ID SMG1_HUMAN Reviewed; 3661 AA. AC Q96Q15; O43305; Q13284; Q8NFX2; Q96QV0; Q96RW3; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 08-FEB-2011, sequence version 3. DT 27-MAR-2024, entry version 189. DE RecName: Full=Serine/threonine-protein kinase SMG1; DE Short=SMG-1; DE Short=hSMG-1; DE EC=2.7.11.1; DE AltName: Full=Lambda/iota protein kinase C-interacting protein {ECO:0000303|PubMed:8524286}; DE Short=Lambda-interacting protein {ECO:0000303|PubMed:8524286}; DE AltName: Full=Nonsense mediated mRNA decay-associated PI3K-related kinase SMG1 {ECO:0000312|HGNC:HGNC:30045}; GN Name=SMG1 {ECO:0000312|HGNC:HGNC:30045}; GN Synonyms=ATX {ECO:0000312|HGNC:HGNC:30045}, KIAA0421 GN {ECO:0000312|HGNC:HGNC:30045}, LIP {ECO:0000312|HGNC:HGNC:30045}; 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 [MRNA] (ISOFORM 4). RX PubMed=9566925; DOI=10.1128/mcb.18.5.3069; RA Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.; RT "Localization of atypical protein kinase C isoforms into lysosome-targeted RT endosomes through interaction with p62."; RL Mol. Cell. Biol. 18:3069-3080(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION OF RENT1, RP ALTERNATIVE SPLICING, ACTIVITY REGULATION, PHOSPHORYLATION, INTERACTION RP WITH RENT1; UPF2 AND UPF3, AND MUTAGENESIS OF ASP-2335. RX PubMed=11544179; DOI=10.1101/gad.913001; RA Yamashita A., Ohnishi T., Kashima I., Taya Y., Ohno S.; RT "Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, RT associates with components of the mRNA surveillance complex and is involved RT in the regulation of nonsense-mediated mRNA decay."; RL Genes Dev. 15:2215-2228(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, PHOSPHORYLATION OF RENT1, RP COFACTOR, ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-2335. RX PubMed=11331269; DOI=10.1074/jbc.c100144200; RA Denning G., Jamieson L., Maquat L.E., Thompson E.A., Fields A.P.; RT "Cloning of a novel phosphatidylinositol kinase-related kinase: RT characterization of the human SMG-1 RNA surveillance protein."; RL J. Biol. Chem. 276:22709-22714(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION OF TP53, RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION, MUTAGENESIS RP OF ASP-2335, AND VARIANTS CYS-144 AND LYS-612. RX PubMed=15175154; DOI=10.1016/j.molcel.2004.05.005; RA Brumbaugh K.M., Otterness D.M., Geisen C., Oliveira V., Brognard J., Li X., RA Lejeune F., Tibbetts R.S., Maquat L.E., Abraham R.T.; RT "The mRNA surveillance protein hSMG-1 functions in genotoxic stress RT response pathways in mammalian cells."; RL Mol. Cell 14:585-598(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1674-3661. RC TISSUE=Brain; RX PubMed=9455477; DOI=10.1093/dnares/4.5.307; RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VIII. 78 RT new cDNA clones from brain which code for large proteins in vitro."; RL DNA Res. 4:307-313(1997). RN [7] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2878-3661, TISSUE SPECIFICITY, AND RP INTERACTION WITH PRKCI. RX PubMed=8524286; DOI=10.1128/mcb.16.1.105; RA Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., Moscat J.; RT "Lambda-interacting protein, a novel protein that specifically interacts RT with the zinc finger domain of the atypical protein kinase C isotype RT lambda/iota and stimulates its kinase activity in vitro and in vivo."; RL Mol. Cell. Biol. 16:105-114(1996). RN [9] RP DUPLICATION. RX PubMed=11948212; DOI=10.1093/jhered/92.6.462; RA Eichler E.E., Johnson M.E., Alkan C., Tuzun E., Sahinalp C., Misceo D., RA Archidiacono N., Rocchi M.; RT "Divergent origins and concerted expansion of two segmental duplications on RT chromosome 16."; RL J. Hered. 92:462-468(2001). RN [10] RP INTERACTION WITH SMG5. RX PubMed=14636577; DOI=10.1016/s1097-2765(03)00443-x; RA Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R., Grimson A., RA Hachiya T., Hentze M.W., Anderson P., Ohno S.; RT "Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes RT containing hSMG-5 and hSMG-7."; RL Mol. Cell 12:1187-1200(2003). RN [11] RP INTERACTION WITH RENT1; UPF2; EST1A AND UPF3B. RX PubMed=12554878; DOI=10.1261/rna.2137903; RA Chiu S.-Y., Serin G., Ohara O., Maquat L.E.; RT "Characterization of human Smg5/7a: a protein with similarities to RT Caenorhabditis elegans SMG5 and SMG7 that functions in the RT dephosphorylation of Upf1."; RL RNA 9:77-87(2003). RN [12] RP FUNCTION, INTERACTION WITH UPF2, AND IDENTIFICATION IN THE SURF COMPLEX. RX PubMed=16452507; DOI=10.1101/gad.1389006; RA Kashima I., Yamashita A., Izumi N., Kataoka N., Morishita R., Hoshino S., RA Ohno M., Dreyfuss G., Ohno S.; RT "Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon RT junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA RT decay."; RL Genes Dev. 20:355-367(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3550 AND SER-3556, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3570, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE SMG1C COMPLEX. RX PubMed=19417104; DOI=10.1101/gad.1767209; RA Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., RA Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., RA Anderson P., Ohno S.; RT "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate RT remodeling of the mRNA surveillance complex during nonsense-mediated mRNA RT decay."; RL Genes Dev. 23:1091-1105(2009). