DLK1_CAEBR
ID DLK1_CAEBR Reviewed; 857 AA.
AC A8X775;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase dlk-1 {ECO:0000250|UniProtKB:O43283};
DE EC=2.7.11.25;
DE AltName: Full=DAP kinase-like kinase;
DE AltName: Full=Death-associated protein kinase-like kinase;
GN Name=dlk-1 {ECO:0000312|EMBL:CAP28486.1}; ORFNames=CBG08707;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP28486.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP28486.1};
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: Component of a MAP kinase pathway that functions
CC presynaptically to regulate synaptic architecture and presynaptic
CC differentiation. Phosphorylates and activates mkk-4 (By similarity).
CC {ECO:0000250|UniProtKB:O01700}.
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=2.7.11.25;
CC Evidence={ECO:0000250|UniProtKB:O43283};
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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O43283};
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:O01700}.
CC -!- PTM: Ubiquitinated by rpm-1. Negatively regulated by ubiquitination by
CC fsn-1 bound rpm-1, followed by degradation (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000250|UniProtKB:O01700}.
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DR EMBL; HE601079; CAP28486.1; -; Genomic_DNA.
DR RefSeq; XP_002640597.1; XM_002640551.1.
DR AlphaFoldDB; A8X775; -.
DR SMR; A8X775; -.
DR STRING; 6238.CBG08707; -.
DR PRIDE; A8X775; -.
DR EnsemblMetazoa; CBG08707a.1; CBG08707a.1; WBGene00030453.
DR GeneID; 8582592; -.
DR KEGG; cbr:CBG_08707; -.
DR CTD; 8582592; -.
DR WormBase; CBG08707a; CBP02144; WBGene00030453; Cbr-dlk-1.
DR eggNOG; KOG4721; Eukaryota.
DR HOGENOM; CLU_315036_0_0_1; -.
DR InParanoid; A8X775; -.
DR OMA; RETPYAN; -.
DR OrthoDB; 938929at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase;
KW Ubl conjugation.
FT CHAIN 1..857
FT /note="Mitogen-activated protein kinase kinase kinase dlk-
FT 1"
FT /id="PRO_0000353197"
FT DOMAIN 62..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 441..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43283,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 68..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43283,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43283,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 857 AA; 96346 MW; F3FF5FBB27CFC75E CRC64;
MMAAAGNASK PSLNNFYAEG LGHLREGLFS CFRPVLGYFG GKPTQEIEKT EDEGWEIPFD
AISNLEWLGS GSQGAVFHGQ YENRTVAVKK VNQLKETEIK HLRHLRHKNI IEFLGVCSKS
PCYCIVMEYC PKGQLCTVLR QKNLITRQMF SDWVKEIADG MHYLHQNKVI HRDLKSPNIL
ISAEDSIKIC DFGTSHLQKK NDSTMMSFCG TVSWMAPEMI KKEPCNEKVD VYSFGVVLWE
MLTRETPYAN IAQMAIIFGV GTNILNLPMP EEAPRGLVLL IKQCLSQKGR NRPSFSHIRQ
HWEIFKPELF EMTEDEWQVA WDSYREFAKA IQYPSTVTKD HGGPKSAFAM EEEMQRKRHE
QLNHIKDIRH MYEAKLKRTN KMYDKLQGCF TELKLKEHEL AEWERNLAER EQMHVYNSPR
SMSAAPRFQL RGNCYPNEAY EEMSSDEDGQ CPPCRGSPYR NSNMSTSSGA QSSPFSRQSS
CRSSAGQQTR RSEGANAQKI SRNDLLRHSS SYWETIGNRG SPARGSGFSQ DSGVWSAGVS
SMAINGGVQG GVPVTYAQTI YRNGEGRWSD GRIASRRRVS SSANKNLPPV FFTRDSPSRV
PHGVVNHSAP RSSSKLNRSS YPSRNAPHQL EDGCCCNHGR VPRAKSVAVS MATRGRSPTP
YDNDASDAAE NPDIHYELQI PETTSYDEAL KSIGETDDVE MDAANGVNPI YSSPITTYNN
PCHVNYENVT EENANDIDLT SSMDSRRSRA DDADVESSED EGNGNNILNT SMESEELRYR
IDTSQSTMMS SLERSLEIGA TRSDGLSDNE RRVQAVKHSI KTHRRTSSNP QAIIHQRIEE
YSSSATEDSD DAGAVRI
