ID SG196_HUMAN Reviewed; 350 AA. AC Q9H5K3; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 168. DE RecName: Full=Protein O-mannose kinase; DE Short=POMK; DE EC=2.7.1.183 {ECO:0000269|PubMed:23929950}; DE AltName: Full=Protein kinase-like protein SgK196; DE AltName: Full=Sugen kinase 196; GN Name=POMK; Synonyms=SGK196; 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 [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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP IDENTIFICATION. RX PubMed=12471243; DOI=10.1126/science.1075762; RA Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S.; RT "The protein kinase complement of the human genome."; RL Science 298:1912-1934(2002). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [6] RP VARIANTS [LARGE SCALE ANALYSIS] PRO-48; PHE-140; MET-254; THR-301 AND RP ILE-342. 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). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP CHARACTERIZATION OF VARIANT MDDGA12 ARG-137. RX PubMed=23929950; DOI=10.1126/science.1239951; RA Yoshida-Moriguchi T., Willer T., Anderson M.E., Venzke D., Whyte T., RA Muntoni F., Lee H., Nelson S.F., Yu L., Campbell K.P.; RT "SGK196 is a glycosylation-specific O-mannose kinase required for RT dystroglycan function."; RL Science 341:896-899(2013). RN [8] RP INVOLVEMENT IN MDDGA12. RX PubMed=24556084; DOI=10.1136/jmedgenet-2013-102236; RA von Renesse A., Petkova M.V., Luetzkendorf S., Heinemeyer J., Gill E., RA Huebner C., von Moers A., Stenzel W., Schuelke M.; RT "POMK mutation in a family with congenital muscular dystrophy with merosin RT deficiency, hypomyelination, mild hearing deficit and intellectual RT disability."; RL J. Med. Genet. 51:275-282(2014). RN [9] RP TISSUE SPECIFICITY, INVOLVEMENT IN MDDGC12, AND VARIANT MDDGA12 ASP-302. RX PubMed=24925318; DOI=10.1093/hmg/ddu296; RA Di Costanzo S., Balasubramanian A., Pond H.L., Rozkalne A., Pantaleoni C., RA Saredi S., Gupta V.A., Sunu C.M., Yu T.W., Kang P.B., Salih M.A., Mora M., RA Gussoni E., Walsh C.A., Manzini M.C.; RT "POMK mutations disrupt muscle development leading to a spectrum of RT neuromuscular presentations."; RL Hum. Mol. Genet. 23:5781-5792(2014). RN [10] RP VARIANTS MDDGA12 ARG-137 AND ARG-258, FUNCTION, AND INVOLVEMENT IN MDDGA12. RX PubMed=23519211; DOI=10.1126/science.1233675; RA Jae L.T., Raaben M., Riemersma M., van Beusekom E., Blomen V.A., Velds A., RA Kerkhoven R.M., Carette J.E., Topaloglu H., Meinecke P., Wessels M.W., RA Lefeber D.J., Whelan S.P., van Bokhoven H., Brummelkamp T.R.; RT "Deciphering the glycosylome of dystroglycanopathies using haploid screens RT for lassa virus entry."; RL Science 340:479-483(2013). CC -!- FUNCTION: Protein O-mannose kinase that specifically mediates CC phosphorylation at the 6-position of an O-mannose of the trisaccharide CC (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)- CC beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide CC (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4- CC (phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a CC carbohydrate structure present in alpha-dystroglycan (DAG1), which is CC required for binding laminin G-like domain-containing extracellular CC proteins with high affinity. Only shows kinase activity when the CC GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O- CC mannose, suggesting that this disaccharide serves as the substrate CC recognition motif. {ECO:0000269|PubMed:23519211, CC ECO:0000269|PubMed:23929950}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-alpha-D-Man]-L- CC Thr-[protein] + ATP = 3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)- CC (O-6-P-alpha-D-Man)]-Thr-[protein] + ADP + H(+); CC Xref=Rhea:RHEA:52616, Rhea:RHEA-COMP:13308, Rhea:RHEA-COMP:13309, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136709, CC ChEBI:CHEBI:136710, ChEBI:CHEBI:456216; EC=2.7.1.183; CC Evidence={ECO:0000269|PubMed:23929950}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.1 uM for ATP {ECO:0000269|PubMed:23929950}; CC -!