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND IDENTIFICATION BY MASS RP 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 [20] RP INTERACTION WITH TELO2 AND TTI1. RX PubMed=20427287; DOI=10.1074/jbc.m110.121699; RA Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., RA Iemura S., Natsume T., Mizushima N.; RT "Tti1 and Tel2 are critical factors in mammalian target of rapamycin RT complex assembly."; RL J. Biol. Chem. 285:20109-20116(2010). RN [21] RP INTERACTION WITH TTI1. RX PubMed=20810650; DOI=10.1101/gad.1934210; RA Hurov K.E., Cotta-Ramusino C., Elledge S.J.; RT "A genetic screen identifies the Triple T complex required for DNA damage RT signaling and ATM and ATR stability."; RL Genes Dev. 24:1939-1950(2010). RN [22] RP INTERACTION WITH RUVBL1 AND RUVBL2. RX PubMed=20371770; DOI=10.1126/scisignal.2000468; RA Izumi N., Yamashita A., Iwamatsu A., Kurata R., Nakamura H., Saari B., RA Hirano H., Anderson P., Ohno S.; RT "AAA+ proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function in RT nonsense-mediated mRNA decay."; RL Sci. Signal. 3:RA27-RA27(2010). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3573, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [24] 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 [25] RP INTERACTION WITH SMG8 AND SMG9, AND ELECTRON MICROSCOPY OF THE SMG1C RP COMPLEX. RX PubMed=21245168; DOI=10.1101/gad.606911; RA Arias-Palomo E., Yamashita A., Fernandez I.S., Nunez-Ramirez R., Bamba Y., RA Izumi N., Ohno S., Llorca O.; RT "The nonsense-mediated mRNA decay SMG-1 kinase is regulated by large-scale RT conformational changes controlled by SMG-8."; RL Genes Dev. 25:153-164(2011). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3550; SER-3556; SER-3570 AND RP THR-3573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [28] RP INTERACTION WITH DHX34. RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020; RA Hug N., Caceres J.F.; RT "The RNA helicase DHX34 activates NMD by promoting a transition from the RT surveillance to the decay-inducing complex."; RL Cell Rep. 8:1845-1856(2014). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3573, AND IDENTIFICATION BY RP 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 [30] RP IDENTIFICATION IN A COMPLEX WITH DHX34 AND UPF1, AND INTERACTION WITH DHX34 RP AND UPF1. RX PubMed=26841701; DOI=10.1038/ncomms10585; RA Melero R., Hug N., Lopez-Perrote A., Yamashita A., Caceres J.F., Llorca O.; RT "The RNA helicase DHX34 functions as a scaffold for SMG1-mediated UPF1 RT phosphorylation."; RL Nat. Commun. 7:10585-10585(2016). RN [31] RP INTERACTION WITH RUVBL1; RUVBL2; SMG8 AND SMG9. RX PubMed=33205750; DOI=10.7554/elife.63042; RA Lopez-Perrote A., Hug N., Gonzalez-Corpas A., Rodriguez C.F., Serna M., RA Garcia-Martin C., Boskovic J., Fernandez-Leiro R., Caceres J.F., Llorca O.; RT "Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA RT decay factor DHX34, as evidenced by Cryo-EM."; RL Elife 9:0-0(2020). RN [32] RP VARIANTS [LARGE SCALE ANALYSIS] THR-35; CYS-126; CYS-144; TYR-151; ASN-160; RP VAL-167; GLY-320; SER-465; ARG-546; SER-588; LYS-612; CYS-753; CYS-809; RP CYS-812; ILE-829; ASP-832; GLY-952; SER-969; LEU-1016; GLN-1029; SER-1072; RP HIS-1103; ARG-1275; PRO-1292; VAL-1332; PRO-1358; THR-1418; CYS-2171; RP SER-2258; LYS-2345; GLU-2730; SER-2889; ALA-2899; THR-3239 AND GLN-3583. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Serine/threonine protein kinase involved in both mRNA CC surveillance and genotoxic stress response pathways. Recognizes the CC substrate consensus sequence [ST]-Q. Plays a central role in nonsense- CC mediated decay (NMD) of mRNAs containing premature stop codons by CC phosphorylating UPF1/RENT1. Recruited by release factors to stalled CC ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase CC complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) CC complex. In EJC-dependent NMD, the SURF complex associates with the CC exon junction complex (EJC) through UPF2 and allows the formation of an CC UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. CC Also acts as a genotoxic stress-activated protein kinase that displays CC some functional overlap with ATM. Can phosphorylate p53/TP53 and is CC required for optimal p53/TP53 activation after cellular exposure to CC genotoxic stress. Its depletion leads to spontaneous DNA damage and CC increased sensitivity to ionizing radiation (IR). May activate PRKCI CC but not PRKCZ. {ECO:0000269|PubMed:11331269, CC ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:15175154, CC ECO:0000269|PubMed:16452507}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:19417104}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:19417104}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:11331269}; CC -!