TYK2_MOUSE
ID TYK2_MOUSE Reviewed; 1184 AA.
AC Q9R117; O88431; Q3TXE3; Q52KQ2; Q8VE41;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Non-receptor tyrosine-protein kinase TYK2;
DE EC=2.7.10.2;
GN Name=Tyk2 {ECO:0000312|EMBL:AAD49423.1};
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].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=11070173; DOI=10.1016/s1074-7613(00)00054-6;
RA Karaghiosoff M., Neubauer H., Lassnig C., Kovarik P., Schindler H.,
RA Pircher H., McCoy B., Bogdan C., Decker T., Brem G., Pfeffer K.,
RA Mueller M.;
RT "Partial impairment of cytokine responses in Tyk2-deficient mice.";
RL Immunity 13:549-560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE34973.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 PROTEIN SEQUENCE OF 736-741, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11070174; DOI=10.1016/s1074-7613(00)00055-8;
RA Shimoda K., Kato K., Aoki K., Matsuda T., Miyamoto A., Shibamori M.,
RA Yamashita M., Numata A., Takase K., Kobayashi S., Shibata S., Asano Y.,
RA Gondo H., Sekiguchi K., Nakayama K., Nakayama T., Okamura T., Okamura S.,
RA Niho Y., Nakayama K.;
RT "Tyk2 plays a restricted role in IFN alpha signaling, although it is
RT required for IL-12-mediated T cell function.";
RL Immunity 13:561-571(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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 [10]
RP FUNCTION IN STAT6 ACTIVATION.
RX PubMed=22859374; DOI=10.1096/fj.12-211755;
RA Zhang X., Zhang Y., Tao B., Wang D., Cheng H., Wang K., Zhou R., Xie Q.,
RA Ke Y.;
RT "Docking protein Gab2 regulates mucin expression and goblet cell
RT hyperplasia through TYK2/STAT6 pathway.";
RL FASEB J. 26:4603-4613(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 884-1174 IN COMPLEX WITH
RP INHIBITOR.
RX PubMed=22995073; DOI=10.1186/1472-6807-12-22;
RA Argiriadi M.A., Goedken E.R., Banach D., Borhani D.W., Burchat A.,
RA Dixon R.W., Marcotte D., Overmeyer G., Pivorunas V., Sadhukhan R.,
RA Sousa S., Moore N.S., Tomlinson M., Voss J., Wang L., Wishart N.,
RA Woller K., Talanian R.V.;
RT "Enabling structure-based drug design of Tyk2 through co-crystallization
RT with a stabilizing aminoindazole inhibitor.";
RL BMC Struct. Biol. 12:22-22(2012).
CC -!- FUNCTION: Non-receptor kinase involved in various processes including
CC cell growth, development, cell migration, innate and adaptive immunity
CC (PubMed:11070174). Plays both structural and catalytic roles in
CC numerous cytokines and interferons signaling. Associates with cytokine
CC and growth factor receptors and activate STAT family members including
CC STAT1, STAT3, STAT4 or STAT6 (PubMed:22859374). The heterodimeric
CC cytokine receptor complexes are composed of a TYK2-associated receptor
CC chain (IFNAR1, IL12RB1, IL10RB or IL13RA1) which serves as the signal
CC transducing chain harboring STAT docking sites once phosphorylated by
CC TYK2, and a second receptor chain associated either with JAK1 or JAK2.
CC In turn, recruited STATs are phosphorylated, form homo- and
CC heterodimers, translocate to the nucleus, and regulate cytokine/growth
CC factor responsive genes. Negatively regulates STAT3 activity by
CC promototing phosphorylation at a specific tyrosine that differs from
CC the site used for signaling (By similarity).
CC {ECO:0000250|UniProtKB:P29597, ECO:0000269|PubMed:11070174,
CC ECO:0000269|PubMed:22859374}.
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:0000250|UniProtKB:P29597};
CC -!- ACTIVITY REGULATION: The protein kinase 1 domain (also termed
CC pseudokinase domain) mediates autoinhibition of the TYK2 kinase domain.
CC {ECO:0000250|UniProtKB:P29597}.
CC -!- SUBUNIT: Interacts with JAKMIP1. Interacts with PIK3R1; this
CC interaction is important for cell migration.
CC {ECO:0000250|UniProtKB:P29597}.
