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Database: UniProt
Entry: F1S3L9_PIG
LinkDB: F1S3L9_PIG
Original site: F1S3L9_PIG 
ID   F1S3L9_PIG              Unreviewed;      1184 AA.
AC   F1S3L9; A0A287ASU9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 95.
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:ENSSSCP00000046973.3,
GN   ECO:0000313|VGNC:VGNC:94615};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:HCZ87389.1};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000046973.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000046973.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HCZ87389.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000046973.3}
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; DQIR01031914; HCZ87389.1; -; Transcribed_RNA.
DR   EMBL; DQIR01105306; HDA60782.1; -; Transcribed_RNA.
DR   Ensembl; ENSSSCT00000065505.3; ENSSSCP00000046973.3; ENSSSCG00000013648.5.
DR   VGNC; VGNC:94615; TYK2.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000159869; -.
DR   HOGENOM; CLU_008155_1_0_1; -.
DR   OMA; QAKHEFV; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000008227; Chromosome 2.
DR   Bgee; ENSSSCG00000013648; Expressed in blood and 43 other cell types or tissues.
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   Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW   2}; Immunity {ECO:0000256|ARBA:ARBA00023130};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW   ECO:0000256|PIRSR:PIRSR000636-2}; Receptor {ECO:0000313|EMBL:HCZ87389.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
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          27..430
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          587..866
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          894..1166
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1020
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT   BINDING         900..908
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         927
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1184 AA;  132336 MW;  AF07FB056471BBE7 CRC64;
     MPLCHWGATT RGRKPDGDGA QPTATTEGLK VLLHWAGPGG GEPWVTFSEV TLTAEEVCIH
     IAHRVGISPL CLNLFALFDA QAQVWLPPNH ILDISGDSSL TLHFRMRFYF RNWHGMNPQE
     PAVYRCGPPG TETSEQAEPG VQLLDPASFE YLFEQGKHEF VNDVASLWEL SSEEEIHHFQ
     NESLGMAFLH LCQLALRHGV PLEKVAKKIS FKDCIPRSFR RQIRQHNALT RLRLRSIFRK
     FLRAFQPGCL SQQVVMVKYL ATLERLAPRF GTERVPVCRL QLLAQAEGEP CYIRDGGQSS
     PDPEPQAAPE PTTHEVLVSG TDGIQWRLVQ AEGPSGGAGD GSSSRIPHTG HSGKKAKAQE
     RGNQPVDRPG EALWTYFCNF QDITHVVLKE RHVSIHCQDK CLELTLPSRA TALSLVALVD
     GYFRLTADSS HYLCHEVAPP RLVMSIQDGI HGPLLEPFVL AKLRPEDGLY LIHWSTSHLN
     RLILTVAQRD QAPGTKGLRL RKFPIELQAE TVTLEGWGRS FPSVRELRAA LQGCSLRAGD
     DCFSLDRCCL PRPGEISNLI ITRGPQACTR PLNLSHLSFH RVHQEDITQL SHLGQGTRTN
     VYEGLLRVGG GGPEEEKSDG RDPSPSSGDR GQELRVVLKV LDPSHHDIAL AFYETASLMS
     QVSHVHLVFV HGVYVHGSEN IMVTEYVEHG PLDVWLRRER GHVPLAWKLA VAQQLASALS
     YLEDKSLVHG NVCGRNILLA RLGQAEGTSP FIKLSDPGVG LNALSREERV ERIPWTAPEC
     LSGGANSLST AADKWGFGAT LLEICFDGEA PLQGRGPSEK ERFYQKQHKL PEPSCPELAT
     LTSQCLTYEP AQRPSFRTIL RDLTQLQPQN LADVLSVNPD LPTSDPTIFH KRYLKKIRDL
     GEGHFGKVSL YCYDPTNDGT GEMVAVKALK AGCGSQLRTG WRREIDILRT LYHEHIVKYK
     GCCEDQGEKS VQLVMEYVPL GSLRDYLPRQ NVGLAQLLLF AQQICEGMAY LHAQHYVHRD
     LAARNVLLDN NRLVKIGDFG LAKAVPEGHD YYCVREDGDS PVFWYAPECL KECKFYYASD
     VWSFGVTMYE LLTYCDSSQS PPSKFIELIG LTQGQMTVLR LTELLEQGER LPQPEKCPHE
     IYRLMKNCWE AKASFRPTFQ NLVPILKTIQ EKYQGQAPSV FSVC
//
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