- ACTIVITY REGULATION: Inhibited by caffeine, LY294002 and wortmannin. CC {ECO:0000269|PubMed:11331269, ECO:0000269|PubMed:11544179, CC ECO:0000269|PubMed:15175154}. CC -!- SUBUNIT: Component of the SMG1C complex composed of SMG1, SMG8 and CC SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large CC conformational change in the SMG1 C-terminal head domain containing the CC catalytic domain (PubMed:33205750). Component of the transient SURF CC (SMG1-UPF1-eRF1-eRF3) complex. Part of a complex composed of SMG1, CC DHX34 and UPF1; within the complex DHX34 acts as a scaffolding protein CC to facilitate SMG1 phosphorylation of UPF1 (PubMed:26841701). Interacts CC with PRKCI. Interacts with TELO2 and TTI1. Interacts with RUVBL1 and CC RUVBL2 (PubMed:33205750). Interacts with UPF2. Interacts with DHX34 CC (via C-terminus); the interaction is RNA-independent (PubMed:25220460, CC PubMed:33205750). {ECO:0000269|PubMed:11544179, CC ECO:0000269|PubMed:12554878, ECO:0000269|PubMed:14636577, CC ECO:0000269|PubMed:16452507, ECO:0000269|PubMed:19417104, CC ECO:0000269|PubMed:20371770, ECO:0000269|PubMed:20427287, CC ECO:0000269|PubMed:20810650, ECO:0000269|PubMed:21245168, CC ECO:0000269|PubMed:25220460, ECO:0000269|PubMed:26841701, CC ECO:0000269|PubMed:33205750, ECO:0000269|PubMed:8524286}. CC -!- INTERACTION: CC Q96Q15; P11940: PABPC1; NbExp=2; IntAct=EBI-1049832, EBI-81531; CC Q96Q15; Q9HAU5: UPF2; NbExp=7; IntAct=EBI-1049832, EBI-372073; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15175154}. Cytoplasm CC {ECO:0000269|PubMed:15175154}. Note=Present in the chromatoid body. CC {ECO:0000250|UniProtKB:Q8BKX6}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q96Q15-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96Q15-2; Sequence=VSP_017748; CC Name=3; CC IsoId=Q96Q15-3; Sequence=VSP_017747; CC Name=4; Synonyms=BLIP; CC IsoId=Q96Q15-4; Sequence=VSP_017746; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest level in heart and CC skeletal muscle. Expressed in placenta, brain, lung and spleen, but not CC in liver. {ECO:0000269|PubMed:15175154, ECO:0000269|PubMed:8524286}. CC -!- PTM: Autophosphorylated. {ECO:0000305|PubMed:11331269, CC ECO:0000305|PubMed:11544179, ECO:0000305|PubMed:15175154}. CC -!- MISCELLANEOUS: This gene is located in a region of chromosome 16 that CC contains 2 segmental duplications. Other genes that are highly related CC to this exist, but they probably represent pseudogenes. CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA86535.2; Type=Erroneous initiation; Note=Truncated 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; AF186377; AAK58892.1; -; mRNA. DR EMBL; AB061371; BAB70696.1; -; mRNA. DR EMBL; AY014957; AAK00511.1; -; mRNA. DR EMBL; AF395444; AAM73708.1; -; mRNA. DR EMBL; AC092287; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB007881; BAA24851.2; -; mRNA. DR EMBL; U32581; AAA86535.2; ALT_INIT; mRNA. DR CCDS; CCDS45430.1; -. [Q96Q15-1] DR PIR; JC6084; JC6084. DR RefSeq; NP_055907.3; NM_015092.4. [Q96Q15-1] DR PDB; 6L53; EM; 3.63 A; A=1-3661. DR PDB; 6L54; EM; 3.43 A; A=1-3661. DR PDB; 6SYT; EM; 3.45 A; A=311-3661. DR PDB; 6Z3R; EM; 2.97 A; A=259-3661. DR PDB; 7PW4; EM; 3.27 A; A=311-3661. DR PDB; 7PW5; EM; 3.40 A; A=311-3661. DR PDB; 7PW6; EM; 3.05 A; A=766-3661. DR PDB; 7PW7; EM; 3.59 A; A=311-3661. DR PDB; 7PW8; EM; 2.82 A; A=311-3661. DR PDB; 7PW9; EM; 3.12 A; A=311-3661. DR PDBsum; 6L53; -. DR PDBsum; 6L54; -. DR PDBsum; 6SYT; -. DR PDBsum; 6Z3R; -. DR PDBsum; 7PW4; -. DR PDBsum; 7PW5; -. DR PDBsum; 7PW6; -. DR PDBsum; 7PW7; -. DR PDBsum; 7PW8; -. DR PDBsum; 7PW9; -. DR EMDB; EMD-0836; -. DR EMDB; EMD-0837; -. DR EMDB; EMD-10347; -. DR EMDB; EMD-11063; -. DR EMDB; EMD-13674; -. DR EMDB; EMD-13675; -. DR EMDB; EMD-13676; -. DR EMDB; EMD-13677; -. DR EMDB; EMD-13678; -. DR EMDB; EMD-13679; -. DR EMDB; EMD-2662; -. DR EMDB; EMD-2663; -. DR EMDB; EMD-2664; -. DR EMDB; EMD-2665; -. DR EMDB; EMD-2666; -. DR EMDB; EMD-3065; -. DR EMDB; EMD-3066; -. DR EMDB; EMD-3278; -. DR SMR; Q96Q15; -. DR BioGRID; 116687; 93. DR ComplexPortal; CPX-2827; SMG1C protein kinase complex. DR CORUM; Q96Q15; -. DR IntAct; Q96Q15; 39. DR MINT; Q96Q15; -. DR STRING; 9606.ENSP00000402515; -. DR BindingDB; Q96Q15; -. DR ChEMBL; CHEMBL1795195; -. DR GuidetoPHARMACOLOGY; 2201; -. DR GlyGen; Q96Q15; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96Q15; -. DR MetOSite; Q96Q15; -. DR PhosphoSitePlus; Q96Q15; -. DR BioMuta; SMG1; -. DR DMDM; 322510104; -. DR EPD; Q96Q15; -. DR jPOST; Q96Q15; -. DR MassIVE; Q96Q15; -. DR MaxQB; Q96Q15; -. DR PaxDb; 9606-ENSP00000402515; -. DR PeptideAtlas; Q96Q15; -. DR ProteomicsDB; 77810; -. [Q96Q15-1] DR ProteomicsDB; 77811; -. [Q96Q15-2] DR ProteomicsDB; 77812; -. [Q96Q15-3] DR ProteomicsDB; 77813; -. [Q96Q15-4] DR Pumba; Q96Q15; -. DR Antibodypedia; 6280; 242 antibodies from 17 providers. DR DNASU; 23049; -. DR Ensembl; ENST00000446231.7; ENSP00000402515.3; ENSG00000157106.18. [Q96Q15-1] DR