ID KIN29_CAEEL Reviewed; 822 AA. AC Q21017; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 2. DT 25-MAY-2022, entry version 156. DE RecName: Full=Serine/threonine-protein kinase kin-29; DE EC=2.7.11.1; GN Name=kin-29 {ECO:0000312|WormBase:F58H12.1}; GN Synonyms=sma-11 {ECO:0000303|PubMed:15840165}; ORFNames=F58H12.1; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK97497.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=11832225; DOI=10.1016/s0896-6273(02)00572-x; RA Lanjuin A., Sengupta P.; RT "Regulation of chemosensory receptor expression and sensory signaling by RT the KIN-29 Ser/Thr kinase."; RL Neuron 33:369-381(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [3] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AUTOPHOSPHORYLATION, RP AND DISRUPTION PHENOTYPE. RX PubMed=15840165; DOI=10.1186/1471-213x-5-8; RA Maduzia L.L., Roberts A.F., Wang H., Lin X., Chin L.J., Zimmerman C.M., RA Cohen S., Feng X.H., Padgett R.W.; RT "C. elegans serine-threonine kinase KIN-29 modulates TGFbeta signaling and RT regulates body size formation."; RL BMC Dev. Biol. 5:8-8(2005). RN [4] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH TAX-6. RX PubMed=17113567; DOI=10.1016/j.bbrc.2006.10.120; RA Singaravelu G., Song H.O., Ji Y.J., Jee C., Park B.J., Ahnn J.; RT "Calcineurin interacts with KIN-29, a Ser/Thr kinase, in Caenorhabditis RT elegans."; RL Biochem. Biophys. Res. Commun. 352:29-35(2007). RN [5] {ECO:0000305} RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17170704; DOI=10.1038/sj.emboj.7601479; RA van der Linden A.M., Nolan K.M., Sengupta P.; RT "KIN-29 SIK regulates chemoreceptor gene expression via an MEF2 RT transcription factor and a class II HDAC."; RL EMBO J. 26:358-370(2007). RN [6] {ECO:0000305} RP FUNCTION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE. RX PubMed=18832350; DOI=10.1534/genetics.108.094771; RA van der Linden A.M., Wiener S., You Y.J., Kim K., Avery L., Sengupta P.; RT "The EGL-4 PKG acts with KIN-29 salt-inducible kinase and protein kinase A RT to regulate chemoreceptor gene expression and sensory behaviors in RT Caenorhabditis elegans."; RL Genetics 180:1475-1491(2008). 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. {ECO:0000269|PubMed:11832225, CC ECO:0000269|PubMed:15840165, ECO:0000269|PubMed:17113567, CC ECO:0000269|PubMed:17170704, ECO:0000269|PubMed:18832350}. 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:0000269|PubMed:15840165}; 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:0000269|PubMed:15840165}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15840165}; CC -!- SUBUNIT: Interacts with tax-6. {ECO:0000269|PubMed:17113567}. CC -!- INTERACTION: CC Q21017; Q0G819: tax-6; NbExp=3; IntAct=EBI-2893174, EBI-323063; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11832225, CC ECO:0000269|PubMed:15840165}. Nucleus {ECO:0000269|PubMed:11832225, CC ECO:0000269|PubMed:15840165}. Note=Nuclear in larval stage. CC Predominantly cytoplasmic in the adult but translocates into the CC nucleus following heat shock. {ECO:0000269|PubMed:11832225, CC ECO:0000269|PubMed:15840165}. CC -!- TISSUE SPECIFICITY: Primarily neuronal, with additional expression in CC body wall muscle and hypodermal cells. Among neuronal cells, expressed CC in multiple sensory neurons and interneurons in the lateral, anterior, CC and lumbar ganglia, as well as in motor neurons in the ventral motor CC cord. Present in the AWB and AWC olfactory neurons. CC {ECO:0000269|PubMed:11832225}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout all stages of postembryonic CC development. Observed in the intestine and in cells in the tail during CC L1, L3 and L4. {ECO:0000269|PubMed:11832225, CC ECO:0000269|PubMed:15840165}. 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. {ECO:0000269|PubMed:15840165, CC ECO:0000269|PubMed:18832350}. CC -!