STK3_MOUSE
ID STK3_MOUSE Reviewed; 497 AA.
AC Q9JI10; Q60877; Q80UG4; Q8CI58;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Serine/threonine-protein kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=Mammalian STE20-like protein kinase 2;
DE Short=MST-2;
DE AltName: Full=STE20-like kinase MST2;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase 3 36kDa subunit;
DE Short=MST2/N;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase 3 20kDa subunit;
DE Short=MST2/C;
GN Name=Stk3; Synonyms=Mess1, Mst2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEOLYTIC PROCESSING.
RC STRAIN=BALB/cJ;
RX PubMed=11278283; DOI=10.1074/jbc.m005109200;
RA Lee K.-K., Ohyama T., Yajima N., Tsubuki S., Yonehara S.;
RT "MST, a physiological caspase substrate, highly sensitizes apoptosis both
RT upstream and downstream of caspase activation.";
RL J. Biol. Chem. 276:19276-19285(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Han J.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Olfactory epithelium;
RA de las Heras R., Mackay-Sim A., Bushell G.R.;
RT "Molecular cloning and characterization of mouse MST2 kinase from olfactory
RT receptor neurons.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-316 AND SER-391, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21145499; DOI=10.1016/j.devcel.2010.11.012;
RA Varelas X., Samavarchi-Tehrani P., Narimatsu M., Weiss A., Cockburn K.,
RA Larsen B.G., Rossant J., Wrana J.L.;
RT "The Crumbs complex couples cell density sensing to Hippo-dependent control
RT of the TGF-beta-SMAD pathway.";
RL Dev. Cell 19:831-844(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20080689; DOI=10.1073/pnas.0911427107;
RA Lu L., Li Y., Kim S.M., Bossuyt W., Liu P., Qiu Q., Wang Y., Halder G.,
RA Finegold M.J., Lee J.S., Johnson R.L.;
RT "Hippo signaling is a potent in vivo growth and tumor suppressor pathway in
RT the mammalian liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1437-1442(2010).
RN [11]
RP INTERACTION WITH DLG5.
RX PubMed=28087714; DOI=10.1101/gad.284539.116;
RA Kwan J., Sczaniecka A., Arash E.H., Nguyen L., Chen C.C., Ratkovic S.,
RA Klezovitch O., Attisano L., McNeill H., Emili A., Vasioukhin V.;
RT "DLG5 connects cell polarity and Hippo signaling protein networks by
RT linking PAR-1 with MST1/2.";
RL Genes Dev. 30:2696-2709(2016).
CC -!- FUNCTION: Stress-activated, pro-apoptotic kinase which, following
CC caspase-cleavage, enters the nucleus and induces chromatin condensation
CC followed by internucleosomal DNA fragmentation. Key component of the
CC Hippo signaling pathway which plays a pivotal role in organ size
CC control and tumor suppression by restricting proliferation and
CC promoting apoptosis. The core of this pathway is composed of a kinase
CC cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory
CC protein SAV1, phosphorylates and activates LATS1/2 in complex with its
CC regulatory protein MOB1, which in turn phosphorylates and inactivates
CC YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2
CC inhibits its translocation into the nucleus to regulate cellular genes
CC important for cell proliferation, cell death, and cell migration.
CC STK3/MST2 and STK4/MST1 are required to repress proliferation of mature
CC hepatocytes, to prevent activation of facultative adult liver stem
CC cells (oval cells), and to inhibit tumor formation. Phosphorylates
CC NKX2-1. Phosphorylates NEK2 and plays a role in centrosome disjunction
CC by regulating the localization of NEK2 to centrosomes, and its ability
CC to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates
CC the transcriptional activity of ESR1 through the modulation of its
CC phosphorylation. Positively regulates RAF1 activation via suppression
CC of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates
CC MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts
CC cooperatively with MOBKL1B to activate STK38 (By similarity).
CC {ECO:0000250|UniProtKB:Q13188, ECO:0000269|PubMed:20080689}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by the C-terminal non-catalytic region.