GeneID; 23049; -. DR KEGG; hsa:23049; -. DR MANE-Select; ENST00000446231.7; ENSP00000402515.3; NM_015092.5; NP_055907.3. DR UCSC; uc002dfm.4; human. [Q96Q15-1] DR AGR; HGNC:30045; -. DR CTD; 23049; -. DR DisGeNET; 23049; -. DR GeneCards; SMG1; -. DR HGNC; HGNC:30045; SMG1. DR HPA; ENSG00000157106; Low tissue specificity. DR MalaCards; SMG1; -. DR MIM; 607032; gene. DR neXtProt; NX_Q96Q15; -. DR OpenTargets; ENSG00000157106; -. DR PharmGKB; PA164725852; -. DR VEuPathDB; HostDB:ENSG00000157106; -. DR eggNOG; KOG0891; Eukaryota. DR GeneTree; ENSGT00940000154776; -. DR InParanoid; Q96Q15; -. DR OMA; AFECHFT; -. DR OrthoDB; 8448at2759; -. DR PhylomeDB; Q96Q15; -. DR TreeFam; TF352560; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; Q96Q15; -. DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR SignaLink; Q96Q15; -. DR SIGNOR; Q96Q15; -. DR BioGRID-ORCS; 23049; 677 hits in 1205 CRISPR screens. DR ChiTaRS; SMG1; human. DR GeneWiki; SMG1_(gene); -. DR GenomeRNAi; 23049; -. DR Pharos; Q96Q15; Tchem. DR PRO; PR:Q96Q15; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q96Q15; Protein. DR Bgee; ENSG00000157106; Expressed in upper leg skin and 194 other cell types or tissues. DR ExpressionAtlas; Q96Q15; baseline and differential. DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; EXP:Reactome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; TAS:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006406; P:mRNA export from nucleus; TAS:UniProtKB. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL. DR CDD; cd05170; PIKKc_SMG1; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR003152; FATC_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000403; PI3/4_kinase_cat_dom. DR InterPro; IPR036940; PI3/4_kinase_cat_sf. DR InterPro; IPR018936; PI3/4_kinase_CS. DR InterPro; IPR014009; PIK_FAT. DR InterPro; IPR031559; SMG1. DR InterPro; IPR035175; SMG1_N. DR InterPro; IPR039414; SMG1_PIKKc. DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1. DR PANTHER; PTHR11139:SF71; SERINE_THREONINE-PROTEIN KINASE SMG1; 1. DR Pfam; PF02260; FATC; 1. DR Pfam; PF00454; PI3_PI4_kinase; 1. DR Pfam; PF15785; SMG1; 1. DR Pfam; PF17229; SMG1_N; 1. DR SMART; SM01343; FATC; 1. DR SMART; SM00146; PI3Kc; 1. DR SMART; SM01345; Rapamycin_bind; 1. DR SUPFAM; SSF48371; ARM repeat; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51189; FAT; 1. DR PROSITE; PS51190; FATC; 1. DR PROSITE; PS00916; PI3_4_KINASE_2; 1. DR PROSITE; PS50290; PI3_4_KINASE_3; 1. DR Genevisible; Q96Q15; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW DNA damage; DNA repair; Kinase; Manganese; Metal-binding; KW Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..3661 FT /note="Serine/threonine-protein kinase SMG1" FT /id="PRO_0000229791" FT DOMAIN 1283..1866 FT /note="FAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534" FT REPEAT 1817..1852 FT /note="HEAT" FT DOMAIN 2124..2463 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT DOMAIN 3629..3661 FT /note="FATC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534, FT ECO:0000255|PROSITE-ProRule:PRU00535" FT REGION 1..1977 FT /note="Interaction with SMG8 and SMG9" FT /evidence="ECO:0000269|PubMed:21245168" FT REGION 1..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 116..144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1154..1175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1898..1919 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2130..2136 FT /note="G-loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 2332..2340 FT /note="Catalytic loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 2352..2376 FT /note="Activation loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 3568..3591 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..67 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 68..82 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 87..101 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 128..142 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3568..3583 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 173 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 3550 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 3556 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 3570 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 3573 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 3577 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8BKX6" FT VAR_SEQ 1..1269 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:9566925" FT /id="VSP_017746" FT VAR_SEQ 1..630 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11331269" FT /id="VSP_017747" FT VAR_SEQ 1..140 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15175154" FT /id="VSP_017748" FT VARIANT 35 FT /note="A -> T (in dbSNP:rs12051350)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041623" FT VARIANT 126 FT /note="R -> C (in dbSNP:rs752796432)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041624" FT VARIANT 144 FT /note="S -> C (in