30095)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="T -> S (in Ref. 2; BAB22802)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..434
FT /note="SL -> FF (in Ref. 1; AAB86421)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="Q -> H (in Ref. 2; BAB22802)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="Q -> R (in Ref. 2; BAE39797)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="A -> V (in Ref. 2; BAE35331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 56300 MW; F3E1100C390A78A7 CRC64;
MLSLVGRVAS ASASGALRGL SPSAALPQAQ LLLRAAPAGV HPARDYAAQA SAAPKAGTAT
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RDSRLVLEVA QHLGESTVRT IAMDGTEGLV
RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFIEMSVEQ
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGNEHYDV
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHGS
//
