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Database: UniProt
Entry: A0A3P8ZLK1_ESOLU
LinkDB: A0A3P8ZLK1_ESOLU
Original site: A0A3P8ZLK1_ESOLU 
ID   A0A3P8ZLK1_ESOLU        Unreviewed;       566 AA.
AC   A0A3P8ZLK1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000029232.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000029232.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000029232.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   AlphaFoldDB; A0A3P8ZLK1; -.
DR   STRING; 8010.ENSELUP00000029232; -.
DR   Ensembl; ENSELUT00000011361.2; ENSELUP00000029232.2; ENSELUG00000006111.2.
DR   GeneTree; ENSGT00940000158850; -.
DR   Proteomes; UP000265140; LG04.
DR   Bgee; ENSELUG00000006111; Expressed in head kidney and 10 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01238; PH_Btk; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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; IPR001562; Znf_Btk_motif.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF61; TYROSINE-PROTEIN KINASE ITK_TSK; 1.
DR   Pfam; PF00779; BTK; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00402; TECBTKDOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00107; BTK; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS51113; ZF_BTK; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00432}.
FT   DOMAIN          4..111
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          190..300
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          325..566
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   566 AA;  65475 MW;  6F8ECBDA4C2D9085 CRC64;
     MLSRVILKGT LIKKSQQKRR TSPCNYKERF FVLNTQDLTY SEQRPGKKPV QKGCIELSRI
     KCVEIVCSEL PIPCSNKYPF QVVHDNYYLY IFAPDNDCRL RWVRALKEET KCNDLVPKYH
     PNFWIEGKWK CCYQTEKMAT GCQEYNPIGY GRRLSDAGQR VVIALQDYSP HGDTDLPLHK
     DQEIRKEPLW YETQDIQACI PFQSSPKHQG NYCLFQPCHS PSVTAHLNRV ICIHLWTFLA
     LSMNSMCHTV NPRVKHYQIR ESETSMFYLA EKYLFNTIPE LIQYHQHNAA GLITRLRHPV
     SLDKESSQNH AELSDGQWEV DPLELTLGEE VGSGQFGLVL QGQWRGHRVA VKMVREGAMS
     EEDFKEEARV MTMLSHCKLV QLYGVCTQQS PMCLLFEFME KGCLLDYIKA QKGHLSQDTL
     LGMCLDVSEA MAYLESNNFI HRDLAARNCL VSKNNEVKVS DFGMTRFVLD DQYTSSQGSK
     FPFKWSSPEV IKYSKFSSKS DVWSFGVFMW EVYTEGRLPY ENQTNSEVVD SLNAGLRLLK
     PRLAPEAVYI LMEWCWKEVG WTNLLG
//
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