JAK2_PIG
ID JAK2_PIG Reviewed; 1131 AA.
AC O19064;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Tyrosine-protein kinase JAK2 {ECO:0000250|UniProtKB:O60674};
DE EC=2.7.10.2 {ECO:0000250|UniProtKB:O60674};
DE AltName: Full=Janus kinase 2;
DE Short=JAK-2;
GN Name=JAK2 {ECO:0000250|UniProtKB:O60674};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Ito Y., Mikawa S., Kobayashi E., Wada Y., Minezawa M.;
RT "Domestic pig mRNA for JAK2, complete cds.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-receptor tyrosine kinase involved in various processes
CC such as cell growth, development, differentiation or histone
CC modifications. Mediates essential signaling events in both innate and
CC adaptive immunity. In the cytoplasm, plays a pivotal role in signal
CC transduction via its association with type I receptors such as growth
CC hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR),
CC thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-
CC beta, IFN-gamma and multiple interleukins. Following ligand-binding to
CC cell surface receptors, phosphorylates specific tyrosine residues on
CC the cytoplasmic tails of the receptor, creating docking sites for STATs
CC proteins. Subsequently, phosphorylates the STATs proteins once they are
CC recruited to the receptor. Phosphorylated STATs then form homodimer or
CC heterodimers and translocate to the nucleus to activate gene
CC transcription. For example, cell stimulation with erythropoietin (EPO)
CC during erythropoiesis leads to JAK2 autophosphorylation, activation,
CC and its association with erythropoietin receptor (EPOR) that becomes
CC phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or
CC STAT5B) is recruited, phosphorylated and activated by JAK2. Once
CC activated, dimerized STAT5 translocates into the nucleus and promotes
CC the transcription of several essential genes involved in the modulation
CC of erythropoiesis. Part of a signaling cascade that is activated by
CC increased cellular retinol and that leads to the activation of STAT5
CC (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced
CC ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating
CC CDKN1B. Cooperates with TEC through reciprocal phosphorylation to
CC mediate cytokine-driven activation of FOS transcription. In the
CC nucleus, plays a key role in chromatin by specifically mediating
CC phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag
CC that promotes exclusion of CBX5 (HP1 alpha) from chromatin.
CC {ECO:0000250|UniProtKB:O60674}.
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=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely
CC to be the in vivo cofactor. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Regulated by autophosphorylation, can both
CC activate or decrease activity. Heme regulates its activity by enhancing
CC the phosphorylation on Tyr-1007 and Tyr-1008.
CC {ECO:0000250|UniProtKB:O60674, ECO:0000250|UniProtKB:Q62120}.
CC -!- SUBUNIT: Interacts with IL23R, SKB1 and STAM2 (By similarity).
CC Interacts with EPOR. Interacts with LYN. Interacts with SIRPA.
CC Interacts with SH2B1. Interacts with TEC (By similarity). Interacts
CC with IFNGR2 (via intracellular domain) (By similarity). Interacts with
CC LEPR (Isoform B) (By similarity). Interacts with HSP90AB1; promotes
CC functional activation in a heat shock-dependent manner. Interacts with
CC STRA6 (By similarity). Interacts with ASB2; the interaction targets
CC JAK2 for Notch-induced proteasomal degradation (By similarity).
CC {ECO:0000250|UniProtKB:O60674, ECO:0000250|UniProtKB:Q62120}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain of JAKs mediates their interaction with
CC cytokine/interferon/growth hormone receptors. Possesses 2 protein
CC kinase domains. The second one probably contains the catalytic domain,
CC while the presence of slight differences suggest a different role for
CC protein kinase 1 (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated, leading to regulate its activity. Leptin
CC promotes phosphorylation on tyrosine residues, including
CC phosphorylation on Tyr-813. Autophosphorylation on Tyr-119 in response
CC to EPO down-regulates its kinase activity. Autophosphorylation on Tyr-
CC 868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are
CC required for maximal kinase activity. Also phosphorylated by TEC (By
CC similarity). Phosphorylated on tyrosine residues in response to
CC interferon gamma signaling. Phosphorylated on tyrosine residues in
CC response to a signaling cascade that is activated by increased cellular
CC retinol (By similarity). {ECO:0000250|UniProtKB:O60674,
CC ECO:0000250|UniProtKB:Q62120}.