- INTERACTION: CC Q9H5K3; O94766: B3GAT3; NbExp=2; IntAct=EBI-11337900, EBI-3917958; CC Q9H5K3; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-11337900, EBI-725665; CC Q9H5K3; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-11337900, EBI-12070086; CC Q9H5K3; Q8WZA1: POMGNT1; NbExp=2; IntAct=EBI-11337900, EBI-3912424; CC Q9H5K3; P04843: RPN1; NbExp=2; IntAct=EBI-11337900, EBI-355963; CC Q9H5K3; P04844: RPN2; NbExp=2; IntAct=EBI-11337900, EBI-719731; CC Q9H5K3; P46977: STT3A; NbExp=2; IntAct=EBI-11337900, EBI-719212; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; CC Single-pass type II membrane protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Highest expression is observed in brain, skeletal CC muscle, kidney and heart in fetal and adult tissues. CC {ECO:0000269|PubMed:24925318}. CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain CC and eye anomalies A12 (MDDGA12) [MIM:615249]: An autosomal recessive CC disorder characterized by congenital muscular dystrophy associated with CC cobblestone lissencephaly and other brain anomalies, eye malformations, CC profound intellectual disability, and death usually in the first years CC of life. Included diseases are the more severe Walker-Warburg syndrome CC and the slightly less severe muscle-eye-brain disease. CC {ECO:0000269|PubMed:23519211, ECO:0000269|PubMed:23929950, CC ECO:0000269|PubMed:24556084, ECO:0000269|PubMed:24925318}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C12 CC (MDDGC12) [MIM:616094]: An autosomal recessive limb-girdle congenital CC muscular dystrophy, characterized by muscle weakness and delayed motor CC development in association with cognitive impairment. CC {ECO:0000269|PubMed:24925318}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. STKL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- CAUTION: Although related to the Ser/Thr protein kinase family, has no CC protein kinase activity and acts as a mannose kinase instead. CC {ECO:0000305|PubMed:23929950}. 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; AK027009; BAB15623.1; -; mRNA. DR EMBL; AC113191; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC101548; AAI01549.1; -; mRNA. DR EMBL; BC113703; AAI13704.1; -; mRNA. DR CCDS; CCDS6141.1; -. DR RefSeq; NP_001264900.1; NM_001277971.1. DR RefSeq; NP_115613.1; NM_032237.4. DR AlphaFoldDB; Q9H5K3; -. DR SMR; Q9H5K3; -. DR BioGRID; 123942; 303. DR IntAct; Q9H5K3; 206. DR STRING; 9606.ENSP00000331258; -. DR GlyConnect; 1664; 3 N-Linked glycans (1 site). DR GlyCosmos; Q9H5K3; 4 sites, 3 glycans. DR GlyGen; Q9H5K3; 5 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q9H5K3; -. DR PhosphoSitePlus; Q9H5K3; -. DR SwissPalm; Q9H5K3; -. DR BioMuta; POMK; -. DR DMDM; 74761446; -. DR CPTAC; non-CPTAC-5675; -. DR EPD; Q9H5K3; -. DR jPOST; Q9H5K3; -. DR MassIVE; Q9H5K3; -. DR MaxQB; Q9H5K3; -. DR PaxDb; 9606-ENSP00000331258; -. DR PeptideAtlas; Q9H5K3; -. DR ProteomicsDB; 80917; -. DR Pumba; Q9H5K3; -. DR Antibodypedia; 24208; 299 antibodies from 22 providers. DR DNASU; 84197; -. DR Ensembl; ENST00000331373.10; ENSP00000331258.5; ENSG00000185900.11. DR Ensembl; ENST00000676193.1; ENSP00000502774.1; ENSG00000185900.11. DR GeneID; 84197; -. DR KEGG; hsa:84197; -. DR MANE-Select; ENST00000331373.10; ENSP00000331258.5; NM_032237.5; NP_115613.1. DR UCSC; uc003xpw.4; human. DR AGR; HGNC:26267; -. DR CTD; 84197; -. DR DisGeNET; 84197; -. DR GeneCards; POMK; -. DR HGNC; HGNC:26267; POMK. DR HPA; ENSG00000185900; Low tissue specificity. DR MalaCards; POMK; -. DR MIM; 615247; gene. DR MIM; 615249; phenotype. DR MIM; 616094; phenotype. DR neXtProt; NX_Q9H5K3; -. DR OpenTargets; ENSG00000185900; -. DR Orphanet; 370959; Congenital