CC Activated by caspase-cleavage. Full activation also requires
CC homodimerization and autophosphorylation of Thr-180, which are
CC inhibited by the proto-oncogene product RAF1. Activated by RASSF1 which
CC acts by preventing its dephosphorylation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; mediated via the coiled-coil region. Interacts with
CC NORE1, which inhibits autoactivation. Interacts with and stabilizes
CC SAV1. Interacts with RAF1, which prevents dimerization and
CC phosphorylation. Interacts with RASSF1. Interacts (via SARAH domain)
CC with NEK2. Interacts with ESR1 only in the presence of SAV1. Interacts
CC with PKB/AKT1. Forms a tripartite complex with MOBKL1B and STK38.
CC Interacts with RASSF2 (via SARAH domain). Interacts with LATS1; this
CC interaction is inhibited in the presence of DLG5. Interacts with MARK3
CC in the presence of DLG5 (By similarity). Interacts with DLG5 (via PDZ
CC domain 3) (PubMed:28087714). {ECO:0000250|UniProtKB:Q13188,
CC ECO:0000269|PubMed:28087714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21145499}. Nucleus
CC {ECO:0000269|PubMed:21145499}. Note=The caspase-cleaved form cycles
CC between nucleus and cytoplasm (By similarity). Phosphorylation at Thr-
CC 117 leads to inhibition of nuclear translocation (By similarity).
CC {ECO:0000250|UniProtKB:Q13188}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JI10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JI10-2; Sequence=VSP_020047;
CC -!- PTM: Phosphorylation at Thr-117 and Thr-390 by PKB/AKT1, leads to
CC inhibition of its: cleavage, kinase activity, autophosphorylation at
CC Thr-180, binding to RASSF1 and nuclear translocation, and increase in
CC its binding to RAF1. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic
CC cleavage results in kinase activation and nuclear translocation of the
CC truncated form (MST1/N). {ECO:0000269|PubMed:11278283}.
CC -!- DISRUPTION PHENOTYPE: Mice show progressive hepatomegaly with a 2-fold
CC increase in liver mass relative to total body mass at 1 month of age
CC and a 3-fold increase by 3 months of age.
CC {ECO:0000269|PubMed:20080689}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA75300.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF271361; AAF75790.1; -; mRNA.
DR EMBL; U28726; AAA75300.1; ALT_FRAME; mRNA.
DR EMBL; AY058922; AAL29682.1; -; mRNA.
DR EMBL; BC037440; AAH37440.1; -; mRNA.
DR EMBL; BC049123; AAH49123.2; -; mRNA.
DR CCDS; CCDS37059.1; -. [Q9JI10-1]
DR RefSeq; NP_062609.2; NM_019635.2. [Q9JI10-1]
DR AlphaFoldDB; Q9JI10; -.
DR SMR; Q9JI10; -.
DR BioGRID; 207869; 2.
DR DIP; DIP-61760N; -.
DR IntAct; Q9JI10; 4.
DR MINT; Q9JI10; -.
DR STRING; 10090.ENSMUSP00000018476; -.
DR BindingDB; Q9JI10; -.
DR ChEMBL; CHEMBL4310; -.
DR DrugCentral; Q9JI10; -.
DR iPTMnet; Q9JI10; -.
DR PhosphoSitePlus; Q9JI10; -.
DR EPD; Q9JI10; -.
DR jPOST; Q9JI10; -.
DR MaxQB; Q9JI10; -.
DR PaxDb; Q9JI10; -.
DR PeptideAtlas; Q9JI10; -.
DR PRIDE; Q9JI10; -.
DR ProteomicsDB; 254590; -. [Q9JI10-1]
DR ProteomicsDB; 254591; -. [Q9JI10-2]
DR Antibodypedia; 26075; 489 antibodies from 42 providers.
DR DNASU; 56274; -.
DR Ensembl; ENSMUST00000018476; ENSMUSP00000018476; ENSMUSG00000022329. [Q9JI10-1]
DR Ensembl; ENSMUST00000067033; ENSMUSP00000064225; ENSMUSG00000022329. [Q9JI10-2]
DR GeneID; 56274; -.
