NLK2_XENTR
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 03-AUG-2022, entry version 72.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC161361; AAI61361.1; -; mRNA.
DR RefSeq; NP_001116917.1; NM_001123445.1.
DR AlphaFoldDB; B1H3E1; -.
DR SMR; B1H3E1; -.
DR STRING; 8364.ENSXETP00000027352; -.
DR GeneID; 100144684; -.
DR KEGG; xtr:100144684; -.
DR CTD; 100144684; -.
DR Xenbase; XB-GENE-1218923; nlk.2.
DR eggNOG; KOG0664; Eukaryota.
DR InParanoid; B1H3E1; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
