DYR1A_MOUSE
ID DYR1A_MOUSE Reviewed; 763 AA.
AC Q61214;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 1A;
DE EC=2.7.12.1 {ECO:0000269|PubMed:20167603};
DE AltName: Full=Dual specificity YAK1-related kinase;
DE AltName: Full=MP86;
DE AltName: Full=Protein kinase minibrain homolog;
DE Short=MNBH;
GN Name=Dyrk1a; Synonyms=Dyrk;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=8975710; DOI=10.1006/geno.1996.0636;
RA Song W.J., Sternberg L.R., Kasten-Sportes C., van Keuren M.L., Chung S.H.,
RA Slack A.C., Miller D.E., Glover T.W., Chiang P.W., Lou L., Kurnit D.W.;
RT "Isolation of human and murine homologues of the Drosophila minibrain gene:
RT human homologue maps to 21q22.2 in the Down syndrome 'critical region'.";
RL Genomics 38:331-339(1996).
RN [2]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9070862; DOI=10.1006/bbrc.1997.6154;
RA Song W.J., Chung S.H., Kurnit D.M.;
RT "The murine Dyrk protein maps to chromosome 16, localizes to the nucleus,
RT and can form multimers.";
RL Biochem. Biophys. Res. Commun. 231:640-644(1997).
RN [3]
RP INTERACTION WITH RAD54L2.
RX PubMed=15199138; DOI=10.1128/mcb.24.13.5821-5834.2004;
RA Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.;
RT "Dyrk1A potentiates steroid hormone-induced transcription via the chromatin
RT remodeling factor Arip4.";
RL Mol. Cell. Biol. 24:5821-5834(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP FUNCTION, INTERACTION WITH SEPTIN4 AND SEPTIN5, AND TISSUE SPECIFICITY.
RX PubMed=18938227; DOI=10.1016/j.neuroscience.2008.09.034;
RA Sitz J.H., Baumgaertel K., Haemmerle B., Papadopoulos C., Hekerman P.,
RA Tejedor F.J., Becker W., Lutz B.;
RT "The Down syndrome candidate dual-specificity tyrosine phosphorylation-
RT regulated kinase 1A phosphorylates the neurodegeneration-related septin
RT 4.";
RL Neuroscience 157:596-605(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-748 AND SER-758, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, and Spleen;
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 [7]
RP FUNCTION, INTERACTION WITH SIRT1, AND CATALYTIC ACTIVITY.
RX PubMed=20167603; DOI=10.1074/jbc.m110.102574;
RA Guo X., Williams J.G., Schug T.T., Li X.;
RT "DYRK1A and DYRK3 promote cell survival through phosphorylation and
RT activation of SIRT1.";
RL J. Biol. Chem. 285:13223-13232(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH CRY2.
RX PubMed=20123978; DOI=10.1128/mcb.01047-09;
RA Kurabayashi N., Hirota T., Sakai M., Sanada K., Fukada Y.;
RT "DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism
RT directing proteasomal degradation of CRY2 for circadian timekeeping.";
RL Mol. Cell. Biol. 30:1757-1768(2010).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=22998443; DOI=10.1021/jm301034u;
RA Tahtouh T., Elkins J.M., Filippakopoulos P., Soundararajan M., Burgy G.,
RA Durieu E., Cochet C., Schmid R.S., Lo D.C., Delhommel F., Oberholzer A.E.,
RA Pearl L.H., Carreaux F., Bazureau J.P., Knapp S., Meijer L.;
RT "Selectivity, cocrystal structures, and neuroprotective properties of
RT leucettines, a family of protein kinase inhibitors derived from the marine
RT sponge alkaloid leucettamine B.";
RL J. Med. Chem. 55:9312-9330(2012).
CC -!- FUNCTION: Dual-specificity kinase which possesses both serine/threonine
CC and tyrosine kinase activities (PubMed:18938227). Plays an important
CC role in double-strand breaks (DSBs) repair following DNA damage.