CC -!- DOMAIN: The FERM domain mediates interaction with JAKMIP1.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are viable and fertile but display
CC multiple immunological defects, most prominently high sensitivity to
CC infections and defective tumor surveillance. Absence of TYK2 results in
CC increased resistance against allergic, autoimmune and inflammatory
CC disease. {ECO:0000269|PubMed:11070174}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. JAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD49423.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH94240.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDL25160.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF173032; AAD49423.1; ALT_INIT; mRNA.
DR EMBL; AF052607; AAC34580.2; -; Genomic_DNA.
DR EMBL; AK159303; BAE34973.1; -; mRNA.
DR EMBL; AC163637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466522; EDL25160.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC094240; AAH94240.1; ALT_INIT; mRNA.
DR EMBL; BC019789; AAH19789.1; -; mRNA.
DR CCDS; CCDS90510.1; -.
DR RefSeq; NP_061263.2; NM_018793.2.
DR RefSeq; XP_011240881.1; XM_011242579.2.
DR PDB; 4E1Z; X-ray; 2.50 A; A=884-1174.
DR PDB; 4E20; X-ray; 2.60 A; A=885-1174.
DR PDBsum; 4E1Z; -.
DR PDBsum; 4E20; -.
DR AlphaFoldDB; Q9R117; -.
DR SMR; Q9R117; -.
DR ComplexPortal; CPX-388; Interleukin-12-receptor complex.
DR ComplexPortal; CPX-389; Interleukin-23-receptor complex.
DR STRING; 10090.ENSMUSP00000001036; -.
DR BindingDB; Q9R117; -.
DR ChEMBL; CHEMBL2321619; -.
DR iPTMnet; Q9R117; -.
DR PhosphoSitePlus; Q9R117; -.
DR SwissPalm; Q9R117; -.
DR EPD; Q9R117; -.
DR PaxDb; Q9R117; -.
DR PRIDE; Q9R117; -.
DR ProteomicsDB; 298077; -.
DR Antibodypedia; 716; 728 antibodies from 41 providers.
DR DNASU; 54721; -.
DR Ensembl; ENSMUST00000214454; ENSMUSP00000150214; ENSMUSG00000032175.
DR GeneID; 54721; -.
DR KEGG; mmu:54721; -.
DR UCSC; uc009oke.1; mouse.
DR CTD; 7297; -.
DR MGI; MGI:1929470; Tyk2.
DR VEuPathDB; HostDB:ENSMUSG00000032175; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000159869; -.
DR InParanoid; Q9R117; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-1059683; Interleukin-6 signaling.
DR Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
DR Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
DR Reactome; R-MMU-6783783; Interleukin-10 signaling.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR Reactome; R-MMU-9020591; Interleukin-12 signaling.
DR Reactome; R-MMU-9020933; Interleukin-23 signaling.
DR Reactome; R-MMU-9020956; Interleukin-27 signaling.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR Reactome; R-MMU-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-MMU-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR BioGRID-ORCS; 54721; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Tyk2; mouse.
DR PRO; PR:Q9R117; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9R117; protein.
DR Bgee; ENSMUSG00000032175; Expressed in granulocyte and 232 other tissues.
DR ExpressionAtlas; Q9R117; baseline and differential.
DR Genevisible; Q3TXE3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042022; C:interleukin-12 receptor complex; IC:ComplexPortal.
DR GO; GO:0072536; C:interleukin-23 receptor complex; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
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; ISO:MGI.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IC:ComplexPortal.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IC:ComplexPortal.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:MGI.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; ISO:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:ComplexPortal.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; IC:ComplexPortal.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
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; IPR016045; Tyr_kinase_non-rcpt_TYK2_N.
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 PIRSF; PIRSF000636; TyrPK_Jak; 1.
DR PRINTS; PR01823; JANUSKINASE.
DR PRINTS; PR00109; TYRKINASE.
DR PRINTS; PR01827; YKINASETYK2.