DR KEGG; mmu:56274; -.
DR UCSC; uc007vlz.1; mouse. [Q9JI10-1]
DR UCSC; uc011zrz.1; mouse. [Q9JI10-2]
DR CTD; 6788; -.
DR MGI; MGI:1928487; Stk3.
DR VEuPathDB; HostDB:ENSMUSG00000022329; -.
DR eggNOG; KOG0574; Eukaryota.
DR GeneTree; ENSGT00940000154984; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q9JI10; -.
DR OMA; QRMANLD; -.
DR OrthoDB; 967913at2759; -.
DR PhylomeDB; Q9JI10; -.
DR TreeFam; TF354217; -.
DR BioGRID-ORCS; 56274; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Stk3; mouse.
DR PRO; PR:Q9JI10; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9JI10; protein.
DR Bgee; ENSMUSG00000022329; Expressed in embryonic post-anal tail and 250 other tissues.
DR ExpressionAtlas; Q9JI10; baseline and differential.
DR Genevisible; Q9JI10; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IGI:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0007417; P:central nervous system development; IGI:MGI.
DR GO; GO:0003157; P:endocardium development; IGI:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IGI:MGI.
DR GO; GO:0035329; P:hippo signaling; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IGI:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:0046621; P:negative regulation of organ growth; IGI:MGI.
DR GO; GO:0001841; P:neural tube formation; IGI:MGI.
DR GO; GO:0035265; P:organ growth; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IGI:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IGI:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IGI:MGI.
DR GO; GO:0060215; P:primitive hemopoiesis; IGI:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0060800; P:regulation of cell differentiation involved in embryonic placenta development; IGI:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024205; Mst1_SARAH_domain.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011524; SARAH_dom.
DR Pfam; PF11629; Mst1_SARAH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50951; SARAH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; ATP-binding; Coiled coil;
KW Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..497
FT /note="Serine/threonine-protein kinase 3"
FT /id="PRO_0000086690"
FT CHAIN 1..322
FT /note="Serine/threonine-protein kinase 3 36kDa subunit"
FT /id="PRO_0000413715"
FT CHAIN 323..497
FT /note="Serine/threonine-protein kinase 3 20kDa subunit"
FT /id="PRO_0000413716"
FT DOMAIN 27..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 443..490
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 287..328
FT /evidence="ECO:0000255"
FT COILED 366..387
FT /evidence="ECO:0000255"
FT COILED 448..479
FT /evidence="ECO:0000255"
FT COMPBIAS 327..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 322..323
FT /note="Cleavage; by caspase-3"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13188"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 117
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q13188"
FT MOD_RES 180
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O54748"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13188"
FT MOD_RES 390
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q13188"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13188"
FT VAR_SEQ 9..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020047"
SQ SEQUENCE 497 AA; 56855 MW; 9CDD365437581665 CRC64;
MEQPPASKSK LKKLSEDSLT KQPEEVFDVL EKLGEGSYGS VFKAIHKESG QVVAIKQVPV
ESDLQEIIKE ISIMQQCDSP YVVKYYGSYF KNTDLWIVME YCGAGSVSDI IRLRNKTLTE
DEIATILKST LKGLEYLHFM RKIHRDIKAG NILLNTEGHA KLADFGVAGQ LTDTMAKRNT
VIGTPFWMAP EVIQEIGYNC VADIWSLGIT SIEMAEGKPP YADIHPMRAI FMIPTNPPPT
FRKPELWSDD FTDFVKKCLV KSPEQRATAT QLLQHPFIKN AKPVSILRDL IAEAMEIKAK
RHEEQQRELE EEEENSDEDE LDSHTMVKTS SESVGTMRAT STMSEGAQTM IEHNSTMLES
DLGTMVINSE EEEEEEEEEE EDGTMKRNAT SPQVQRPSFM DYFDKQDFKN KSHENCDQSM
REPGPMSNSV FPDNWRVPQD GDFDFLKNLS LEELQMRLKA LDPMMEREIE ELHQRYSAKR
QPILDAMDAK KRRQQNF
