MK08_XENLA
ID MK08_XENLA Reviewed; 426 AA.
AC Q8QHK8; Q8JJC3;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Mitogen-activated protein kinase 8;
DE Short=MAP kinase 8;
DE Short=MAPK 8;
DE EC=2.7.11.24;
DE AltName: Full=Stress-activated protein kinase JNK1;
GN Name=mapk8; Synonyms=jnk1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:BAB85483.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, COFACTOR, TISSUE
RP SPECIFICITY, AND ACTIVITY REGULATION.
RC TISSUE=Oocyte;
RX PubMed=11751577; DOI=10.1093/embo-reports/kvf008;
RA Yamanaka H., Moriguchi T., Masuyama N., Kusakabe M., Hanafusa H.,
RA Takada R., Takada S., Nishida E.;
RT "JNK functions in the non-canonical Wnt pathway to regulate convergent
RT extension movements in vertebrates.";
RL EMBO Rep. 3:69-75(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responds to activation by environmental stress and pro-
CC inflammatory cytokines by phosphorylating a number of transcription
CC factors, and thus regulating transcriptional activity (By similarity).
CC Regulates morphogenic cell movements, controlling convergent extension
CC during gastrulation. May play a role in the regulation of the circadian
CC clock (By similarity). {ECO:0000250|UniProtKB:P45983,
CC ECO:0000250|UniProtKB:Q91Y86, ECO:0000269|PubMed:11751577}.
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:0000269|PubMed:11751577};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation, potentially by the dual-specificity kinase, MKK7.
CC Indirectly activated by Wnt5a. {ECO:0000250|UniProtKB:P45983,
CC ECO:0000269|PubMed:11751577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49185}. Nucleus
CC {ECO:0000250|UniProtKB:Q91Y86}. Synapse {ECO:0000250|UniProtKB:P49185}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Beta;
CC IsoId=Q8QHK8-1; Sequence=Displayed;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q8QHK8-2; Sequence=VSP_007348, VSP_007349;
CC -!- TISSUE SPECIFICITY: Strongly expressed in presumptive ectoderm and
CC mesoderm regions and weakly expressed in endoderm regions during early
CC stages of embryo development. Expressed in the head and dorsal regions
CC during neurula and tailbud stages. {ECO:0000269|PubMed:11751577}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-183 and Tyr-185, 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; AB073999; BAB85483.1; -; mRNA.
DR EMBL; AB074000; BAB91438.1; -; mRNA.
DR EMBL; BC046834; AAH46834.1; -; mRNA.
DR RefSeq; NP_001080184.1; NM_001086715.1. [Q8QHK8-1]
DR AlphaFoldDB; Q8QHK8; -.
DR SMR; Q8QHK8; -.
DR BioGRID; 98118; 1.
DR IntAct; Q8QHK8; 1.
DR MINT; Q8QHK8; -.
DR DNASU; 379876; -.
DR GeneID; 379876; -.
DR KEGG; xla:379876; -.
DR CTD; 379876; -.
DR Xenbase; XB-GENE-1217560; mapk8.L.
DR OMA; DMKSERA; -.
DR BRENDA; 2.7.11.24; 6725.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 379876; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
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 GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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 Alternative splicing; ATP-binding; Biological rhythms; Cytoplasm;
KW Developmental protein; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..426
FT /note="Mitogen-activated protein kinase 8"
FT /id="PRO_0000186268"
FT DOMAIN 26..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 375..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 183..185
FT /note="TXY"
FT COMPBIAS 385..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 33..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 380..384
FT /note="GAAVT -> AQVQQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11751577"
FT /id="VSP_007348"
FT VAR_SEQ 385..426
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11751577"
FT /id="VSP_007349"
SQ SEQUENCE 426 AA; 47928 MW; 51990EC50A556092 CRC64;
MSRSKRDSNF SVFEIGDSTF TVLKRYQNLK PIGSGAQGIV CAAFDAVLER HVAIKKLSRP
FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE FQDLYIVMEL MDANLCQVIQ
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAGTSF
MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCILGEMIK GGVLFPGTDH IDQWNKVIEQ
LGTPCTEFMK KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK
MLVIDASKRI SVDDALQHPY INVWYDPLEA EAPPPKIPDK QLDEREHTIE EWKELIYKEV
LDWEERAKNG VIRGQPAPLG AAVTDGSQAH TSSSSGDASS MSTDPTLPSD TDSSLETSAG
TLGCCR