DR SMART; SM00295; B41; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; SH2 domain;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..1184
FT /note="Non-receptor tyrosine-protein kinase TYK2"
FT /id="PRO_0000088178"
FT DOMAIN 33..430
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 449..529
FT /note="SH2; atypical"
FT DOMAIN 589..866
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 894..1166
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 294..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1020
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 900..908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 927
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 295
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29597"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 604
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29597"
FT MOD_RES 1051
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P29597"
FT MOD_RES 1052
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29597"
FT CONFLICT 195
FT /note="C -> F (in Ref. 1; AAC34580)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="H -> R (in Ref. 1; AAC34580)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="K -> E (in Ref. 1; AAC34580)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="S -> C (in Ref. 1; AAC34580)"
FT CONFLICT 1103
FT /note="M -> T (in Ref. 1; AAC34580)"
FT HELIX 891..893
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 894..902
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 904..913
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 917..919
FT /evidence="ECO:0007829|PDB:4E20"
FT STRAND 922..929
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 935..950
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 959..964
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 971..976
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 983..986
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 987..989
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 994..1013
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1023..1025
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 1026..1028
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1030..1032
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 1034..1036
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 1050..1053
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 1058..1060
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1062..1064
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1067..1071
FT /evidence="ECO:0007829|PDB:4E1Z"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1077..1092
FT /evidence="ECO:0007829|PDB:4E1Z"
FT TURN 1093..1095
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1097..1099
FT /evidence="ECO:0007829|PDB:4E20"
FT HELIX 1101..1109
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1114..1127
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1139..1148
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1153..1155
FT /evidence="ECO:0007829|PDB:4E1Z"
FT HELIX 1159..1172
FT /evidence="ECO:0007829|PDB:4E1Z"
SQ SEQUENCE 1184 AA; 133315 MW; 2B42052073463AC8 CRC64;
MVGTMPLCGR RAILEDSKAD GTEAQPLVPT GCLMVLLHWP GPEGGEPWVT FSQTSLTAEE
VCIHIAHKVG ITPPCLNLFA LYNAQAKVWL PPNHILDTSQ DMNLYFRMRF YFRNWHGMNP
QEPAVYRCGF PGAETSSDRA EQGVQLLDSA SFEYLFEQGK HEFMNDVVSL RDLSSEEEIH
HFKNESLGMA FLHLCHLALS RGVPLEEMAR EISFKNCIPH SFRQHIRQHN VLTRLRLHRV
FRRFLRAFRP GHLSQQVVMV KYLATLERLA PRFGSERIPV CHLEVLAQPE RDPCYIQNSG
QTAGDPGPEL PSGPPTHEVL VTGTGGIQWH PLQTQESERG NSRGNPHGSR SGKKPKAPKA
GEHLTESPQE PPWTYFCDFQ DISHVVLKER RVHIHLQDNK CLLLCLCSQA EALSFVALVD
GYFRLTADSS HYLCHEVAPP RLVTSIQNGI HGPLMDPFVQ AKLWPEDGLY LIQWSTSHLH
RLILTVAHRN PAFSNGPRGL RLRKFPITQQ PGAFVLDGWG RSFASLGDLR LALQGCSLRA
GDDCFPLHHC CLPRPREISN LVIMRGSRAH TRPLNLSQLS FHRVHQDEIT QLSHLGQGTR
TNVYEGLLRV GGPDEGKVDN GCPPEPGGTS GQQLRVVLKV LDPSHHDIAL AFYETASLMS
QVSHMHLAFL HGVCVRGSEN IIVTEFVEHG PLDVWLRRQR GQVPMTWKMV VAQQLASALS
YLEDKNLVHG NVCGRNILLA RLGLEEGTNP FIKLSDPGVG QGALSREERV ERIPWTAPEC
LSGGTSSLGT ATDMWGFGAT LLEICFDGEA PLQGRGPSEK ERFYTKKHQL PEPSSPELAT
LTRQCLTYEP AQRPSFRTIL RDLTRLQPQN LVGTSAVNSD SPASDPTVFH KRYLKKIRDL
GEGHFGKVSL YCYDPTNDGT GEMVAVKALK EGCGPQLRSG WQREIEILRT LYHEHIVKYK
GCCEDQGEKS VQLVMEYVPL GSLRDYLPRH CVGLAQLLLF AQQICEGMAY LHAQHYIHRD
LAARNVLLDN DRLVKIGDFG LAKAVPEGHE YYRVREDGDS PVFWYAPECL KECKFYYASD
VWSFGVTLYE LLTYCDSNQS PHMKFTELIG HTQGQMTVLR LTELLERGER LPRPDRCPCE
IYHLMKNCWE TEASFRPTFQ NLVPILQTAQ EKYQGQVPSV FSVC
