NLK_CAEBR
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 03-AUG-2022, entry version 80.
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}.
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DR EMBL; HE600936; CAP35763.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XSC1; -.
DR SMR; A8XSC1; -.
DR STRING; 6238.CBG18286; -.
DR WormBase; CBG18286; CBP39975; WBGene00037733; Cbr-lit-1.
DR eggNOG; KOG0664; Eukaryota.
DR HOGENOM; CLU_000288_133_2_1; -.
DR InParanoid; A8XSC1; -.
DR OMA; DGARCHI; -.
DR OrthoDB; 741207at2759; -.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
