IRAK2_HUMAN
ID IRAK2_HUMAN Reviewed; 625 AA.
AC O43187; B4DQZ6; Q08AG6; Q5K546;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Interleukin-1 receptor-associated kinase-like 2;
DE Short=IRAK-2;
GN Name=IRAK2;
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], AND VARIANT GLU-431.
RA Rosati O., Martin M.U.;
RT "Identification of Exon 13 and the 3'UTR region of human IRAK-2 and
RT characterisation of the full length gene.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-590, FUNCTION, TISSUE SPECIFICITY,
RP INTERACTION WITH TRAF6; MYD88 AND IL1R1, AND VARIANT GLU-431.
RC TISSUE=Endothelial cell;
RX PubMed=9374458; DOI=10.1126/science.278.5343.1612;
RA Muzio M., Ni J., Feng P., Dixit V.M.;
RT "IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1
RT signaling.";
RL Science 278:1612-1615(1997).
RN [5]
RP FUNCTION.
RX PubMed=10383454; DOI=10.1074/jbc.274.27.19403;
RA Wesche H., Gao X., Li X., Kirschning C.J., Stark G.R., Cao Z.;
RT "IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated
RT kinase (IRAK) family.";
RL J. Biol. Chem. 274:19403-19410(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 2-112.
RX PubMed=20485341; DOI=10.1038/nature09121;
RA Lin S.-C., Lo Y.-C., Wu H.;
RT "Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R
RT signalling.";
RL Nature 465:885-890(2010).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-43; TYR-47; VAL-99; THR-147; GLY-214;
RP LEU-249; VAL-392; THR-421; GLU-431; VAL-439; ASN-469; ILE-503 AND TRP-566.
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).
CC -!- FUNCTION: Binds to the IL-1 type I receptor following IL-1 engagement,
CC triggering intracellular signaling cascades leading to transcriptional
CC up-regulation and mRNA stabilization. {ECO:0000269|PubMed:10383454,
CC ECO:0000269|PubMed:9374458}.
CC -!- SUBUNIT: Interacts with MYD88. IL-1 stimulation leads to the formation
CC of a signaling complex which dissociates from the IL-1 receptor
CC following the binding of PELI1. {ECO:0000269|PubMed:9374458}.
CC -!- INTERACTION:
CC O43187; P10398: ARAF; NbExp=2; IntAct=EBI-447733, EBI-365961;
CC O43187; Q9NWZ3: IRAK4; NbExp=6; IntAct=EBI-447733, EBI-448378;
CC O43187; P46977: STT3A; NbExp=2; IntAct=EBI-447733, EBI-719212;
CC O43187; Q13148: TARDBP; NbExp=2; IntAct=EBI-447733, EBI-372899;
CC O43187; P58753: TIRAP; NbExp=2; IntAct=EBI-447733, EBI-528644;
CC O43187; Q9H0E2: TOLLIP; NbExp=2; IntAct=EBI-447733, EBI-74615;
CC O43187; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-447733, EBI-359276;
CC O43187; Q5D1E8: ZC3H12A; NbExp=2; IntAct=EBI-447733, EBI-747793;
CC O43187; P68467: K7R; Xeno; NbExp=2; IntAct=EBI-447733, EBI-8022707;
CC O43187; Q6PDS3: Sarm1; Xeno; NbExp=2; IntAct=EBI-447733, EBI-6117196;
CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, lung, liver,
CC skeletal muscle, kidney, pancreas and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:9374458}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. Pelle subfamily. {ECO:0000305}.
CC -!- CAUTION: Asn-335 is present instead of the conserved Asp which is
CC expected to be an active site residue. This enzyme has been shown to be
CC catalytically inactive. {ECO:0000305}.
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DR EMBL; AJ496794; CAD43180.3; -; mRNA.
DR EMBL; AK299033; BAG61108.1; -; mRNA.
DR EMBL; BC125184; AAI25185.1; -; mRNA.
DR EMBL; AF026273; AAB87669.1; -; mRNA.
DR CCDS; CCDS33697.1; -.
DR RefSeq; NP_001561.3; NM_001570.3.
DR PDB; 3MOP; X-ray; 3.40 A; K/L/M/N=2-112.
DR PDBsum; 3MOP; -.
DR AlphaFoldDB; O43187; -.
DR SMR; O43187; -.
DR BioGRID; 109865; 51.
DR CORUM; O43187; -.
DR DIP; DIP-31800N; -.
DR ELM; O43187; -.
DR IntAct; O43187; 47.
DR MINT; O43187; -.
DR STRING; 9606.ENSP00000256458; -.
DR BindingDB; O43187; -.
DR ChEMBL; CHEMBL4105759; -.
DR iPTMnet; O43187; -.
DR PhosphoSitePlus; O43187; -.
DR BioMuta; IRAK2; -.
DR CPTAC; CPTAC-1319; -.
DR EPD; O43187; -.
DR jPOST; O43187; -.
DR MassIVE; O43187; -.
DR MaxQB; O43187; -.
DR PaxDb; O43187; -.
DR PeptideAtlas; O43187; -.
DR PRIDE; O43187; -.
DR ProteomicsDB; 48804; -.
DR Antibodypedia; 4605; 717 antibodies from 42 providers.
DR DNASU; 3656; -.
DR Ensembl; ENST00000256458.5; ENSP00000256458.4; ENSG00000134070.5.
DR GeneID; 3656; -.
DR KEGG; hsa:3656; -.
