ID C7ATY7_SINCH Unreviewed; 1120 AA.
AC C7ATY7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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};
OS Siniperca chuatsi (Mandarin fish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Centrarchiformes; Centrarchoidei; Sinipercidae; Siniperca.
OX NCBI_TaxID=119488 {ECO:0000313|EMBL:ACU12481.1};
RN [1] {ECO:0000313|EMBL:ACU12481.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19539032; DOI=10.1016/j.fsi.2009.06.001;
RA Guo C.J., Zhang Y.F., Yang L.S., Yang X.B., Wu Y.Y., Liu D., Chen W.J.,
RA Weng S.P., Yu X.Q., He J.G.;
RT "The JAK and STAT family members of the mandarin fish Siniperca chuatsi:
RT molecular cloning, tissues distribution and immunobiological activity.";
RL Fish Shellfish Immunol. 27:349-359(2009).
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 -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004184}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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; FJ629182; ACU12481.1; -; mRNA.
DR AlphaFoldDB; C7ATY7; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13333; FERM_C_JAK2; 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; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
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; 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; 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 PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
DR PANTHER; PTHR45807:SF1; TYROSINE-PROTEIN KINASE JAK2; 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 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; 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.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW 2}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW ECO:0000256|PIRSR:PIRSR000636-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
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 35..369
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 388..473
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 533..797
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 837..1114
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 964
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT BINDING 843..851
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT BINDING 870
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT BINDING 871
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1120 AA; 128592 MW; E16E14722DF61DF8 CRC64;
MASLPAMDTV TDAYPTVHQN GTAHRESPDT RPAAAVLRLH FYHSSQGAAD CSFLSYPPGE
YVAEELCIDA AKACNISPLY CSLFGLFRER DSMWFAPNHI FQLDELASED VFFKIRYYFP
GWYSGGASRA YRYGVAKGSE SPVVDDFVMS YLFSQWRNDF VNGLVKIPNS HETQEECLGM
AVLDMTRTAK ERQMSPLDIY HTISYKSFLP KDVRAQIQDC NFLTRKRIRF RFKRFIQQFS
QCRTTARDLK LKYLISMESL EKAFYTETFQ VREPSSGQLI ILVVADSGIQ WCREKLKDTD
QELQNLCDFP DVTDISIKHA SKEDAAESRV VTINKQDGKN LELEFPSLSE ALSFVSLIDG
YYRLTTDAHH YLCKEVAPPR LVEAIAPHCH GPISMEFAIN RLQKCGNKRG LYILRCSPKD
FNKYFLTFPV EVYDAVEYKH CQITRSANGE FNLSGTKRNF SSLQELLSCY QKETVRSDSV
IFQFSKCCPP KSKEKSCLLM CRSNKGSEVP LSPSLHRHNI SQMVFHKIRK EDLEFMESLG
QGTFTKIFKG VRKELGDYGV VHQTEVVMKV LDQAYRNYSE SFFEAASMMS QLSHKHLILN
YGVCVCGEEN IMVQEYVKFG SLDTYLKKNK NSINILWKLE VAKQLAWAMN FLEEKHLIHG
NVCAKNVLLI REDDRRAGNP PFIKLSDPGI SITVLPKEIL IERIPWVPPE CIEDPAHLTL
AADKWSFGTT LWEICSGGEK PLATLDNSKK TLFYEDHHQL PAPKWTELAN LITSCMDYEP
TFRPTFRAVV RDLHSLFTPD YELIVDSDIL PNKTVGSAWS TGGFESQEPA QFEERHLIFL
QQLGKGNFGS VEMCRYDPLQ DNTGEVVAVK KLQHSTAEHI RDFEREIEIL KSLQHENIVK
YKGVCYSAGR RNLRLIMEYL PFGSLRDYLM KNRERIDHKK LVHYTSQICK GMEYLSSKRY
IHRDLATRNI LVESELRVKI GDFGLTKVLP QDKEYYMVKE PGESPIFWYA LESLTESKFS
VASDVWSFGV VLYELFTHSD KNSSPPAVFM SMMGNDKQGQ LIVYHLIELL KSGSRLPQPL
GCPTEIHEIM EECWDNDPGL RPSFKELALR IDLFRDSKEF
//
