ID   JNK_SUBDO               Reviewed;         361 AA.
AC   Q966Y3; Q8I1N5;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Stress-activated protein kinase JNK;
DE            EC=2.7.11.24;
GN   Name=JNK;
OS   Suberites domuncula (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha; Suberitida;
OC   Suberitidae; Suberites.
OX   NCBI_TaxID=55567 {ECO:0000312|EMBL:CAC38785.1};
RN   [1] {ECO:0000312|EMBL:CAC38785.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Boehm M., Hentschel U., Friedrich A., Steffen R., Pahler S., Gamulin V.,
RA   Mueller I.M., Mueller W.E.G.;
RT   "Molecular response of the sponge Suberites domuncula to bacterial
RT   infection.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12354665; DOI=10.1016/s0378-1119(02)00690-x;
RA   Mueller W.E.G., Boehm M., Grebenjuk V.A., Skorokhod A., Mueller I.M.,
RA   Gamulin V.;
RT   "Conservation of the positions of metazoan introns from sponges to
RT   humans.";
RL   Gene 295:299-309(2002).
CC   -!- FUNCTION: Responds to activation by environmental stress and pro-
CC       inflammatory cytokines by phosphorylating a number of transcription
CC       factors, and thus regulates transcriptional activity.
CC       {ECO:0000250|UniProtKB:P45983}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P45983};
CC   -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC       phosphorylation. {ECO:0000250|UniProtKB:P45983}.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-179 and Tyr-181, which activates the
CC       enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR   EMBL; AJ291511; CAC38785.1; -; mRNA.
DR   EMBL; AJ307673; CAC85496.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q966Y3; -.
DR   SMR; Q966Y3; -.
DR   PRIDE; Q966Y3; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008351; MAPK_JNK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01772; JNKMAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..361
FT                   /note="Stress-activated protein kinase JNK"
FT                   /id="PRO_0000186272"
FT   DOMAIN          22..317
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           179..181
FT                   /note="TXY"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         29..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         179
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         181
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  41566 MW;  5CAA9A360CDAA744 CRC64;
     MSSSDYYSQR VGDTVFTVQK RYTNLTNIGS GAQGVVCSAF DTVTQEKIAI KKLVKPFQNE
     TYAKRAFREL RLMKMVDHKN IIGLKNLFTP AKSLDDFQDV YIVMELMDAN LCRVIGIELD
     HDRMSYLLYQ LLCGIKHLHS AGIIHRDLKP SNIVVKEDCS LKILDFGLAR TADQTFNMTP
     YVVTRYYRAP EVIVGMKYKE NVDIWSVGCI FAEMIRGDIL LPGKDYIDQW NKVTQVLGTP
     PSVFFKQLSS SVRLYCESQP RYAGKSWKDL FPDDVFPNDT PEDKAKTRHG RDLLSKMLQI
     DPQNRITVEQ ALAHPYVSIW YDPAEVHAPP PKRYDHALDE QSIPLDQWKT RIYEEVKTYN
     S