ID I3M210_ICTTR Unreviewed; 1194 AA.
AC I3M210;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
GN Name=TYK2 {ECO:0000313|Ensembl:ENSSTOP00000002949.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000002949.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000002949.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001149,
CC ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. JAK subfamily. {ECO:0000256|PIRNR:PIRNR000636}.
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DR EMBL; AGTP01088369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01088370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3M210; -.
DR STRING; 43179.ENSSTOP00000002949; -.
DR Ensembl; ENSSTOT00000003298.3; ENSSTOP00000002949.3; ENSSTOG00000003264.3.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000159869; -.
DR HOGENOM; CLU_008155_1_0_1; -.
DR InParanoid; I3M210; -.
DR TreeFam; TF327041; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005131; F:growth hormone receptor binding; IEA:Ensembl.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IEA:Ensembl.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; IEA:Ensembl.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of type II interferon production; IEA:Ensembl.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0060333; P:type II interferon-mediated signaling pathway; IEA:Ensembl.
DR CDD; cd05080; PTKc_Tyk2_rpt2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; 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; IPR016045; Tyr_kinase_non-rcpt_TYK2_N.
DR PANTHER; PTHR45807:SF6; NON-RECEPTOR TYROSINE-PROTEIN KINASE TYK2; 1.
DR PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
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; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW ECO:0000256|PIRSR:PIRSR000636-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000636};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000636}.
FT DOMAIN 40..442
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 599..882
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 904..1183
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 349..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1030
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT BINDING 910..918
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT BINDING 937
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1194 AA; 133978 MW; AB5F307FACF843BC CRC64;
MCCLLSAESA LRSMPLCQKG AAAKGSKPHR DRAQPMADMG GLKVLLHWAG PRGGEPWVTF
SKTSLTAEEV CIHIAHKVGI TPPCFNLFAL FDAQAQVWLP PNHILEVSRD TSLTLYFRMR
FYFRNWHGMN PQEPAVYRCG LPGAETSSEP TEQGVQLLDP ASFEYLFEQG KHEFVNDVVS
LWELSSEEEI HHFKNESLGM AFLHLSHLAL QRGVPLEEVA KEISFKDCIP LSFRQQIRQH
NALTRLRLRN VFRKFLHAFQ PGHLSQQMVM VKYIATLEHL APRFGTERIP VCHLELLSQA
EGEPCYIQDS RRASADHNLE PALGSPTHEV LVTGTGGIQW RPVQVEVSSD VNDSSRNSQT
HLSGKKAKAR EAGGQPANRP REPPWTYFCD FQDITHLVLK GCRVTIYQQD NKCLELRLPS
RAAALSFVAL VDGYFRLTAD SSHYLCQEVA PPRLVMSIQE GIHGPLLEPF VQAKLQPEEG
LYLIHWSTVH LHRLILTVAQ PEPVPGVQSL RIRKFPIEQQ DGAFMLEGWG RSFASVQELR
GALQGCSLRA GDDCFSLRRC CLPQPGEISN LIIMRGSRAS SRPLNLSQLS FHRIHQDEIT
QLSHLGQGTR TNVYEGLLRV GGPEEGKADG GDSPKPGGGC GQQLRVVLKV LDPSHHDIAL
AFYETASLMS QVSHAHLAFV HGVCVRGSEN IMVTEYVENG PLDVWLRREK GHVPMTWKVA
VAQQLASALS YLEDKNLVHG NVCGRNILLA RLGLAEGTSP FIKLSDPGVG LGALSREERV
ERIPWTAPEC LPAGATSLCT AADKWGFGAT LLEICFDGEA PLQGRGPSEK ERFYQKQHRL
PEPSCPELAT ITSQCLTYER ALRPSFRTIL RDLTQLQPHD LVDVSTINPD SPVSDPTVFH
KRYLKKIRDL GEGHFGKVSL YCYDPTNDGT GEMVAVKALK ADCGPQLRSG WRREIDILRT
LYHEHIVKYK GCCEDQGEKS VQLVMEYVPL GSLRDYLPRH NVGLAQLLLF SQQICEGMAY
LHAQHYIHRD LAARNVLLDN DRLVKIGDFG LAKAVPEGHE YYRVREDGDS PVFWYAPECL
KECKFYYASD VWSFGVTLYE LLTYCDSSQS PPSKFLELIG LTQGQITVLR LTELLERGER
LPRPERCPCE IYHLMKNCWE AESSFRPTFQ NLIPILKMVH EKYQGQAPSV FSVC
//
