ID ATPB_HUMAN Reviewed; 529 AA. AC P06576; A8K4X0; Q14283; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 3. DT 04-NOV-2026, entry version 266. DE RecName: Full=ATP synthase F(1) complex subunit beta, mitochondrial {ECO:0000305}; DE EC=7.1.2.2 {ECO:0000305|PubMed:25168243}; DE AltName: Full=ATP synthase F1 subunit beta {ECO:0000312|HGNC:HGNC:830}; DE Flags: Precursor; GN Name=ATP5F1B {ECO:0000312|HGNC:HGNC:830}; GN Synonyms=ATP5B {ECO:0000312|HGNC:HGNC:830}, ATPMB, ATPSB GN {ECO:0000312|HGNC:HGNC:830}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., Fukuyama R., RA Maekawa M., Shimizu Y., Shimizu N., Liu J.D., Wallace D.C.; RT "The human ATP synthase beta subunit gene: sequence analysis, chromosome RT assignment, and differential expression."; RL Genomics 5:829-843(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-274. RX PubMed=2900241; DOI=10.1016/s0021-9258(18)37950-x; RA Ohta S., Tomura H., Matsuda K., Kagawa Y.; RT "Gene structure of the human mitochondrial adenosine triphosphate synthase RT beta subunit."; RL J. Biol. Chem. 263:11257-11262(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-274. RX PubMed=2870059; DOI=10.1093/oxfordjournals.jbchem.a135452; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 labeling of RT 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; 265-279; RP 282-345; 388-422; 433-456 AND 490-519, AND IDENTIFICATION BY MASS RP 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 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 the RT 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; 265-279; RP 282-345; 407-422 AND 463-480, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAR-2005) to UniProtKB. RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-198 AND LYS-426, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA 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 [14] 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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-529, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP SUBCELLULAR LOCATION, INTERACTION WITH TTC5, FUNCTION, AND CATALYTIC RP ACTIVITY. RX PubMed=25168243; DOI=10.1038/cdd.2014.135; RA Maniam S., Coutts A.S., Stratford M.R., McGouran J., Kessler B., RA La Thangue N.B.; RT "Cofactor Strap regulates oxidative phosphorylation and mitochondrial p53 RT activity through ATP synthase."; RL Cell Death Differ. 22:156-163(2015). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [19] RP INTERACTION WITH MTLN. RX PubMed=32243843; DOI=10.1016/j.stemcr.2020.03.002; RA Friesen M., Warren C.R., Yu H., Toyohara T., Ding Q., Florido M.H.C., RA Sayre C., Pope B.D., Goff L.A., Rinn J.L., Cowan C.A.; RT "Mitoregulin Controls beta-Oxidation in Human and Mouse Adipocytes."; RL Stem Cell Reports 14:590-602(2020). RN [20] RP INTERACTION WITH MIMS2. RX PubMed=36374104; DOI=10.1128/mcb.00143-22; RA Suzuki C., Fujiwara T., Shima H., Ono K., Saito K., Kato H., Onodera K., RA Ichikawa S., Fukuhara N., Onishi Y., Yokoyama H., Nakamura Y., Igarashi K., RA Harigae H.; RT "Elucidation of the Role of FAM210B in Mitochondrial Metabolism and RT Erythropoiesis."; RL Mol. Cell. Biol. 42:e0014322-e0014322(2022). RN [21] {ECO:0007744|PDB:8H9E, ECO:0007744|PDB:8H9I, ECO:0007744|PDB:8H9L, ECO:0007744|PDB:8H9P, ECO:0007744|PDB:8H9S, ECO:0007744|PDB:8H9T, ECO:0007744|PDB:8H9U, ECO:0007744|PDB:8H9V} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH ADP AND MG(2+), RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX, FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, AND SUBUNIT. RX PubMed=37244256; DOI=10.1016/j.molcel.2023.04.029; RA Lai Y., Zhang Y., Zhou S., Xu J., Du Z., Feng Z., Yu L., Zhao Z., Wang W., RA Tang Y., Yang X., Guddat L.W., Liu F., Gao Y., Rao Z., Gong H.; RT "Structure of the human ATP synthase."; RL Mol. Cell 83:2137-2147.e4(2023). RN [22] RP INVOLVEMENT IN HUMOP2, VARIANT HUMOP2 PRO-335, FUNCTION, AND RP CHARACTERIZATION OF VARIANT HUMOP2 PRO-335. RX PubMed=36239646; DOI=10.1056/nejmoa2202949; RA Ganetzky R.D., Markhard A.L., Yee I., Clever S., Cahill A., Shah H., RA Grabarek Z., To T.L., Mootha V.K.; RT "Congenital hypermetabolism and uncoupled oxidative phosphorylation."; RL N. Engl. J. Med. 387:1395-1403(2022). RN [23] RP VARIANT VAL-130. RX PubMed=25787250; DOI=10.1073/pnas.1503696112; RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W., RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P., RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P., RA Lifton R.P.; RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in RT insulin-producing adenomas."