ID   MYLK3_HUMAN             Reviewed;         819 AA.
AC   Q32MK0; B5BUL9; B7Z5U8; Q32MK1; Q96DV1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 3.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Myosin light chain kinase 3;
DE            EC=2.7.11.18;
DE   AltName: Full=Cardiac-MyBP-C-associated Ca/CaM kinase;
DE            Short=Cardiac-MLCK;
GN   Name=MYLK3; Synonyms=MLCK;
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 1), AND VARIANT LEU-180.
RC   TISSUE=Cardiac myocyte;
RA   Mues A., Seidel R., Gautel M.;
RT   "The cardiac-MyBP-C associated Ca/CaM kinase is a novel MLCK with cardiac-
RT   specific domains.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Tongue;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA   Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA   Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA   Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA   Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA   Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA   Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in vitro-
RT   expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-180.
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   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=17885681; DOI=10.1172/jci30804;
RA   Seguchi O., Takashima S., Yamazaki S., Asakura M., Asano Y., Shintani Y.,
RA   Wakeno M., Minamino T., Kondo H., Furukawa H., Nakamaru K., Naito A.,
RA   Takahashi T., Ohtsuka T., Kawakami K., Isomura T., Kitamura S., Tomoike H.,
RA   Mochizuki N., Kitakaze M.;
RT   "A cardiac myosin light chain kinase regulates sarcomere assembly in the
RT   vertebrate heart.";
RL   J. Clin. Invest. 117:2812-2824(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-408, AND
RP   IDENTIFICATION BY 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   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] ARG-390.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Kinase that phosphorylates MYL2 in vitro. Promotes sarcomere
CC       formation in cardiomyocytes and increases cardiomyocyte contractility
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-
CC         seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-
CC         COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.18;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-
CC         phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900,
CC         Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:456216; EC=2.7.11.18;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- INTERACTION:
CC       Q32MK0; P62258: YWHAE; NbExp=2; IntAct=EBI-1222801, EBI-356498;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q32MK0-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q32MK0-4; Sequence=VSP_044312;
CC   -!- TISSUE SPECIFICITY: Restricted to heart. {ECO:0000269|PubMed:17885681}.
CC   -!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI09098.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAC42766.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ247087; CAC42766.1; ALT_INIT; mRNA.
DR   EMBL; AK299443; BAH13034.1; -; mRNA.
DR   EMBL; AB451455; BAG70269.1; -; mRNA.
DR   EMBL; AC007225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC109097; AAI09098.2; ALT_INIT; mRNA.
DR   CCDS; CCDS10723.2; -. [Q32MK0-3]
DR   CCDS; CCDS76861.1; -. [Q32MK0-4]
DR   RefSeq; NP_001295230.1; NM_001308301.1. [Q32MK0-4]
DR   RefSeq; NP_872299.2; NM_182493.2. [Q32MK0-3]
DR   RefSeq; XP_006721397.1; XM_006721334.3.
DR   AlphaFoldDB; Q32MK0; -.
DR   SMR; Q32MK0; -.
DR   BioGRID; 124881; 11.
DR   IntAct; Q32MK0; 7.
DR   STRING; 9606.ENSP00000378288; -.
DR   BindingDB; Q32MK0; -.
DR   ChEMBL; CHEMBL4627; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; Q32MK0; -.
DR   iPTMnet; Q32MK0; -.
DR   PhosphoSitePlus; Q32MK0; -.
DR   BioMuta; MYLK3; -.
DR   DMDM; 254763411; -.
DR   jPOST; Q32MK0; -.
DR   MassIVE; Q32MK0; -.
DR   MaxQB; Q32MK0; -.
DR   PaxDb; 9606-ENSP00000378288; -.
DR   PeptideAtlas; Q32MK0; -.
DR   ProteomicsDB; 61603; -. [Q32MK0-3]
DR   ProteomicsDB; 6721; -.
DR   Pumba; Q32MK0; -.
DR   Antibodypedia; 28053; 303 antibodies from 27 providers.
DR   DNASU; 91807; -.
DR   Ensembl; ENST00000394809.9; ENSP00000378288.4; ENSG00000140795.13. [Q32MK0-3]
DR   Ensembl; ENST00000536476.5; ENSP00000439297.1; ENSG00000140795.13. [Q32MK0-4]
DR   GeneID; 91807; -.
DR   KEGG; hsa:91807; -.
DR   MANE-Select; ENST00000394809.9; ENSP00000378288.4; NM_182493.3; NP_872299.2.
DR   UCSC; uc002eei.5; human. [Q32MK0-3]
DR   AGR; HGNC:29826; -.
DR   CTD; 91807; -.
DR   DisGeNET; 91807; -.
DR   GeneCards; MYLK3; -.
DR   HGNC; HGNC:29826; MYLK3.
DR   HPA; ENSG00000140795; Group enriched (heart muscle, skeletal muscle, tongue).
DR   MIM; 612147; gene.
