ID   NLK2_XENTR              Reviewed;         454 AA.
AC   B1H3E1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Serine/threonine-protein kinase NLK2;
DE            EC=2.7.11.24;
DE   AltName: Full=Nemo-like kinase 2;
DE            Short=Nlk.2;
GN   Name=nlk.2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAI61361.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula {ECO:0000312|EMBL:AAI61361.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Negatively regulates Wnt/beta-catenin-signaling during
CC       development. Plays a role together with sox11 in neural induction
CC       during early embryogenesis. Involved in TGFbeta-mediated mesoderm
CC       induction in early embryos, acting downstream of map3k7/tak1 to
CC       phosphorylate stat3. Augments the rnf138/narf-directed ubiquitination
CC       and degradation of tcf/lef by enhancing the association of rnf138/narf
CC       and tcf/lef. Phosphorylates mef2a to play a role in anterior neural
CC       development, including eye formation (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q8QGV6};
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:0000250|UniProtKB:Q8QGV6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O54949};
CC   -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC       phosphorylation. {ECO:0000250|UniProtKB:Q63844}.
CC   -!- SUBUNIT: Interacts with sox11, hmgxb4/hmg2l1, rnf138/narf, stat3.1 and
CC       mef2a. {ECO:0000250|UniProtKB:Q8QGV6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O54949}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily. {ECO:0000255}.
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DR   EMBL; BC161361; AAI61361.1; -; mRNA.
DR   RefSeq; NP_001116917.1; NM_001123445.1.
DR   AlphaFoldDB; B1H3E1; -.
DR   SMR; B1H3E1; -.
DR   STRING; 8364.ENSXETP00000054580; -.
DR   PaxDb; 8364-ENSXETP00000027352; -.
DR   Ensembl; ENSXETT00000109106; ENSXETP00000109134; ENSXETG00000046767.
DR   GeneID; 100144684; -.
DR   KEGG; xtr:100144684; -.
DR   AGR; Xenbase:XB-GENE-1218923; -.
DR   CTD; 100144684; -.
DR   Xenbase; XB-GENE-1218923; nlk.2.
DR   eggNOG; KOG0664; Eukaryota.
DR   InParanoid; B1H3E1; -.
DR   OrthoDB; 158564at2759; -.
DR   Proteomes; UP000008143; Chromosome 9.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
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:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISS:UniProtKB.
DR   GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0042501; P:serine phosphorylation of STAT protein; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd07853; STKc_NLK; 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; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF153; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Developmental protein; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation pathway;
KW   Wnt signaling pathway.
FT   CHAIN           1..454
FT                   /note="Serine/threonine-protein kinase NLK2"
FT                   /id="PRO_0000370236"
FT   DOMAIN          67..356
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P53779,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT                   ProRule:PRU10027"
FT   BINDING         73..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53779,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53779,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   454 AA;  50652 MW;  8DD61C2D6CCEEC4F CRC64;
     MAFQGPGRSL PGQLCAGVFG GLIQPPLGQK FYCPNGGSGG GGVPAVPSPL PQALSAPQCN
     GDGRGEPEPD RPIGYGAFGV VWSVTDPRDG KRVALKKMPN VFQNLVSCKR VFRELKMLCF
     FKHDNVLSAL DILQPPQIDC FEEIYVITEL MQTDLHKVIV SPQPLSSDHI KVFLYQILRG
     LKYLHSAGIL HRDIKPGNLL VNSNCVLKIC DFGLARVEEL DESQHMTQEV VTQYYRAPEI
     LMGSRHYRSA IDIWSVGCIF AELLGRRILF QAQSPIQQLD LITDLLGTPP LTAMRSACEG
     ARAHILRGPH KPPSLSVLYM LSGEATHEAV HLLCRMLLFD PLKRISAKDA LAHPYLEEGR
     LRYHTCMCHC CYSVSSGRVY TADFEPTATN RFDDSYEKSL TSVWQVKELV HRFITDQQQG
     KRPPLCINPH SAAFKTFIRS TAWHSSKVSK KEER
//