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015). RN [24] RP VARIANTS DYT38 PRO-334 AND ALA-482, AND INVOLVEMENT IN DYT38. RX PubMed=36860166; DOI=10.1093/brain/awad068; RA Nasca A., Mencacci N.E., Invernizzi F., Zech M., Keller Sarmiento I.J., RA Legati A., Frascarelli C., Bustos B.I., Romito L.M., Krainc D., RA Winkelmann J., Carecchio M., Nardocci N., Zorzi G., Prokisch H., RA Lubbe S.J., Garavaglia B., Ghezzi D.; RT "Variants in ATP5F1B are associated with dominantly inherited dystonia."; RL Brain 146:2730-2738(2023). CC -!- FUNCTION: Catalytic subunit beta, of the mitochondrial membrane ATP CC synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP CC from ADP in the presence of a proton gradient across the membrane which CC is generated by electron transport complexes of the respiratory chain CC (Probable) (PubMed:37244256). ATP synthase complex consist of a soluble CC F(1) head domain - the catalytic core - and a membrane F(1) domain CC - the membrane proton channel (PubMed:37244256). These two domains are CC linked by a central stalk rotating inside the F(1) region and a CC stationary peripheral stalk (PubMed:37244256). During catalysis, ATP CC synthesis in the catalytic domain of F(1) is coupled via a rotary CC mechanism of the central stalk subunits to proton translocation CC (Probable). In vivo, can only synthesize ATP although its ATP hydrolase CC activity can be activated artificially in vitro (By similarity). With CC the subunit alpha (ATP5F1A), forms the catalytic core in the F(1) CC domain (PubMed:37244256). {ECO:0000250|UniProtKB:P19483, CC ECO:0000269|PubMed:37244256, ECO:0000305|PubMed:25168243, CC ECO:0000305|PubMed:36239646, ECO:0000305|PubMed:37244256}. 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:0000305|PubMed:25168243, ECO:0000305|PubMed:37244256}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57722; CC Evidence={ECO:0000305|PubMed:25168243, ECO:0000305|PubMed:37244256}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000305|PubMed:37244256}; CC -!- SUBUNIT: Homotrimer (PubMed:37244256). Component of the ATP synthase CC complex composed at least of ATP5F1A/subunit alpha, ATP5F1B/subunit CC beta, ATP5MC1/subunit c (homooctamer), MT-ATP6/subunit a, MT- CC ATP8/subunit 8, ATP5ME/subunit e, ATP5MF/subunit f, ATP5MG/subunit g, CC ATP5MK/subunit k, ATP5MJ/subunit j, ATP5F1C/subunit gamma, CC ATP5F1D/subunit delta, ATP5F1E/subunit epsilon, ATP5PF/subunit F6, CC ATP5PB/subunit b, ATP5PD/subunit d, ATP5PO/subunit OSCP CC (PubMed:37244256). ATP synthase complex consists of a soluble F(1) head CC domain (subunits alpha(3) and beta(3)) - the catalytic core - and a CC membrane F(0) domain - the membrane proton channel (subunits c, a, 8, CC e, f, g, k and j) (PubMed:37244256). These two domains are linked by a CC central stalk (subunits gamma, delta, and epsilon) rotating inside the CC F1 region and a stationary peripheral stalk (subunits F6, b, d, and CC OSCP) (PubMed:37244256). Interacts with PPIF (By similarity). Interacts CC with BCL2L1 isoform BCL-X(L); the interaction mediates the association CC of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP CC synthase and enhances neurons metabolic efficiency (By similarity). CC Interacts with CLN5 and PPT1 (By similarity). Interacts with S100A1; CC this interaction increases F1-ATPase activity (By similarity). CC Interacts with MTLN (PubMed:32243843). Interacts with TTC5/STRAP; the CC interaction results in decreased mitochondrial ATP production CC (PubMed:25168243). Interacts with MIMS2; the interaction regulates CC mitochondrial energy metabolism (PubMed:36374104). CC {ECO:0000250|UniProtKB:P10719, ECO:0000250|UniProtKB:P56480, CC ECO:0000269|PubMed:25168243, ECO:0000269|PubMed:32243843, CC ECO:0000269|PubMed:36374104, ECO:0000269|PubMed:37244256}. CC -!- INTERACTION: CC P06576; P25705: ATP5F1A; NbExp=8; IntAct=EBI-356231, EBI-351437; CC P06576; P36542: ATP5F1C; NbExp=3; IntAct=EBI-356231, EBI-711768; CC P06576; Q9UII2: ATP5IF1; NbExp=5; IntAct=EBI-356231, EBI-718459; CC P06576; O75947: ATP5PD; NbExp=3; IntAct=EBI-356231, EBI-724024; CC P06576; Q5TC12: ATPAF1; NbExp=4; IntAct=EBI-356231, EBI-1166891; CC P06576; Q8N5M1: ATPAF2; NbExp=9; IntAct=EBI-356231, EBI-1166928; CC P06576; P54253: ATXN1; NbExp=3; IntAct=EBI-356231, EBI-930964; CC P06576; Q13895: BYSL; NbExp=3; IntAct=EBI-356231, EBI-358049; CC P06576; P28566: HTR1E; NbExp=2; IntAct=EBI-356231, EBI-1043151; CC P06576; Q8N448: LNX2; NbExp=4; IntAct=EBI-356231, EBI-2340947; CC P06576; Q5T1Q4: SLC35F1; NbExp=3; IntAct=EBI-356231, EBI-13365456; CC P06576; P63104: YWHAZ; NbExp=2; IntAct=EBI-356231, EBI-347088; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:25168243}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P00829}; Matrix side CC {ECO:0000250|UniProtKB:P00829, ECO:0000269|PubMed:25168243}. CC -!