dbSNP:rs766737607)" FT /evidence="ECO:0000269|PubMed:15175154, FT ECO:0000269|PubMed:17344846" FT /id="VAR_041625" FT VARIANT 151 FT /note="N -> Y (in dbSNP:rs750788715)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041626" FT VARIANT 160 FT /note="D -> N" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041627" FT VARIANT 167 FT /note="A -> V (in dbSNP:rs1382468496)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041628" FT VARIANT 320 FT /note="D -> G" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041629" FT VARIANT 465 FT /note="G -> S (in dbSNP:rs200419100)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041630" FT VARIANT 546 FT /note="H -> R (in dbSNP:rs376234691)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041631" FT VARIANT 588 FT /note="A -> S (in dbSNP:rs750840136)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041632" FT VARIANT 612 FT /note="I -> K (in dbSNP:rs17842615)" FT /evidence="ECO:0000269|PubMed:15175154, FT ECO:0000269|PubMed:17344846" FT /id="VAR_041633" FT VARIANT 753 FT /note="S -> C (in dbSNP:rs569679854)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041634" FT VARIANT 809 FT /note="S -> C (in dbSNP:rs919788709)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041635" FT VARIANT 812 FT /note="R -> C (in dbSNP:rs1233400465)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041636" FT VARIANT 829 FT /note="V -> I" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041637" FT VARIANT 832 FT /note="N -> D (in dbSNP:rs80176913)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041638" FT VARIANT 952 FT /note="A -> G (in dbSNP:rs555078480)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041639" FT VARIANT 969 FT /note="N -> S (in dbSNP:rs1412788971)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041640" FT VARIANT 1016 FT /note="F -> L (in dbSNP:rs1394431566)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041641" FT VARIANT 1029 FT /note="R -> Q" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041642" FT VARIANT 1072 FT /note="T -> S (in dbSNP:rs45516593)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041643" FT VARIANT 1103 FT /note="N -> H (in dbSNP:rs563883658)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041644" FT VARIANT 1275 FT /note="P -> R" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041645" FT VARIANT 1292 FT /note="Q -> P (in dbSNP:rs375411122)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041646" FT VARIANT 1332 FT /note="I -> V (in dbSNP:rs949474935)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041647" FT VARIANT 1358 FT /note="S -> P" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041648" FT VARIANT 1418 FT /note="R -> T (in dbSNP:rs17731779)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041649" FT VARIANT 2171 FT /note="S -> C (in a breast pleomorphic lobular carcinoma FT sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041650" FT VARIANT 2258 FT /note="G -> S (in dbSNP:rs35572280)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041651" FT VARIANT 2345 FT /note="M -> K (in dbSNP:rs56276814)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041652" FT VARIANT 2730 FT /note="Q -> E (in dbSNP:rs34960798)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041653" FT VARIANT 2889 FT /note="G -> S (in dbSNP:rs35952340)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041654" FT VARIANT 2899 FT /note="P -> A (in dbSNP:rs55782217)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041655" FT VARIANT 3239 FT /note="I -> T (in a breast infiltrating ductal carcinoma FT sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041656" FT VARIANT 3583 FT /note="K -> Q (in a breast infiltrating ductal carcinoma FT sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041657" FT MUTAGEN 2335 FT /note="D->A: Loss of function." FT /evidence="ECO:0000269|PubMed:11331269, FT ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:15175154" FT CONFLICT 14 FT /note="G -> GGGGG (in Ref. 2; BAB70696)" FT /evidence="ECO:0000305" FT CONFLICT 20 FT /note="K -> N (in Ref. 2; BAB70696)" FT /evidence="ECO:0000305" FT CONFLICT 22 FT /note="P -> S (in Ref. 2; BAB70696)" FT /evidence="ECO:0000305" FT CONFLICT 40 FT /note="D -> G (in Ref. 2; BAB70696)" FT /evidence="ECO:0000305" FT CONFLICT 686 FT /note="S -> A (in Ref. 2; BAB70696)" FT /evidence="ECO:0000305" FT CONFLICT 743 FT /note="K -> R (in Ref. 2; BAB70696)" FT /evidence="ECO:0000305" FT CONFLICT 1193 FT /note="C -> F (in Ref. 2; BAB70696)" FT /evidence="ECO:0000305" FT CONFLICT 2009 FT /note="K -> R (in Ref. 2; BAB70696)" FT /evidence="ECO:0000305" FT CONFLICT 2077 FT /note="S -> N (in Ref. 1; AAK58892)" FT /evidence="ECO:0000305" FT HELIX 38..42 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 62..69 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 81..88 FT /evidence="ECO:0007829|PDB:6L54" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 97..102 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:6L54" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 