ID STK10_HUMAN Reviewed; 968 AA. AC O94804; A6ND35; B2R8F5; Q9UIW4; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 20-APR-2010, entry version 99. DE RecName: Full=Serine/threonine-protein kinase 10; DE EC=2.7.11.1; DE AltName: Full=Lymphocyte-oriented kinase; GN Name=STK10; Synonyms=LOK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=99216434; PubMed=10199912; DOI=10.1007/s002510050509; RA Kuramochi S., Matsuda Y., Okamoto M., Kitamura F., Yonekawa H., RA Karasuyama H.; RT "Molecular cloning of the human gene STK10 encoding lymphocyte- RT oriented kinase, and comparative chromosomal mapping of the human, RT mouse, and rat homologues."; RL Immunogenetics 49:369-375(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-968. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; 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 RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS RP SPECTROMETRY. RX PubMed=17192257; DOI=10.1074/mcp.T600062-MCP200; RA Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., RA Keri G., Wehland J., Daub H.; RT "Proteomics analysis of protein kinases by target class-selective RT prefractionation and tandem mass spectrometry."; RL Mol. Cell. Proteomics 6:537-547(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS RP SPECTROMETRY. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS RP SPECTROMETRY. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using RT sequential IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-14; SER-20; RP THR-185; SER-191; SER-392; SER-438 AND THR-952, AND MASS SPECTROMETRY. RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-185; SER-191; RP SER-438; SER-454 AND THR-952, AND MASS SPECTROMETRY. 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 [13] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-450; SER-454; RP SER-455; SER-951 AND THR-952, AND MASS SPECTROMETRY. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-20; THR-185; RP SER-191; THR-391; SER-438; SER-444; SER-448; SER-450; SER-454; RP SER-514; SER-549; SER-951 AND THR-952, AND MASS SPECTROMETRY. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND SER-450, AND RP MASS SPECTROMETRY. RC TISSUE=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 [17] RP VARIANT TGCT GLU-277. RX PubMed=16175573; DOI=10.1002/gcc.20265; RA Bignell G., Smith R., Hunter C., Stephens P., Davies H., Greenman C., RA Teague J., Butler A., Edkins S., Stevens C., O'meara S., Parker A., RA Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J., RA Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., RA Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., RA Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., RA Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., RA West S., Widaa S., Yates A., Gillis A.J.M., Stoop H.J., RA van Gurp R.J.H.L.M., Oosterhuis J.W., Looijenga L.H.J., Futreal P.A., RA Wooster R., Stratton M.R.; RT "Sequence analysis of the protein kinase gene family in human RT testicular germ-cell tumors of adolescents and adults."; RL Genes Chromosomes Cancer 45:42-46(2006). RN [18] RP VARIANTS [LARGE SCALE ANALYSIS] CYS-268; GLU-277; TRP-322; ILE-336; RP SER-467; THR-710; LEU-853; THR-905 AND TYR-947. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Can act on substrates such as myelin basic protein and CC histone 2A on serine and threonine residues (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in lymphoid organs. CC -!- PTM: Autophosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. STE20 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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; AB015718; BAA35073.1; -; mRNA. DR EMBL; AK313350; BAG36152.1; -; mRNA. DR EMBL; AC024561; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW61439.1; -; Genomic_DNA. DR EMBL; AL133081; CAB61400.1; -; mRNA. DR IPI; IPI00304742; -. DR PIR; T42687; T42687. DR RefSeq; NP_005981.3; -. DR UniGene; Hs.519756; -. DR PDB; 2J7T; X-ray; 2.00 A; A=18-317. DR PDBsum; 2J7T; -. DR STRING; O94804; -. DR PhosphoSite; O94804; -. DR PRIDE; O94804; -. DR Ensembl; ENST00000176763; ENSP00000176763; ENSG00000072786; Homo sapiens. DR GeneID; 6793; -. DR KEGG; hsa:6793; -. DR UCSC; uc003mbo.1; human. DR CTD; 6793; -. DR GeneCards; GC05M171403; -. DR H-InvDB; HIX0005414; -. DR HGNC; HGNC:11388; STK10. DR MIM; 603919; gene. DR PharmGKB; PA36197; -. DR eggNOG; prNOG12234; -. DR HOGENOM; HBG444013; -. DR HOVERGEN; HBG052712; -. DR InParanoid; O94804; -. DR OMA; ASQSRPN; -. DR OrthoDB; EOG9HQH3T; -. DR PhylomeDB; O94804; -. DR BRENDA; 2.7.11.1; 247. DR NextBio; 26535; -. DR ArrayExpress; O94804; -. DR Bgee; O94804; -. DR CleanEx; HS_STK10; -. DR Genevestigator; O94804; -. DR GermOnline; ENSG00000072786; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS:ProtInc. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR022165; PKK. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR017442; Se/Thr_prot_kinase-like_dom. DR InterPro; IPR008271; Ser/Thr_prot_kinase_AS. DR InterPro; IPR002290; Ser/Thr_prot_kinase_dom. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF12474; PKK; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Kinase_like; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coiled coil; Complete proteome; Kinase; KW Nucleotide-binding; Phosphoprotein; Polymorphism; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 968 Serine/threonine-protein kinase 10. FT /FTId=PRO_0000086697. FT DOMAIN 36 294 Protein kinase. FT NP_BIND 42 50 ATP (By similarity). FT COILED 573 947 Potential. FT COMPBIAS 750 884 Gln-rich. FT ACT_SITE 157 157 Proton acceptor (By similarity). FT BINDING 65 65 ATP (By similarity). FT MOD_RES 13 13 Phosphoserine. FT MOD_RES 14 14 Phosphothreonine. FT MOD_RES 20 20 Phosphoserine. FT MOD_RES 185 185 Phosphothreonine. FT MOD_RES 191 191 Phosphoserine. FT MOD_RES 391 391 Phosphothreonine. FT MOD_RES 392 392 Phosphoserine. FT MOD_RES 438 438 Phosphoserine. FT MOD_RES 444 444 Phosphoserine. FT MOD_RES 448 448 Phosphoserine. FT MOD_RES 450 450 Phosphoserine. FT MOD_RES 454 454 Phosphoserine. FT MOD_RES 455 455 Phosphoserine. FT MOD_RES 514 514 Phosphoserine. FT MOD_RES 549 549 Phosphoserine. FT MOD_RES 951 951 Phosphoserine. FT MOD_RES 952 952 Phosphothreonine. FT VARIANT 268 268 R -> C (in dbSNP:rs35826078). FT /FTId=VAR_041131. FT VARIANT 277 277 K -> E (in a testicular germ cell tumor; FT somatic mutation). FT /FTId=VAR_023827. FT VARIANT 322 322 R -> W (in dbSNP:rs56214442). FT /FTId=VAR_041132. FT VARIANT 336 336 T -> I (in dbSNP:rs55972616). FT /FTId=VAR_041133. FT VARIANT 467 467 N -> S (in dbSNP:rs56063773). FT /FTId=VAR_041134. FT VARIANT 480 480 P -> L (in dbSNP:rs34505340). FT /FTId=VAR_051671. FT VARIANT 520 520 P -> L (in dbSNP:rs17074311). FT /FTId=VAR_051672. FT VARIANT 710 710 M -> T (in dbSNP:rs34936670). FT /FTId=VAR_041135. FT VARIANT 853 853 S -> L (in dbSNP:rs56066852). FT /FTId=VAR_041136. FT VARIANT 905 905 S -> T (in dbSNP:rs55791916). FT /FTId=VAR_041137. FT VARIANT 942 942 S -> N (in dbSNP:rs1128204). FT /FTId=VAR_051673. FT VARIANT 947 947 C -> Y (in dbSNP:rs56355550). FT /FTId=VAR_041138. FT STRAND 27 30 FT HELIX 32 34 FT STRAND 36 43 FT STRAND 50 55 FT TURN 56 58 FT STRAND 61 67 FT HELIX 75 87 FT STRAND 96 101 FT STRAND 106 111 FT HELIX 118 125 FT HELIX 131 150 FT HELIX 160 162 FT STRAND 163 165 FT STRAND 171 173 FT HELIX 177 187 FT HELIX 196 198 FT HELIX 201 208 FT TURN 212 216 FT HELIX 217 232 FT TURN 236 239 FT HELIX 242 251 FT HELIX 260 262 FT HELIX 265 274 FT TURN 279 281 FT HELIX 285 288 FT TURN 292 296 FT HELIX 301 314 SQ SEQUENCE 968 AA; 112135 MW; 15E245193ECC553D CRC64; MAFANFRRIL RLSTFEKRKS REYEHVRRDL DPNEVWEIVG ELGDGAFGKV YKAKNKETGA LAAAKVIETK SEEELEDYIV EIEILATCDH PYIVKLLGAY YHDGKLWIMI EFCPGGAVDA IMLELDRGLT EPQIQVVCRQ MLEALNFLHS KRIIHRDLKA GNVLMTLEGD IRLADFGVSA KNLKTLQKRD SFIGTPYWMA PEVVMCETMK DTPYDYKADI WSLGITLIEM AQIEPPHHEL NPMRVLLKIA KSDPPTLLTP SKWSVEFRDF LKIALDKNPE TRPSAAQLLE HPFVSSITSN KALRELVAEA KAEVMEEIED GRDEGEEEDA VDAASTLENH TQNSSEVSPP SLNADKPLEE SPSTPLAPSQ SQDSVNEPCS QPSGDRSLQT TSPPVVAPGN ENGLAVPVPL RKSRPVSMDA RIQVAQEKQV AEQGGDLSPA ANRSQKASQS RPNSSALETL GGEKLANGSL EPPAQAAPGP SKRDSDCSSL CTSESMDYGT NLSTDLSLNK EMGSLSIKDP KLYKKTLKRT RKFVVDGVEV SITTSKIISE DEKKDEEMRF LRRQELRELR LLQKEEHRNQ TQLSNKHELQ LEQMHKRFEQ EINAKKKFFD TELENLERQQ KQQVEKMEQD HAVRRREEAR RIRLEQDRDY TRFQEQLKLM KKEVKNEVEK LPRQQRKESM KQKMEEHTQK KQLLDRDFVA KQKEDLELAM KRLTTDNRRE ICDKERECLM KKQELLRDRE AALWEMEEHQ LQERHQLVKQ QLKDQYFLQR HELLRKHEKE REQMQRYNQR MIEQLKVRQQ QEKARLPKIQ RSEGKTRMAM YKKSLHINGG GSAAEQREKI KQFSQQEEKR QKSERLQQQQ KHENQMRDML AQCESNMSEL QQLQNEKCHL LVEHETQKLK ALDESHNQNL KEWRDKLRPR KKALEEDLNQ KKREQEMFFK LSEEAECPNP STPSKAAKFF PYSSADAS //