- DISEASE: Hypermetabolism due to uncoupled mitochondrial oxidative CC phosphorylation 2 (HUMOP2) [MIM:620085]: A disorder apparent in infancy CC and characterized by euthyroid hypermetabolism, failure to thrive CC despite excessive caloric intake, intermittent hyperthermia, and CC developmental delay. {ECO:0000269|PubMed:36239646}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Dystonia 38 (DYT38) [MIM:621502]: A form of dystonia, a CC disorder defined by the presence of sustained involuntary muscle CC contraction, often leading to abnormal postures. DYT38 is an autosomal CC dominant form with incomplete penetrance characterized by the onset of CC focal dystonia in childhood or the early teenage years. CC {ECO:0000269|PubMed:36860166}. Note=Disease susceptibility may be CC associated with variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {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; 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 CCDS; CCDS8924.1; -. DR PIR; A33370; A33370. DR RefSeq; NP_001677.2; NM_001686.4. DR PDB; 8H9E; EM; 2.53 A; D/E/F=48-529. DR PDB; 8H9I; EM; 2.77 A; D/E/F=48-529. DR PDB; 8H9L; EM; 2.61 A; D/E/F=48-529. DR PDB; 8H9P; EM; 3.02 A; D/E/F=48-529. DR PDB; 8H9S; EM; 2.53 A; D/E/F=48-529. DR PDB; 8H9T; EM; 2.77 A; D/E/F=48-529. DR PDB; 8H9U; EM; 2.61 A; D/E/F=48-529. DR PDB; 8H9V; EM; 3.02 A; D/E/F=48-529. DR PDB; 8KI3; EM; 2.89 A; D/E/F=48-529. DR AlphaFoldDB; P06576; -. DR EMDB; EMD-34564; -. DR EMDB; EMD-34568; -. DR EMDB; EMD-34572; -. DR EMDB; EMD-34576; -. DR EMDB; EMD-34580; -. DR EMDB; EMD-34581; -. DR EMDB; EMD-34582; -. DR EMDB; EMD-34583; -. DR EMDB; EMD-37251; -. DR SMR; P06576; -. DR BioGRID; 106994; 703. DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex. DR CORUM; P06576; -. DR FunCoup; P06576; 2188. DR IntAct; P06576; 270. DR NDEx; IQUERY-CP-ATP5F1B; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000262030; -. DR BindingDB; P06576; -. DR ChEMBL; CHEMBL2062350; -. DR DrugBank; DB07384; 1-ACETYL-2-CARBOXYPIPERIDINE. DR DrugBank; DB07394; AUROVERTIN B. DR DrugBank; DB01119; Diazoxide. DR DrugBank; DB08949; Inositol nicotinate. DR DrugBank; DB08629; N1-(2-AMINO-4-METHYLPENTYL)OCTAHYDRO-PYRROLO[1,2-A] PYRIMIDINE. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR DrugBank; DB08399; Piceatannol. DR DrugBank; DB04216; Quercetin. DR TCDB; 3.A.2.1.15; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily. DR CarbonylDB; P06576; -. DR GlyCosmos; P06576; 2 sites, 1 glycan. DR GlyGen; P06576; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P06576; -. DR MetOSite; P06576; -. DR PhosphoSitePlus; P06576; -. DR SwissPalm; P06576; -. DR BioMuta; ATP5B; -. DR DMDM; 114549; -. DR OGP; P06576; -. DR REPRODUCTION-2DPAGE; IPI00303476; -. DR REPRODUCTION-2DPAGE; P06576; -. DR CPTAC; CPTAC-315; -. DR CPTAC; CPTAC-316; -. DR jPOST; P06576; -. DR MassIVE; P06576; -. DR PaxDb; 9606-ENSP00000262030; -. DR PeptideAtlas; P06576; -. DR PRIDE; P06576; -. DR ProteomicsDB; 51907; -. DR Pumba; P06576; -. DR TopDownProteomics; P06576; -. DR Antibodypedia; 877; 647 antibodies from 40 providers. DR DNASU; 506; -. DR Ensembl; ENST00000262030.8; ENSP00000262030.3; ENSG00000110955.10. DR GeneID; 506; -. DR KEGG; hsa:506; -. DR MANE-Select; ENST00000262030.8; ENSP00000262030.3; NM_001686.4; NP_001677.2. DR AGR; HGNC:830; -. DR ClinPGx; PA25122; -. DR CTD; 506; -. DR DisGeNET; 506; -. DR GeneCards; ATP5F1B; -. DR HGNC; HGNC:830; ATP5F1B. DR HPA; ENSG00000110955; Tissue enhanced (skeletal muscle, tongue). DR MalaCards; ATP5F1B; -. DR MIM; 102910; gene. DR MIM; 620085; phenotype. DR MIM; 621502; phenotype. DR OpenTargets; ENSG00000110955; -. DR VEuPathDB; HostDB:ENSG00000110955; -. DR eggNOG; KOG1350; Eukaryota. DR GeneTree; ENSGT00550000074800; -. DR HOGENOM; CLU_022398_0_2_1; -. DR InParanoid; P06576; -. DR OMA; AACHFQQ; -. DR OrthoDB; 14523at2759; -. DR PAN-GO; P06576; 3 GO annotations based on evolutionary models. DR PhylomeDB; P06576; -. DR BioCyc; MetaCyc:HS03358-MONOMER; -. DR PathwayCommons; P06576; -. DR