CC Mechanistically, phosphorylates RNF169 and increases its ability to
CC block accumulation of TP53BP1 at the DSB sites thereby promoting
CC homologous recombination repair (HRR) (By similarity). May play a role
CC in a signaling pathway regulating nuclear functions of cell
CC proliferation. Modulates alternative splicing by phosphorylating the
CC splice factor SRSF6 (By similarity). Exhibits a substrate preference
CC for proline at position P+1 and arginine at position P-3. Has pro-
CC survival function and negatively regulates the apoptotic process.
CC Promotes cell survival upon genotoxic stress through phosphorylation of
CC SIRT1. This in turn inhibits TP53 activity and apoptosis
CC (PubMed:20167603). Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-
CC 434' (PubMed:18938227). {ECO:0000250|UniProtKB:Q9NR20,
CC ECO:0000269|PubMed:18938227, ECO:0000269|PubMed:20123978,
CC ECO:0000269|PubMed:20167603}.
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=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:20167603};
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=2.7.12.1; Evidence={ECO:0000269|PubMed:20167603};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:20167603};
CC -!- ACTIVITY REGULATION: Inhibited by RANBP9.
CC {ECO:0000250|UniProtKB:Q13627}.
CC -!- SUBUNIT: Interacts with RANBP9 (By similarity). Interacts with
CC RAD54L2/ARIP4 (PubMed:15199138). Interacts with WDR68 (By similarity).
CC Interacts with CRY2 (PubMed:20123978). Interacts with SIRT1
CC (PubMed:20167603). Interacts with SEPTIN4 and SEPTIN5
CC (PubMed:18938227). {ECO:0000250|UniProtKB:Q13627,
CC ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:18938227,
CC ECO:0000269|PubMed:20123978, ECO:0000269|PubMed:20167603,
CC ECO:0000269|PubMed:9070862}.
CC -!- INTERACTION:
CC Q61214; Q61214: Dyrk1a; NbExp=2; IntAct=EBI-80344, EBI-80344;
CC Q61214; Q9JHG6: Rcan1; NbExp=2; IntAct=EBI-80344, EBI-644061;
CC Q61214; Q923E4: Sirt1; NbExp=4; IntAct=EBI-80344, EBI-1802585;
CC Q61214; P53805-2: RCAN1; Xeno; NbExp=5; IntAct=EBI-80344, EBI-1541912;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9070862}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level)
CC (PubMed:22998443). Expressed in a variety of embryonic and adult
CC tissues (PubMed:8975710). Expressed abundantly in neurons of the brain,
CC spinal cord, and retina in developing embryos (PubMed:8975710).
CC Expressed in the entorhinal, temporal and visual cortices and the
CC hippocampus of the brain where is colocalizes with SEPTIN4
CC (PubMed:18938227). Expressed and extensively colocalizes with SEPTIN4
CC in apical dendrites of pyramidal cells (PubMed:18938227). Also
CC expressed in Purkinje cells in the cerebellum in postnatal day 1 and
CC adult mice (PubMed:18938227). {ECO:0000269|PubMed:18938227,
CC ECO:0000269|PubMed:22998443, ECO:0000269|PubMed:8975710}.
CC -!- DOMAIN: The polyhistidine repeats act as targeting signals to nuclear
CC speckles. {ECO:0000250|UniProtKB:Q13627}.
CC -!- PTM: Autophosphorylated on numerous tyrosine residues. Can also
CC autophosphorylate on serine and threonine residues (in vitro) (By
CC similarity). {ECO:0000250|UniProtKB:Q13627}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
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DR EMBL; U58497; AAC52994.1; -; mRNA.
DR CCDS; CCDS28350.1; -.
DR RefSeq; NP_001106860.1; NM_001113389.1.
DR RefSeq; NP_031916.1; NM_007890.2.
DR RefSeq; XP_011244396.1; XM_011246094.2.