- DISRUPTION PHENOTYPE: Defective in the expression of a set of CC chemoreceptor genes, and exhibit characteristics associated with CC altered sensory signaling, including increased lifespan, decreased body CC size, and deregulated entry into the dauer developmental stage. Exhibit CC defects in food-induced quiescence behavior. CC {ECO:0000269|PubMed:11832225, ECO:0000269|PubMed:15840165, CC ECO:0000269|PubMed:17170704, ECO:0000269|PubMed:18832350}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. SNF1 subfamily. {ECO:0000305}. 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; AF403714; AAK97497.1; -; mRNA. DR EMBL; FO081451; CCD71675.1; -; Genomic_DNA. DR PIR; T16504; T16504. DR RefSeq; NP_508493.1; NM_076092.5. DR AlphaFoldDB; Q21017; -. DR SMR; Q21017; -. DR BioGRID; 45518; 3. DR IntAct; Q21017; 2. DR MINT; Q21017; -. DR STRING; 6239.F58H12.1; -. DR EPD; Q21017; -. DR PaxDb; Q21017; -. DR PeptideAtlas; Q21017; -. DR EnsemblMetazoa; F58H12.1.1; F58H12.1.1; WBGene00002210. DR GeneID; 180574; -. DR KEGG; cel:CELE_F58H12.1; -. DR UCSC; F58H12.1; c. elegans. DR CTD; 180574; -. DR WormBase; F58H12.1; CE28479; WBGene00002210; kin-29. DR eggNOG; KOG0583; Eukaryota. DR GeneTree; ENSGT00940000156445; -. DR HOGENOM; CLU_016746_0_0_1; -. DR InParanoid; Q21017; -. DR OMA; KIPYWVS; -. DR OrthoDB; 1127668at2759; -. DR PRO; PR:Q21017; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00002210; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046811; F:histone deacetylase inhibitor activity; IDA:WormBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:RHEA. DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central. DR GO; GO:0043053; P:dauer entry; IMP:WormBase. DR GO; GO:0040024; P:dauer larval development; IMP:WormBase. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; TAS:WormBase. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase. DR GO; GO:0046777; P:protein autophosphorylation; IDA:WormBase. DR GO; GO:0006468; P:protein phosphorylation; ISS:WormBase. DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase. DR GO; GO:0000003; P:reproduction; IMP:WormBase. DR GO; GO:0009408; P:response to heat; IEP:WormBase. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:WormBase. 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 1: Evidence at protein level; 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..822 FT /note="Serine/threonine-protein kinase kin-29" FT /id="PRO_0000398619" FT DOMAIN 16..267 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 22..30 FT /note="ATP" FT /evidence="ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 348..367 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 389..423 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 577..602 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 389..418 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 138 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027" FT BINDING 45 FT /note="ATP" FT /evidence="ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 822 AA; 91365 MW; 0BA31A3FB654B2D6 CRC64; MAAPRRRMGL EKIGLYDVGR AIGKGNFATV RIARHKIAKT KVAIKSIDVS ALDRENLIKL EREVKIVKVI DHPHIVKSYE IMRVDNMLYI VSEYCSSGEL YETLIEKGRV AENVARKWFS ETASAVAYLH SQGIVHRDLK AENILLGKNS NIKIIDFGFS NFQTGDQLLN TWCGSPPYAA PELLLGNSYD GMKADIWSMG VLLYILVAGG FPFPSDSVNK LKRSVLSGLV KIPYWVSVEC ADFIRKMLVL NPGKRYTIQN VLQHRWMHIR DDVQKNQAAQ LLEAIPSSSI EIRQQSTKLN PTIMMFMQQH GKWSEEQIID AVLGRDFESP IFATYELLAD KVKKGTLEGT GEEFPRRGSR GSILSGKANV DEQPLTPTIS AHQLAQLNLS SPDCDSDDSS NSDLCDDSPM SSMGPMNHER QFGTPHGLDI IGNRFENRRH TLCASEQLLS PNMMGQFPPP NLLLNNFSMN PPLGFPPMPE GQAAEFPLPS LHPAFATIPI ADLSKMLPVP KSERRASAGE TLLPTNFDLT QHLANLPAPP ISFPTVEEEG KSYLSKYGGK RNTVHCLGNQ LGGGIQNPIP RYQRTPYTKA PPAERRSSWA SPSLSAQQQN HLEKLFKQAL QTNNDMTRLH KEFKGLSHGC AQSQITNEGS SLACPQISIT DEYNRQHNIA PSASSFDPVS IFQKNAQEVV FGQRPATAIG FSSTSFSGMS TPEQTTRSID DRVRSIVCTL PFTEVIDELK ASLNILKIPF SESHEMVYEP QVTEMRRLSL PSGVEIGVAV LPPEHKAHVE FAIINNDSPT SEYLCDQLIC RLRMIDPSWS SE //