muscular dystrophy with cerebellar involvement. DR Orphanet; 445110; Limb-girdle muscular dystrophy due to POMK deficiency. DR Orphanet; 899; Walker-Warburg syndrome. DR VEuPathDB; HostDB:ENSG00000185900; -. DR eggNOG; ENOG502QQQV; Eukaryota. DR GeneTree; ENSGT00390000004945; -. DR HOGENOM; CLU_067581_0_0_1; -. DR InParanoid; Q9H5K3; -. DR OMA; NTWHRRL; -. DR OrthoDB; 2896800at2759; -. DR PhylomeDB; Q9H5K3; -. DR BioCyc; MetaCyc:G66-30734-MONOMER; -. DR BRENDA; 2.7.1.183; 2681. DR PathwayCommons; Q9H5K3; -. DR Reactome; R-HSA-5173105; O-linked glycosylation. DR SignaLink; Q9H5K3; -. DR BioGRID-ORCS; 84197; 14 hits in 1145 CRISPR screens. DR ChiTaRS; POMK; human. DR GenomeRNAi; 84197; -. DR Pharos; Q9H5K3; Tbio. DR PRO; PR:Q9H5K3; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9H5K3; Protein. DR Bgee; ENSG00000185900; Expressed in paraflocculus and 208 other cell types or tissues. DR ExpressionAtlas; Q9H5K3; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019200; F:carbohydrate kinase activity; IBA:GO_Central. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0007420; P:brain development; TAS:UniProtKB. DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB. DR GO; GO:0007611; P:learning or memory; IEA:Ensembl. DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl. DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB. DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR039318; POMK. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR PANTHER; PTHR22618:SF2; PROTEIN O-MANNOSE KINASE; 1. DR PANTHER; PTHR22618; UNCHARACTERIZED; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; Q9H5K3; HS. PE 1: Evidence at protein level; KW Acetylation; ATP-binding; Congenital muscular dystrophy; Disease variant; KW Dystroglycanopathy; Endoplasmic reticulum; Glycoprotein; Kinase; KW Limb-girdle muscular dystrophy; Lissencephaly; Membrane; KW Nucleotide-binding; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..350 FT /note="Protein O-mannose kinase" FT /id="PRO_0000262996" FT TOPO_DOM 1..20 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 21..43 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 44..350 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 81..350 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT CARBOHYD 165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 235 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 48 FT /note="S -> P (in dbSNP:rs34466747)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041372" FT VARIANT 137 FT /note="L -> R (in MDDGA12; loss of kinase activity; FT dbSNP:rs397509385)" FT /evidence="ECO:0000269|PubMed:23519211, FT ECO:0000269|PubMed:23929950" FT /id="VAR_069625" FT VARIANT 140 FT /note="Y -> F (in dbSNP:rs34750053)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041373" FT VARIANT 254 FT /note="V -> M (in dbSNP:rs34715198)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041374" FT VARIANT 258 FT /note="Q -> R (in MDDGA12; dbSNP:rs397509386)" FT /evidence="ECO:0000269|PubMed:23519211" FT /id="VAR_069626" FT VARIANT 301 FT /note="M -> T (in dbSNP:rs33920561)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041375" FT VARIANT 302 FT /note="V -> D (in MDDGA12; dbSNP:rs199756983)" FT /evidence="ECO:0000269|PubMed:24925318" FT /id="VAR_072560" FT VARIANT 342 FT /note="M -> I (in a lung small cell carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041376" SQ SEQUENCE 350 AA; 40050 MW; E074FDB2E5861B0F CRC64; MEKQPQNSRR GLAPREVPPA VGLLLIMALM NTLLYLCLDH FFIAPRQSTV DPTHCPYGHF RIGQMKNCSP WLSCEELRTE VRQLKRVGEG AVKRVFLSEW KEHKVALSQL TSLEMKDDFL HGLQMLKSLQ GTHVVTLLGY CEDDNTMLTE YHPLGSLSNL EETLNLSKYQ NVNTWQHRLE LAMDYVSIIN YLHHSPVGTR VMCDSNDLPK TLSQYLLTSN FSILANDLDA LPLVNHSSGM LVKCGHRELH GDFVAPEQLW PYGEDVPFHD DLMPSYDEKI DIWKIPDISS FLLGHIEGSD MVRFHLFDIH KACKSQTPSE RPTAQDVLET YQKVLDTLRD AMMSQAREML //