Reactome; R-HSA-1268020; Mitochondrial protein import. DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis. DR Reactome; R-HSA-8949613; Cristae formation. DR Reactome; R-HSA-9837999; Mitochondrial protein degradation. DR SignaLink; P06576; -. DR SIGNOR; P06576; -. DR Agora; ENSG00000110955; -. DR BioGRID-ORCS; 506; 586 hits in 1170 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ATP5B; human. DR GeneWiki; ATP5B; -. DR GenomeRNAi; 506; -. DR Pharos; P06576; Tbio. DR PRO; PR:P06576; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P06576; protein. DR Bgee; ENSG00000110955; Expressed in apex of heart and 200 other cell types or tissues. DR ExpressionAtlas; P06576; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:CAFA. DR GO; GO:0005743; C:mitochondrial inner membrane; EXP:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB. DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IDA:UniProtKB. DR GO; GO:0043532; F:angiostatin binding; IPI:CAFA. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IDA:UniProtKB. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB. DR GO; GO:0006754; P:ATP biosynthetic process; IMP:UniProtKB. DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:UniProtKB. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IGI:CAFA. DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:UniProtKB. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB. DR GO; GO:1902600; P:proton transmembrane transport; IMP:UniProtKB. DR GO; GO:0051453; P:regulation of intracellular pH; IMP:UniProtKB. 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; 3.40.50.300:FF:000026; ATP synthase subunit beta; 1. DR Gene3D; 2.40.10.170; -; 1. DR Gene3D; 1.10.1140.10; Bovine Mitochondrial F1-atpase, Atp Synthase Beta Chain, Chain D, domain 3; 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 3D-structure; Acetylation; ATP synthesis; ATP-binding; CF(1); KW Direct protein sequencing; Disease variant; Dystonia; Glycoprotein; KW Hydrogen ion transport; Ion transport; Magnesium; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Transit peptide; Translocase; Transport. FT TRANSIT 1..47 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:19892738" FT CHAIN 48..529 FT /note="ATP synthase F(1) complex subunit beta, FT mitochondrial" FT /id="PRO_0000002443" FT BINDING 209 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:37244256, FT ECO:0007744|PDB:8H9V, ECO:0007744|PDB:8KI3" FT BINDING 209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 209 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 210 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 210 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 211 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:37244256, FT ECO:0007744|PDB:8H9V, ECO:0007744|PDB:8KI3" FT BINDING 211 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 211 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 212 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:37244256, FT ECO:0007744|PDB:8H9V, ECO:0007744|PDB:8KI3" FT BINDING 212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 212 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 213 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:37244256, FT ECO:0007744|PDB:8H9V, ECO:0007744|PDB:8KI3" FT BINDING 213 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 213 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000269|PubMed:37244256, FT ECO:0007744|PDB:8H9V, ECO:0007744|PDB:8KI3" FT BINDING 213 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 214 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:37244256, FT ECO:0007744|PDB:8H9V, ECO:0007744|PDB:8KI3" FT BINDING 214 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00829" FT BINDING 238 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="ligand shared between two neighboring FT subunits" 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:0000250|UniProtKB:P56480" FT MOD_RES 124 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 133 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 133 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 161 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 161 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 198 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 259 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 259 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 264 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 264 