CC -!- PTM: Undergoes Notch-induced ubiquitination and subsequent proteasomal
CC degradation which is mediated by ASB1 or ASB2, the substrate-
CC recognition components of probable ECS E3 ubiquitin-protein ligase
CC complexes. {ECO:0000250|UniProtKB:O60674}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. JAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB006011; BAA21662.1; -; mRNA.
DR RefSeq; NP_999278.1; NM_214113.1.
DR AlphaFoldDB; O19064; -.
DR SMR; O19064; -.
DR STRING; 9823.ENSSSCP00000005606; -.
DR PaxDb; O19064; -.
DR PRIDE; O19064; -.
DR Ensembl; ENSSSCT00000034678; ENSSSCP00000029236; ENSSSCG00000005215.
DR Ensembl; ENSSSCT00000086181; ENSSSCP00000061060; ENSSSCG00000005215.
DR Ensembl; ENSSSCT00005047950; ENSSSCP00005029500; ENSSSCG00005029324.
DR Ensembl; ENSSSCT00005047985; ENSSSCP00005029524; ENSSSCG00005029324.
DR Ensembl; ENSSSCT00005047994; ENSSSCP00005029532; ENSSSCG00005029324.
DR Ensembl; ENSSSCT00015085604; ENSSSCP00015034788; ENSSSCG00015063581.
DR Ensembl; ENSSSCT00025050590; ENSSSCP00025021588; ENSSSCG00025037142.
DR Ensembl; ENSSSCT00030072992; ENSSSCP00030033312; ENSSSCG00030052311.
DR Ensembl; ENSSSCT00035024766; ENSSSCP00035009315; ENSSSCG00035019132.
DR Ensembl; ENSSSCT00045055979; ENSSSCP00045039034; ENSSSCG00045032577.
DR Ensembl; ENSSSCT00055036075; ENSSSCP00055028647; ENSSSCG00055018283.
DR Ensembl; ENSSSCT00060087675; ENSSSCP00060037966; ENSSSCG00060064055.
DR Ensembl; ENSSSCT00065098044; ENSSSCP00065042985; ENSSSCG00065071184.
DR Ensembl; ENSSSCT00070059083; ENSSSCP00070050290; ENSSSCG00070029405.
DR Ensembl; ENSSSCT00070059086; ENSSSCP00070050293; ENSSSCG00070029405.
DR GeneID; 397201; -.
DR KEGG; ssc:397201; -.
DR CTD; 3717; -.
DR VGNC; VGNC:89271; JAK2.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000155640; -.
DR InParanoid; O19064; -.
DR OMA; ICAVACK; -.
DR OrthoDB; 58906at2759; -.
DR ChiTaRS; JAK2; pig.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000005215; Expressed in stomach and 44 other tissues.
DR ExpressionAtlas; O19064; baseline and differential.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0030526; C:granulocyte macrophage colony-stimulating factor receptor complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005126; F:cytokine receptor binding; IBA:GO_Central.
DR GO; GO:0005131; F:growth hormone receptor binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0035401; F:histone kinase activity (H3-Y41 specific); ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005143; F:interleukin-12 receptor binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0042976; P:activation of Janus kinase activity; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0036016; P:cellular response to interleukin-3; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0038065; P:collagen-activated signaling pathway; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0038157; P:granulocyte-macrophage colony-stimulating factor signaling pathway; IEA:Ensembl.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0061180; P:mammary gland epithelium development; IEA:Ensembl.
DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0060399; P:positive regulation of growth hormone receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEA:Ensembl.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IEA:Ensembl.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; IEA:Ensembl.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0010572; P:positive regulation of platelet activation; IEA:Ensembl.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; IEA:Ensembl.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; IEA:Ensembl.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0034050; P:programmed cell death induced by symbiont; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IBA:GO_Central.
DR CDD; cd13333; FERM_C_JAK2; 1.
DR CDD; cd05078; PTK_Jak2_rpt1; 1.
DR CDD; cd14205; PTKc_Jak2_rpt2; 1.