DR MANE-Select; ENST00000256458.5; ENSP00000256458.4; NM_001570.4; NP_001561.3.
DR UCSC; uc003bve.2; human.
DR CTD; 3656; -.
DR DisGeNET; 3656; -.
DR GeneCards; IRAK2; -.
DR HGNC; HGNC:6113; IRAK2.
DR HPA; ENSG00000134070; Tissue enhanced (bone).
DR MIM; 603304; gene.
DR neXtProt; NX_O43187; -.
DR OpenTargets; ENSG00000134070; -.
DR PharmGKB; PA29913; -.
DR VEuPathDB; HostDB:ENSG00000134070; -.
DR eggNOG; KOG1187; Eukaryota.
DR GeneTree; ENSGT00940000159835; -.
DR HOGENOM; CLU_000288_173_0_1; -.
DR InParanoid; O43187; -.
DR OMA; ALSEWDW; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O43187; -.
DR TreeFam; TF328924; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; O43187; -.
DR Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
DR Reactome; R-HSA-975155; MyD88 dependent cascade initiated on endosome.
DR Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-HSA-975871; MyD88 cascade initiated on plasma membrane.
DR SignaLink; O43187; -.
DR BioGRID-ORCS; 3656; 7 hits in 1106 CRISPR screens.
DR ChiTaRS; IRAK2; human.
DR EvolutionaryTrace; O43187; -.
DR GeneWiki; IRAK2; -.
DR GenomeRNAi; 3656; -.
DR Pharos; O43187; Tbio.
DR PRO; PR:O43187; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O43187; protein.
DR Bgee; ENSG00000134070; Expressed in cartilage tissue and 147 other tissues.
DR Genevisible; O43187; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0001959; P:regulation of cytokine-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
DR CDD; cd08795; Death_IRAK2; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR042151; Death_IRAK2.
DR InterPro; IPR033611; IRAK2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR24419:SF2; PTHR24419:SF2; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..625
FT /note="Interleukin-1 receptor-associated kinase-like 2"
FT /id="PRO_0000086032"
FT DOMAIN 13..94
FT /note="Death"
FT DOMAIN 210..489
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 111..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 337..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 43
FT /note="R -> Q (in dbSNP:rs34945585)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041342"
FT VARIANT 47
FT /note="S -> Y (in dbSNP:rs11465864)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030527"
FT VARIANT 99
FT /note="I -> V (in dbSNP:rs55898544)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041343"
FT VARIANT 147
FT /note="R -> T (in dbSNP:rs56053222)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041344"
FT VARIANT 214
FT /note="R -> G (in dbSNP:rs35060588)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041345"
FT VARIANT 249
FT /note="S -> L (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041346"
FT VARIANT 392
FT /note="L -> V (in dbSNP:rs3844283)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030528"
FT VARIANT 421
FT /note="P -> T (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041347"
FT VARIANT 431
FT /note="D -> E (in dbSNP:rs708035)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:9374458, ECO:0000269|Ref.1"
FT /id="VAR_030529"
FT VARIANT 439
FT /note="L -> V (in dbSNP:rs11465927)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030530"
FT VARIANT 469
FT /note="D -> N (in dbSNP:rs56242986)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041348"
FT VARIANT 503
FT /note="L -> I (in dbSNP:rs9854688)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030531"
FT VARIANT 566
FT /note="R -> W (in dbSNP:rs55740652)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041349"
FT VARIANT 574
FT /note="D -> H (in dbSNP:rs11465930)"
FT /id="VAR_030532"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:3MOP"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:3MOP"
FT TURN 17..22
FT /evidence="ECO:0007829|PDB:3MOP"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:3MOP"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:3MOP"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:3MOP"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3MOP"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:3MOP"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3MOP"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:3MOP"
FT TURN 77..81
FT /evidence="ECO:0007829|PDB:3MOP"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3MOP"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:3MOP"
SQ SEQUENCE 625 AA; 69433 MW; 715C954BC9452710 CRC64;
MACYIYQLPS WVLDDLCRNM DALSEWDWME FASYVITDLT QLRKIKSMER VQGVSITREL
LWWWGMRQAT VQQLVDLLCR LELYRAAQII LNWKPAPEIR CPIPAFPDSV KPEKPLAASV
RKAEDEQEEG QPVRMATFPG PGSSPARAHQ PAFLQPPEED APHSLRSDLP TSSDSKDFST
SIPKQEKLLS LAGDSLFWSE ADVVQATDDF NQNRKISQGT FADVYRGHRH GKPFVFKKLR
ETACSSPGSI ERFFQAELQI CLRCCHPNVL PVLGFCAARQ FHSFIYPYMA NGSLQDRLQG
QGGSDPLPWP QRVSICSGLL CAVEYLHGLE IIHSNVKSSN VLLDQNLTPK LAHPMAHLCP
VNKRSKYTMM KTHLLRTSAA YLPEDFIRVG QLTKRVDIFS CGIVLAEVLT GIPAMDNNRS
PVYLKDLLLS DIPSSTASLC SRKTGVENVM AKEICQKYLE KGAGRLPEDC AEALATAACL
CLRRRNTSLQ EVCGSVAAVE ERLRGRETLL PWSGLSEGTG SSSNTPEETD DVDNSSLDAS
SSMSVAPWAG AATPLLPTEN GEGRLRVIVG READSSSEAC VGLEPPQDVT ETSWQIEINE
AKRKLMENIL LYKEEKVDSI ELFGP