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 312 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 415 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 426 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 433 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10719" FT MOD_RES 480 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 485 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 522 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 522 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P56480" FT MOD_RES 529 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 106 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT VARIANT 130 FT /note="A -> V" FT /evidence="ECO:0000269|PubMed:25787250" FT /id="VAR_074188" FT VARIANT 274 FT /note="E -> Q (in dbSNP:rs1042001)" FT /evidence="ECO:0000269|PubMed:2870059, FT ECO:0000269|PubMed:2900241" FT /id="VAR_048371" FT VARIANT 334 FT /note="T -> P (in DYT38; uncertain significance)" FT /evidence="ECO:0000269|PubMed:36860166" FT /id="VAR_091581" FT VARIANT 335 FT /note="L -> P (in HUMOP2; elevated baseline extracellular FT acidification rate; increased glucose consumption; FT increased lactate release)" FT /evidence="ECO:0000269|PubMed:36239646" FT /id="VAR_087864" FT VARIANT 482 FT /note="V -> A (in DYT38; uncertain significance)" FT /evidence="ECO:0000269|PubMed:36860166" FT /id="VAR_091582" FT CONFLICT 1..6 FT /note="MLGFVG -> MTSLWGKGTGCKLFKF (in Ref. 3; FT BAA00016/CAA27246)" FT /evidence="ECO:0000305" FT CONFLICT 36..40 FT /note="APTAV -> VRRRF (in Ref. 2; AAA51808)" FT /evidence="ECO:0000305" FT CONFLICT 36..40 FT /note="APTAV -> VRRRS (in Ref. 3; BAA00016/CAA27246)" FT /evidence="ECO:0000305" FT CONFLICT 130..132 FT /note="API -> DQL (in Ref. 2; AAA51808)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="H -> D (in Ref. 2; AAA51808)" FT /evidence="ECO:0000305" FT CONFLICT 435 FT /note="Q -> H (in Ref. 2; AAA51808)" FT /evidence="ECO:0000305" FT STRAND 60..67 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 70..78 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 85..90 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 107..114 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 133..137 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 161..166 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 169..172 FT /evidence="ECO:0007829|PDB:8H9L" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:8H9T" FT HELIX 188..193 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:8H9T" FT STRAND 201..205 FT /evidence="ECO:0007829|PDB:8H9E" FT TURN 208..211 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 212..226 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 231..238 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 240..252 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 265..271 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 276..295 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 308..321 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 335..343 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 349..351 FT /evidence="ECO:0007829|PDB:8H9I" FT STRAND 353..359 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 363..365 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 370..375 FT /evidence="ECO:0007829|PDB:8H9E" FT TURN 376..378 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 380..385 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 387..390 FT /evidence="ECO:0007829|PDB:8H9E" FT TURN 391..393 FT /evidence="ECO:0007829|PDB:8H9E" FT TURN 400..402 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 410..413 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 415..437 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 439..441 FT /evidence="ECO:0007829|PDB:8H9L" FT HELIX 443..445 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 450..464 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 469..471 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 472..475 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 477..480 FT /evidence="ECO:0007829|PDB:8H9U" FT HELIX 484..496 FT /evidence="ECO:0007829|PDB:8H9E" FT TURN 497..499 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 500..502 FT /evidence="ECO:0007829|PDB:8H9E" FT HELIX 504..506 FT /evidence="ECO:0007829|PDB:8H9E" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:8H9I" FT HELIX 513..521 FT /evidence="ECO:0007829|PDB:8H9E" 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 //