DR   neXtProt; NX_Q32MK0; -.
DR   OpenTargets; ENSG00000140795; -.
DR   PharmGKB; PA162396375; -.
DR   VEuPathDB; HostDB:ENSG00000140795; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   GeneTree; ENSGT00940000160007; -.
DR   HOGENOM; CLU_000288_90_0_1; -.
DR   InParanoid; Q32MK0; -.
DR   OMA; IHVQEMD; -.
DR   OrthoDB; 5402680at2759; -.
DR   PhylomeDB; Q32MK0; -.
DR   TreeFam; TF314166; -.
DR   PathwayCommons; Q32MK0; -.
DR   SignaLink; Q32MK0; -.
DR   SIGNOR; Q32MK0; -.
DR   BioGRID-ORCS; 91807; 16 hits in 1185 CRISPR screens.
DR   ChiTaRS; MYLK3; human.
DR   GeneWiki; MYLK3; -.
DR   GenomeRNAi; 91807; -.
DR   Pharos; Q32MK0; Tchem.
DR   PRO; PR:Q32MK0; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q32MK0; Protein.
DR   Bgee; ENSG00000140795; Expressed in cardiac muscle of right atrium and 139 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISS:BHF-UCL.
DR   GO; GO:0004687; F:myosin light chain kinase activity; ISS:BHF-UCL.
DR   GO; GO:0055003; P:cardiac myofibril assembly; ISS:BHF-UCL.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IMP:BHF-UCL.
DR   GO; GO:0060298; P:positive regulation of sarcomere organization; ISS:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:BHF-UCL.
DR   GO; GO:0002528; P:regulation of vascular permeability involved in acute inflammatory response; IMP:BHF-UCL.
DR   GO; GO:0045214; P:sarcomere organization; ISS:BHF-UCL.
DR   GO; GO:0048769; P:sarcomerogenesis; ISS:BHF-UCL.
DR   CDD; cd14192; STKc_MLCK3; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24342:SF15; DEATH-ASSOCIATED PROTEIN KINASE 2; 1.
DR   PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q32MK0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..819
FT                   /note="Myosin light chain kinase 3"
FT                   /id="PRO_0000272200"
FT   DOMAIN          515..770
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          146..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        636
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         521..529
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         544
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:E9PT87"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:E9PT87"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         408
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..341
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044312"
FT   VARIANT         70
FT                   /note="S -> T (in dbSNP:rs9923813)"
FT                   /id="VAR_058335"
FT   VARIANT         180
FT                   /note="V -> L (in dbSNP:rs28407821)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT                   /id="VAR_058336"
FT   VARIANT         390
FT                   /note="G -> R (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs141602742)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035630"
FT   CONFLICT        149
FT                   /note="R -> G (in Ref. 2; BAG70269)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="G -> R (in Ref. 1; CAC42766)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   819 AA;  88393 MW;  21148BBACB0FF0D9 CRC64;
     MSGTSKESLG HGGLPGLGKT CLTTMDTKLN MLNEKVDQLL HFQEDVTEKL QSMCRDMGHL
     ERGLHRLEAS RAPGPGGADG VPHIDTQAGW PEVLELVRAM QQDAAQHGAR LEALFRMVAA
     VDRAIALVGA TFQKSKVADF LMQGRVPWRR GSPGDSPEEN KERVEEEGGK PKHVLSTSGV
     QSDAREPGEE SQKADVLEGT AERLPPIRAS GLGADPAQAV VSPGQGDGVP GPAQAFPGHL
     PLPTKVEAKA PETPSENLRT GLELAPAPGR VNVVSPSLEV APGAGQGASS SRPDPEPLEE
     GTRLTPGPGP QCPGPPGLPA QARATHSGGE TPPRISIHIQ EMDTPGEMLM TGRGSLGPTL
     TTEAPAAAQP GKQGPPGTGR CLQAPGTEPG EQTPEGAREL SPLQESSSPG GVKAEEEQRA
     GAEPGTRPSL ARSDDNDHEV GALGLQQGKS PGAGNPEPEQ DCAARAPVRA EAVRRMPPGA
     EAGSVVLDDS PAPPAPFEHR VVSVKETSIS AGYEVCQHEV LGGGRFGQVH RCTEKSTGLP
     LAAKIIKVKS AKDREDVKNE INIMNQLSHV NLIQLYDAFE SKHSCTLVME YVDGGELFDR
     ITDEKYHLTE LDVVLFTRQI CEGVHYLHQH YILHLDLKPE NILCVNQTGH QIKIIDFGLA
     RRYKPREKLK VNFGTPEFLA PEVVNYEFVS FPTDMWSVGV ITYMLLSGLS PFLGETDAET
     MNFIVNCSWD FDADTFEGLS EEAKDFVSRL LVKEKSCRMS ATQCLKHEWL NNLPAKASRS
     KTRLKSQLLL QKYIAQRKWK KHFYVVTAAN RLRKFPTSP
//