ID G3VGH9_SARHA Unreviewed; 467 AA.
AC G3VGH9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Stress-activated protein kinase JNK {ECO:0000256|RuleBase:RU368052};
DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU368052};
GN Name=MAPK10 {ECO:0000313|Ensembl:ENSSHAP00000002283.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000002283.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000002283.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000002283.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU368052}.
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 Evidence={ECO:0000256|ARBA:ARBA00000494};
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; Evidence={ECO:0000256|ARBA:ARBA00000088};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU368052};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368052}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily.
CC {ECO:0000256|RuleBase:RU368052}.
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DR AlphaFoldDB; G3VGH9; -.
DR Ensembl; ENSSHAT00000002307.2; ENSSHAP00000002283.2; ENSSHAG00000002029.2.
DR GeneTree; ENSGT00940000153692; -.
DR InParanoid; G3VGH9; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd07850; STKc_JNK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR PANTHER; PTHR24055:SF162; MITOGEN-ACTIVATED PROTEIN KINASE 10; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01772; JNKMAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU368052};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Kinase {ECO:0000256|RuleBase:RU368052};
KW Magnesium {ECO:0000256|RuleBase:RU368052};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU368052};
KW Phosphoprotein {ECO:0000256|RuleBase:RU368052};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU368052};
KW Transferase {ECO:0000256|RuleBase:RU368052}.
FT DOMAIN 67..362
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 408..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 53046 MW; B6B952EAAE073EBD CRC64;
MVFMSRYFLS YFGEPTFDVK IAFCQGFDKQ VDVSYIAKYY NMSKSKVDNQ FYSVEVGDST
FTVLKRYQNL KPIGSGAQGI VCAAYDAVLD RNVAIKKLSR PFQNQTHAKR AYRELVLMKC
VNHKNIISLL NVFTPQKSLE EFQDVYLVME LMDANLCQVI QMELDHERMS YLLYQMLCGI
KHLHSAGIIH RDLKPSNIVV KSDCTLKILD FGLARTAGTS FMMTPYVVTR YYRAPEVILG
MGYKENVDIW SVGCIMGEMV RHKILFPGRD YIDQWNKVIE QLGTPCPEFM KKLQPTVRNY
VENRPKYAGL TFPKLFPDSL FPADSEHNKL KASQARDLLS KMLVIDPAKR ISVDDALQHP
YINVWYDPAE VEAPPPQIYD KQLDEREHTI EEWKELIYKE VMNSEEKTKN GVVKGQPSPS
GAAVNSSESL PPSSSVNDIS SMSTDQTLAS DTDSSLETSA GPLGCCR
//