114..117 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 124..141 FT /evidence="ECO:0007829|PDB:6L54" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 154..162 FT /evidence="ECO:0007829|PDB:6L54" FT TURN 163..167 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 171..174 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 178..181 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 189..198 FT /evidence="ECO:0007829|PDB:6L54" FT TURN 199..201 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 202..204 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 211..222 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 230..245 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 261..274 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 281..292 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 297..306 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 307..309 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 314..321 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 326..330 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 336..346 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 356..373 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 380..387 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 389..394 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 395..411 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 421..424 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 429..443 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 445..447 FT /evidence="ECO:0007829|PDB:7PW9" FT HELIX 450..466 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 475..486 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 490..492 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 494..510 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 517..523 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 529..532 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 533..535 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 539..552 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 558..582 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 590..592 FT /evidence="ECO:0007829|PDB:7PW4" FT HELIX 595..597 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 598..600 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 604..622 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 625..630 FT /evidence="ECO:0007829|PDB:6L54" FT STRAND 634..636 FT /evidence="ECO:0007829|PDB:7PW9" FT HELIX 638..644 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 647..650 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 653..656 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 658..673 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 674..678 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 679..681 FT /evidence="ECO:0007829|PDB:7PW9" FT TURN 700..705 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 706..718 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 725..741 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 746..753 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 755..766 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 768..771 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 773..785 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 792..805 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 807..810 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 811..821 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 826..829 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 831..833 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 836..850 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 859..870 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 882..889 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 890..895 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 903..905 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 909..926 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 927..929 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 936..955 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 962..964 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 970..998 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 1002..1005 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1010..1018 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1020..1040 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1044..1057 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1068..1082 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1086..1096 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1107..1114 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 1115..1117 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 1118..1133 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 1134..1136 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 1144..1150 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1180..1196 