DR CDD; cd10379; SH2_Jak2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR041155; FERM_F1.
DR InterPro; IPR041046; FERM_F2.
DR InterPro; IPR041381; JAK1-3/TYK2_PHL_dom.
DR InterPro; IPR037838; JAK2_FERM_C-lobe.
DR InterPro; IPR035860; JAK2_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035588; PTK_Jak2_rpt1.
DR InterPro; IPR035589; PTKc_Jak2_rpt2.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
DR InterPro; IPR020693; Tyr_kinase_non-rcpt_Jak2.
DR Pfam; PF18379; FERM_F1; 1.
DR Pfam; PF18377; FERM_F2; 1.
DR Pfam; PF17887; Jak1_Phl; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF000636; TyrPK_Jak; 1.
DR PRINTS; PR01823; JANUSKINASE.
DR PRINTS; PR01825; JANUSKINASE2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; ATP-binding; Chromatin regulator; Cytoplasm; Immunity;
KW Innate immunity; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW SH2 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
FT CHAIN 1..1131
FT /note="Tyrosine-protein kinase JAK2"
FT /id="PRO_0000324093"
FT DOMAIN 37..380
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 401..482
FT /note="SH2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 545..809
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 849..1126
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..239
FT /note="Interaction with cytokine/interferon/growth hormone
FT receptors"
FT /evidence="ECO:0000250"
FT ACT_SITE 976
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 855..863
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 882
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 119
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q62120"
FT MOD_RES 372
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62120"
FT MOD_RES 373
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62120"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62120"
FT MOD_RES 570
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60674"
FT MOD_RES 813
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62120"
FT MOD_RES 868
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q62120"
FT MOD_RES 966
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q62120"
FT MOD_RES 972
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q62120"
FT MOD_RES 1007
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O60674"
FT MOD_RES 1008
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O60674"
SQ SEQUENCE 1131 AA; 130759 MW; 6339C7417087EB2C CRC64;
MGMACLTMTE MEGTSTSPVH QNGDIPGNAN SVKQIDPVLQ VYLYHSLGKA EGDYLKFPAG
EYVAEEICVA ASKACGITPV YHSMFALMNE TERIWYPPNH VFHVDESTRH NVLYRIRFYF
PYWYCNGSNR TYRHGISRGA EAPLLDDFVM SYLFAQWRHD FLYGWVKIPV THETQEECLG
MAVLDMMRIA KEKDQTPLDI YSSVSYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIEQF
SHCKATARNL KLKYLINLET LQSAFYTEQF EVKEPGRGPS GEEIFATIII TGNGGIQWSR
GKHKESETLT EQDLQLYCDF PDIIDVSIKQ ANQEGSNESR IVTIHKQDGK SLEIELSSLR
EALSFVSLID GYYRLTADAH HYLCKEVAPP MVLENIQSNC HGPISMDFAI SKLKKAGNQT
GLFVLRCSPK DFNKYFLTFA VERENVTEYK HCLITKNENG EYNLSGTRKN FSNLKDLLNC
YQMETVRSDS IIFQFTKCCP PKPKDKSNLL VFRTNGISDV PTSPTLQRHN NVNQMVFHKI
RNEDLIFNES LGQGTFTKIF KGVRREVGDY GQLHETEVLL KVLDKAHRNY SESFFEAASM
MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK LEVAKQLAWA
MHFLEEKTLI HGNVCAKNIL LIREEDRKTG NPPFIKLSDP GISITVLPKD ILQERIPWVP
PECIENPKNL NLATDKWSFG TTLWEICSGG DKPLNALDSQ RKLQFYEDRH QLPAPKWTEL
ANLINNCMDY EPDFRPSFRA IIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD
PTQFEERHLK FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE
ILKSLQHDNI VKYKGVCYSA GRRNLRLIME YLPYGSLRDY LQKHKERIDH KKLLQYTSQI
CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV LPQDKEYYKV KEPGESPIFW
YAPESLTESK FSVASDVWSF GVVLYELFTY IEKSKSPPAE FMRMIGNDKQ GQMIVFHLIE
LLKNNGRLPR PDGCPDEIYI IMTECWNNNV NQRPSFRDLA LRVDQIRDSM A
