ID NLK_CAEBR Reviewed; 657 AA. AC A8XSC1; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 24-JAN-2024, entry version 85. DE RecName: Full=Serine/threonine kinase NLK {ECO:0000250|UniProtKB:Q9U9Y8}; DE EC=2.7.11.24; DE AltName: Full=Loss of intestine protein 1; DE AltName: Full=Nemo-like kinase {ECO:0000250|UniProtKB:Q9U9Y8}; GN Name=lit-1 {ECO:0000312|WormBase:CBG18286}; GN Synonyms=nlk {ECO:0000250|UniProtKB:Q9U9Y8}; GN ORFNames=CBG18286 {ECO:0000312|WormBase:CBG18286}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., RA Durbin R.M., Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative RT genomics."; RL PLoS Biol. 1:166-192(2003). CC -!- FUNCTION: Has a role in the Wnt signaling pathway controlling the CC asymmetry of cell divisions during embryogenesis (By similarity). CC Operates in the AB and EMS cell lineages influencing cell specification CC (By similarity). Required for body wall muscle development, endoderm CC development, pop-1 asymmetry and T-cell division asymmetry (By CC similarity). Component of the beta-catenin-lit-1 complex which promotes CC the phosphorylation, down-regulation and subcellular relocation of pop- CC 1 (By similarity). Regulates plp-1 nuclear localization in embryos (By CC similarity). Plays a role in male tail tip morphogenesis (By CC similarity). {ECO:0000250|UniProtKB:Q9U9Y8}. 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:O54949}; 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:O54949}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:O54949}; CC -!- SUBUNIT: Component of the beta-catenin-lit-1 complex (also called the CC lit-1/wrm-1 complex or the wrm-1/lit-1 kinase complex) at least CC composed of lit-1 and wrm-1 (By similarity). Interacts with wrm-1 (via CC N-terminus); the interaction is direct and activates lit-1 kinase CC activity which leads to the phosphorylation of pop-1 (By similarity). CC This promotes pop-1 interaction with par-5 and translocation of pop-1 CC from the nucleus to the cytoplasm (By similarity). Interacts with pop-1 CC (when phosphorylated on 'Ser-125'); the interaction is dependent on the CC beta-catenin-lit-1 complex (By similarity). CC {ECO:0000250|UniProtKB:Q9U9Y8}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex CC {ECO:0000250|UniProtKB:Q9U9Y8}. Nucleus {ECO:0000250|UniProtKB:Q9U9Y8}. CC Note=Located in the anterior cell cortex before and during asymmetric CC cell division. After division, located preferentially in the nucleus of CC the posterior daughter cell (By similarity). Localizes to the nucleus CC in hyp9 and hyp10 cells prior to male tail tip morphogenesis (By CC similarity). {ECO:0000250|UniProtKB:Q9U9Y8}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; HE600936; CAP35763.2; -; Genomic_DNA. DR AlphaFoldDB; A8XSC1; -. DR SMR; A8XSC1; -. DR STRING; 6238.A8XSC1; -. DR WormBase; CBG18286; CBP39975; WBGene00037733; Cbr-lit-1. DR eggNOG; KOG0664; Eukaryota. DR HOGENOM; CLU_000288_133_2_1; -. DR InParanoid; A8XSC1; -. DR OMA; QHRYLEE; -. DR OrthoDB; 158564at2759; -. DR Proteomes; UP000008549; Chromosome III. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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; 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:SF484; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Developmental protein; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway. FT CHAIN 1..657 FT /note="Serine/threonine kinase NLK" FT /id="PRO_0000372801" FT DOMAIN 208..554 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 391 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 214..222 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 237 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 657 AA; 74169 MW; A31A2CB3AD089A22 CRC64; MPSSTLLELA PNTHSKCKFE TRNRSSSSSS GCSSSSTELY DLAAAHAALI SRQQQILNQG IPIIPEHQLA AAAVAHHHHQ LHPSVQHQLV AGHHHHHLPQ VAHHPAILPR SDVIQQPSHF ALHQHLQNLV QQQQQQQALH HHQQLVGDMA LVSHTHPAAV GSTTCYEKNP QKQQQVPQIP TQPQVAHVSS NAILAAAQPF YQPPVQDSQP DRPIGYGAFG VVWSVTDPRS GKRVALKKMP NVFQNLASCK RVFREIKMLS SFRHDNVLSL LDILQPANPS FFQEFTSWHL TPSIHHQRLI SHIKPICLFF VLPLVSLLCA HMYVCMWWHG TALLEGRKET ITYVLTELMQ SDLHKIIVSP QTLTIDHVKV FVYQILRGLK YLHTANILHR DIKPGNLLVN SNCILKICDF GLARTWDSRD RLNMTHEVVT QYYRAPELLM GARRYTGAVD IWSVGCIFAE LLQRKILFQA AGPIEQLQMI IDLLGTPSQE AMKYACEGAK NHVLRAGPRA PNLQSLYRLS QQTTDDAVDL LVKLLKFNPD ERISVEEALS HPYLEEGRLR FHSCMCSCCY TKANVPSRIF SQELDPKHES PFDPKWEKDM SRLSMFELRE KMYQFVMDRP ALYGVALCIN PQSAAYKNFA SSSVAQASEL PPSPQAW //