KIN29_CAEBR
ID KIN29_CAEBR Reviewed; 813 AA.
AC A8WRV1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Serine/threonine-protein kinase kin-29;
DE EC=2.7.11.1;
GN Name=kin-29 {ECO:0000312|EMBL:CAP23209.2}; ORFNames=CBG02036;
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:CAP23209.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP23209.2};
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: Regulates chemoreceptor expression by phosphorylating the
CC hda-4 class II histone deacetylase (HDAC) and inhibiting the gene
CC repression functions of hda-4 and the mef-2 transcription factor,
CC enabling the correct sensing and transduction of food signals. Role in
CC determining body size, the dauer decision and serotonin-mediated egg
CC laying. May modulate the Sma/Mab pathway and regulates development in
CC the later larval stages (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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q21017};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q21017};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q21017};
CC -!- SUBUNIT: Interacts with tax-6. {ECO:0000250|UniProtKB:Q21017}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q21017}. Nucleus
CC {ECO:0000250|UniProtKB:Q21017}. Note=Nuclear in larval stage.
CC Predominantly cytoplasmic in the adult but translocates into the
CC nucleus following heat shock (By similarity).
CC {ECO:0000250|UniProtKB:Q21017}.
CC -!- PTM: Autophosphorylated. Elevated cAMP levels appears to act via PKA to
CC directly or indirectly phosphorylate multiple sites on kin-29 and
CC inhibit function (By similarity). {ECO:0000250|UniProtKB:Q21017}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; HE601451; CAP23209.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WRV1; -.
DR SMR; A8WRV1; -.
DR STRING; 6238.CBG02036; -.
DR EnsemblMetazoa; CBG02036.1; CBG02036.1; WBGene00025179.
DR WormBase; CBG02036; CBP33973; WBGene00025179; Cbr-kin-29.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_016746_0_0_1; -.
DR InParanoid; A8WRV1; -.
DR OMA; KIPYWVS; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046811; F:histone deacetylase inhibitor activity; IEA:EnsemblMetazoa.
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:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0043053; P:dauer entry; IEA:EnsemblMetazoa.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:0040010; P:positive regulation of growth rate; IEA:EnsemblMetazoa.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:EnsemblMetazoa.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000003; P:reproduction; IEA:EnsemblMetazoa.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblMetazoa.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:EnsemblMetazoa.
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; 1.
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.
FT CHAIN 1..813
FT /note="Serine/threonine-protein kinase kin-29"
FT /id="PRO_0000398618"
FT DOMAIN 18..269
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 383..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 813 AA; 90497 MW; 96A6749A765E9CF1 CRC64;
MAAAAPKRRM GLEKIGLYDV GRAIGKGNFA TVRIARHRIA KTKVAVKSID VSKLDKENLI
KLEREVKIVT MIDHPHIVKC YEIMRVDNML YIVSEYCSTG ELYATLMGKG RVTEDIARKW
FTETAAAVSY LHNKGIVHRD LKTENILLGK DSKIKLIDFG FSNFQTPDQL LNTWCGSPPY
AAPELLLGNS YDGMKADIWS MGVLLYILVT GGFPFGSESV NDLKRSVLSG VVKIPYWVSV
ECADFIRKML VLNPTKRMTI QNVLAHRWMH IRNDVKKQVQ NLESSIRPTP SKLNPTIMMF
MQQHGKWTEE QIIDAVLGRN FESPIFATYE LLADKVKIGS LEGTGEEYPR RGSRGSILSG
RANVDEQPLT PTISAHQLAQ LNLSSPDCDS DDSSNSDLCD ESPLSSLEPN HKQFTLPRGL
DLMGNRFENR RHTLCASEQL LSPNLMGQFP PPNLLLNNFT MSPLGFPPMP EGQAAEFPFP
SLHPALGAFP TTDLSKMLPV PKSERRASAG ETLLPTNFDL QQHLANLSAN PVSFPTVEEE
GRSYLAKYGG KRNTVHCLGN QIGGGVQNPI PRYQRTPYAK APPAERRSSW ASPSLSQQQQ
SHLEKIFKDA LQTNNDISRL HKEFKNLSHG CAQSQITNEG SSLACPQISI TDEYNRQHNI
APSASSFDPV SIFQKNAQEV VFGQRPATAI GFSSTSFSGM STPEQTTRSM DDRVRSIVCT
LPFAEVVEEL KSSLNILKIP FAETQEMVYE PQVTEMRRLS LPSGVEIGVA VLPPEHKSHV
EFAIINNDSP TSEILCDQLI CRLRMIDPNW SSE