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1200..1215 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 1216..1218 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 1228..1239 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1242..1249 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 1251..1255 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1282..1304 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 1315..1317 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1318..1331 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1333..1340 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1348..1366 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1371..1373 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1379..1382 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1391..1406 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1407..1409 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1418..1433 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 1434..1436 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1438..1449 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1459..1466 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1467..1479 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 1480..1494 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1497..1511 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 1514..1516 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1518..1534 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1536..1550 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1560..1569 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1587..1590 FT /evidence="ECO:0007829|PDB:6Z3R" FT STRAND 1591..1593 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1596..1611 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1616..1636 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1640..1648 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 1651..1659 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1668..1677 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1686..1695 FT /evidence="ECO:0007829|PDB:6SYT" FT HELIX 1708..1719 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1720..1725 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 1729..1740 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1742..1756 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1782..1798 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 1801..1803 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1804..1813 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 1818..1821 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1823..1828 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1829..1831 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1836..1849 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1853..1855 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1857..1864 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1925..1938 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 1939..1941 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 1942..1957 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1963..1977 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 1980..1992 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 2011..2023 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2036..2044 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2047..2054 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2069..2082 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2085..2087 FT /evidence="ECO:0007829|PDB:6L54" FT STRAND 2090..2092 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 2097..2101 FT /evidence="ECO:0007829|PDB:7PW9" FT STRAND 2120..2124 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2126..2130 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2132..2136 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2138..2144 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2149..2157 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2161..2175 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 2176..2179 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2180..2182 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2195..2197 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2199..2201 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2203..2206 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2212..2214 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 2215..2231 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2249..2262 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2272..2274 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2277..2290 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2295..2303 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2307..2331 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2340..2343 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 2345..2347 