DR RefSeq; XP_011244397.1; XM_011246095.2.
DR AlphaFoldDB; Q61214; -.
DR SMR; Q61214; -.
DR BioGRID; 199347; 29.
DR ELM; Q61214; -.
DR IntAct; Q61214; 6.
DR MINT; Q61214; -.
DR STRING; 10090.ENSMUSP00000113660; -.
DR BindingDB; Q61214; -.
DR ChEMBL; CHEMBL4750; -.
DR iPTMnet; Q61214; -.
DR PhosphoSitePlus; Q61214; -.
DR EPD; Q61214; -.
DR jPOST; Q61214; -.
DR MaxQB; Q61214; -.
DR PaxDb; Q61214; -.
DR PRIDE; Q61214; -.
DR ProteomicsDB; 277654; -.
DR Antibodypedia; 8587; 426 antibodies from 39 providers.
DR DNASU; 13548; -.
DR Ensembl; ENSMUST00000023614; ENSMUSP00000023614; ENSMUSG00000022897.
DR Ensembl; ENSMUST00000119878; ENSMUSP00000113660; ENSMUSG00000022897.
DR GeneID; 13548; -.
DR KEGG; mmu:13548; -.
DR UCSC; uc008abg.2; mouse.
DR CTD; 1859; -.
DR MGI; MGI:1330299; Dyrk1a.
DR VEuPathDB; HostDB:ENSMUSG00000022897; -.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000157408; -.
DR InParanoid; Q61214; -.
DR OMA; PPIGWTA; -.
DR OrthoDB; 689446at2759; -.
DR PhylomeDB; Q61214; -.
DR TreeFam; TF314624; -.
DR BRENDA; 2.7.12.1; 3474.
DR Reactome; R-MMU-1538133; G0 and Early G1.
DR BioGRID-ORCS; 13548; 12 hits in 77 CRISPR screens.
DR ChiTaRS; Dyrk1a; mouse.
DR PRO; PR:Q61214; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q61214; protein.
DR Bgee; ENSMUSG00000022897; Expressed in animal zygote and 266 other tissues.
DR ExpressionAtlas; Q61214; baseline and differential.
DR Genevisible; Q61214; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005883; C:neurofilament; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; IPI: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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0034205; P:amyloid-beta formation; ISO:MGI.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:ARUK-UCL.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:ARUK-UCL.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0090312; P:positive regulation of protein deacetylation; IDA:BHF-UCL.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:MGI.
DR CDD; cd14226; PKc_DYRK1; 1.
DR InterPro; IPR028318; DYRK1A/B_MNB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR044131; PKc_DYR1A/1B.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24058:SF121; PTHR24058:SF121; 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; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..763
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase 1A"
FT /id="PRO_0000085932"
FT DOMAIN 159..479
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 33..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 117..134
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 34..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..624
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 165..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 238..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 111
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 140
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 145
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 159
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 177
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 219
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q63470"
FT MOD_RES 310
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 319
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 321
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 402
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 449
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13627"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 763 AA; 85494 MW; E117DDD6C5E8C74F CRC64;
MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AAQMPHSHQY SDRRQPSISD QQVSALPYSD
QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL IKTYKHINEV YYAKKKRRHQ
QGQGDDSSHK KERKVYNDGY DDDNYDYIVK NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV
EQEWVAIKII KNKKAFLNQA QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM
LSYNLYDLLR NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR
SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI LVEMHTGEPL
FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD GTWSLKKTKD GKREYKPPGT
RKLHNILGVE TGGPGGRRAG ESGHTVADYL KFKDLILRML DYDPKTRIQP YYALQHSFFK
KTADEGTNTS NSVSTSPAME QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG
HFAAAVQAMD CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH
HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH SHHSMTSLSS
STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV NLTVYSNPRQ ETGIAGHPTY
QFSANTGPAH YMTEGHLAMR QGADREESPM TGVCVQQSPV ASS