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2350..2352 FT /evidence="ECO:0007829|PDB:7PW8" FT TURN 2356..2360 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2361..2363 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2364..2367 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2377..2381 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2384..2386 FT /evidence="ECO:0007829|PDB:6L54" FT STRAND 2388..2390 FT /evidence="ECO:0007829|PDB:6Z3R" FT HELIX 2391..2405 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 2407..2418 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 2422..2424 FT /evidence="ECO:0007829|PDB:6L54" FT HELIX 3608..3620 FT /evidence="ECO:0007829|PDB:7PW8" FT STRAND 3627..3629 FT /evidence="ECO:0007829|PDB:7PW6" FT HELIX 3633..3645 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 3647..3651 FT /evidence="ECO:0007829|PDB:7PW8" FT HELIX 3655..3657 FT /evidence="ECO:0007829|PDB:7PW8" SQ SEQUENCE 3661 AA; 410501 MW; 216A55F3121F5829 CRC64; MSRRAPGSRL SSGGGGGGTK YPRSWNDWQP RTDSASADPD NLKYSSSRDR GGSSSYGLQP SNSAVVSRQR HDDTRVHADI QNDEKGGYSV NGGSGENTYG RKSLGQELRV NNVTSPEFTS VQHGSRALAT KDMRKSQERS MSYSDESRLS NLLRRITRED DRDRRLATVK QLKEFIQQPE NKLVLVKQLD NILAAVHDVL NESSKLLQEL RQEGACCLGL LCASLSYEAE KIFKWIFSKF SSSAKDEVKL LYLCATYKAL ETVGEKKAFS SVMQLVMTSL QSILENVDTP ELLCKCVKCI LLVARCYPHI FSTNFRDTVD ILVGWHIDHT QKPSLTQQVS GWLQSLEPFW VADLAFSTTL LGQFLEDMEA YAEDLSHVAS GESVDEDVPP PSVSLPKLAA LLRVFSTVVR SIGERFSPIR GPPITEAYVT DVLYRVMRCV TAANQVFFSE AVLTAANECV GVLLGSLDPS MTIHCDMVIT YGLDQLENCQ TCGTDYIISV LNLLTLIVEQ INTKLPSSFV EKLFIPSSKL LFLRYHKEKE VVAVAHAVYQ AVLSLKNIPV LETAYKLILG EMTCALNNLL HSLQLPEACS EIKHEAFKNH VFNVDNAKFV VIFDLSALTT IGNAKNSLIG MWALSPTVFA LLSKNLMIVH SDLAVHFPAI QYAVLYTLYS HCTRHDHFIS SSLSSSSPSL FDGAVISTVT TATKKHFSII LNLLGILLKK DNLNQDTRKL LMTWALEAAV LMKKSETYAP LFSLPSFHKF CKGLLANTLV EDVNICLQAC SSLHALSSSL PDDLLQRCVD VCRVQLVHSG TRIRQAFGKL LKSIPLDVVL SNNNHTEIQE ISLALRSHMS KAPSNTFHPQ DFSDVISFIL YGNSHRTGKD NWLERLFYSC QRLDKRDQST IPRNLLKTDA VLWQWAIWEA AQFTVLSKLR TPLGRAQDTF QTIEGIIRSL AAHTLNPDQD VSQWTTADND EGHGNNQLRL VLLLQYLENL EKLMYNAYEG CANALTSPPK VIRTFFYTNR QTCQDWLTRI RLSIMRVGLL AGQPAVTVRH GFDLLTEMKT TSLSQGNELE VTIMMVVEAL CELHCPEAIQ GIAVWSSSIV GKNLLWINSV AQQAEGRFEK ASVEYQEHLC AMTGVDCCIS SFDKSVLTLA NAGRNSASPK HSLNGESRKT VLSKPTDSSP EVINYLGNKA CECYISIADW AAVQEWQNAI HDLKKSTSST SLNLKADFNY IKSLSSFESG KFVECTEQLE LLPGENINLL AGGSKEKIDM KKLLPNMLSP DPRELQKSIE VQLLRSSVCL ATALNPIEQD QKWQSITENV VKYLKQTSRI AIGPLRLSTL TVSQSLPVLS TLQLYCSSAL ENTVSNRLST EDCLIPLFSE ALRSCKQHDV RPWMQALRYT MYQNQLLEKI KEQTVPIRSH LMELGLTAAK FARKRGNVSL ATRLLAQCSE VQLGKTTTAQ DLVQHFKKLS TQGQVDEKWG PELDIEKTKL LYTAGQSTHA MEMLSSCAIS FCKSVKAEYA VAKSILTLAK WIQAEWKEIS GQLKQVYRAQ HQQNFTGLST LSKNILTLIE LPSVNTMEEE YPRIESESTV HIGVGEPDFI LGQLYHLSSV QAPEVAKSWA ALASWAYRWG RKVVDNASQG EGVRLLPREK SEVQNLLPDT ITEEEKERIY GILGQAVCRP AGIQDEDITL QITESEDNEE DDMVDVIWRQ LISSCPWLSE LDESATEGVI KVWRKVVDRI FSLYKLSCSA YFTFLKLNAG QIPLDEDDPR LHLSHRVEQS TDDMIVMATL RLLRLLVKHA GELRQYLEHG LETTPTAPWR GIIPQLFSRL NHPEVYVRQS ICNLLCRVAQ DSPHLILYPA IVGTISLSSE SQASGNKFST AIPTLLGNIQ GEELLVSECE GGSPPASQDS NKDEPKSGLN EDQAMMQDCY SKIVDKLSSA NPTMVLQVQM LVAELRRVTV LWDELWLGVL LQQHMYVLRR IQQLEDEVKR VQNNNTLRKE EKIAIMREKH TALMKPIVFA LEHVRSITAA PAETPHEKWF QDNYGDAIEN ALEKLKTPLN PAKPGSSWIP FKEIMLSLQQ RAQKRASYIL RLEEISPWLA AMTNTEIALP GEVSARDTVT IHSVGGTITI LPTKTKPKKL LFLGSDGKSY PYLFKGLEDL HLDERIMQFL SIVNTMFATI NRQETPRFHA RHYSVTPLGT RSGLIQWVDG ATPLFGLYKR WQQREAALQA QKAQDSYQTP QNPGIVPRPS ELYYSKIGPA LKTVGLSLDV SRRDWPLHVM KAVLEELMEA TPPNLLAKEL WSSCTTPDEW WRVTQSYARS TAVMSMVGYI IGLGDRHLDN VLIDMTTGEV VHIDYNVCFE KGKSLRVPEK VPFRMTQNIE TALGVTGVEG VFRLSCEQVL HIMRRGRETL LTLLEAFVYD PLVDWTAGGE AGFAGAVYGG GGQQAESKQS KREMEREITR SLFSSRVAEI KVNWFKNRDE MLVVLPKLDG SLDEYLSLQE QLTDVEKLQG KLLEEIEFLE GAEGVDHPSH TLQHRYSEHT QLQTQQRAVQ EAIQVKLNEF EQWITHYQAA FNNLEATQLA SLLQEISTQM DLGPPSYVPA TAFLQNAGQA HLISQCEQLE GEVGALLQQR RSVLRGCLEQ LHHYATVALQ YPKAIFQKHR IEQWKTWMEE LICNTTVERC QELYRKYEMQ YAPQPPPTVC QFITATEMTL QRYAADINSR LIRQVERLKQ EAVTVPVCED QLKEIERCIK VFLHENGEEG SLSLASVIIS ALCTLTRRNL MMEGAASSAG EQLVDLTSRD GAWFLEELCS MSGNVTCLVQ LLKQCHLVPQ DLDIPNPMEA SETVHLANGV YTSLQELNSN FRQIIFPEAL RCLMKGEYTL ESMLHELDGL IEQTTDGVPL QTLVESLQAY LRNAAMGLEE ETHAHYIDVA RLLHAQYGEL IQPRNGSVDE TPKMSAGQML LVAFDGMFAQ VETAFSLLVE KLNKMEIPIA WRKIDIIREA RSTQVNFFDD DNHRQVLEEI FFLKRLQTIK EFFRLCGTFS KTLSGSSSLE DQNTVNGPVQ IVNVKTLFRN SCFSEDQMAK PIKAFTADFV RQLLIGLPNQ ALGLTLCSFI SALGVDIIAQ VEAKDFGAES KVSVDDLCKK AVEHNIQIGK FSQLVMNRAT VLASSYDTAW KKHDLVRRLE TSISSCKTSL QRVQLHIAMF QWQHEDLLIN RPQAMSVTPP PRSAILTSMK KKLHTLSQIE TSIATVQEKL AALESSIEQR LKWAGGANPA LAPVLQDFEA TIAERRNLVL KESQRASQVT FLCSNIIHFE SLRTRTAEAL NLDAALFELI KRCQQMCSFA SQFNSSVSEL ELRLLQRVDT GLEHPIGSSE WLLSAHKQLT QDMSTQRAIQ TEKEQQIETV CETIQNLVDN IKTVLTGHNR QLGDVKHLLK AMAKDEEAAL ADGEDVPYEN SVRQFLGEYK SWQDNIQTVL FTLVQAMGQV RSQEHVEMLQ EITPTLKELK TQSQSIYNNL VSFASPLVTD ATNECSSPTS SATYQPSFAA AVRSNTGQKT QPDVMSQNAR KLIQKNLATS ADTPPSTVPG TGKSVACSPK KAVRDPKTGK AVQERNSYAV SVWKRVKAKL EGRDVDPNRR MSVAEQVDYV IKEATNLDNL AQLYEGWTAW V //