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 01-OCT-2014, entry version 116. 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 Rhabditoidea; Rhabditidae; Peloderinae; 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 RT by 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 RT investigating biology."; RL Science 282:2012-2018(1998). RN [3] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, RP AUTOPHOSPHORYLATION, 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., RA Zimmerman C.M., Cohen S., Feng X.H., Padgett R.W.; RT "C. elegans serine-threonine kinase KIN-29 modulates TGFbeta signaling RT and 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 RT Caenorhabditis 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., RA Sengupta P.; RT "The EGL-4 PKG acts with KIN-29 salt-inducible kinase and protein RT kinase A to regulate chemoreceptor gene expression and sensory RT behaviors in Caenorhabditis elegans."; RL Genetics 180:1475-1491(2008). CC -!- FUNCTION: Regulates chemoreceptor expression by phosphorylating CC the hda-4 class II histone deacetylase (HDAC) and inhibiting the CC gene repression functions of hda-4 and the mef-2 transcription CC factor, enabling the correct sensing and transduction of food CC signals. Role in determining body size, the dauer decision and CC serotonin-mediated egg laying. May modulate the Sma/Mab pathway CC and regulates development in the later larval stages. CC {ECO:0000269|PubMed:11832225, ECO:0000269|PubMed:15840165, CC ECO:0000269|PubMed:17113567, ECO:0000269|PubMed:17170704, CC ECO:0000269|PubMed:18832350}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000269|PubMed:15840165}. CC -!- COFACTOR: Magnesium. {ECO:0000269|PubMed:15840165}. CC -!- SUBUNIT: Interacts with tax-6. {ECO:0000269|PubMed:17113567}. CC -!- INTERACTION: CC Q0G819:tax-6; NbExp=3; IntAct=EBI-2893174, EBI-2412118; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11832225, CC ECO:0000269|PubMed:15840165}. Nucleus CC {ECO:0000269|PubMed:11832225, ECO:0000269|PubMed:15840165}. CC Note=Nuclear in larval stage. Predominantly cytoplasmic in the CC adult but translocates into the nucleus following heat shock. CC {ECO:0000269|PubMed:11832225, ECO:0000269|PubMed:15840165}. CC -!- TISSUE SPECIFICITY: Primarily neuronal, with additional expression CC in body wall muscle and hypodermal cells. Among neuronal cells, CC expressed in multiple sensory neurons and interneurons in the CC lateral, anterior, and lumbar ganglia, as well as in motor neurons CC in the ventral motor cord. Present in the AWB and AWC olfactory CC neurons. {ECO:0000269|PubMed:11832225}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout all stages of CC postembryonic development. Observed in the intestine and in cells CC in the tail during L1, L3 and L4. {ECO:0000269|PubMed:11832225, CC ECO:0000269|PubMed:15840165}. CC -!- PTM: Autophosphorylated. Elevated cAMP levels appears to act via CC PKA to directly or indirectly phosphorylate multiple sites on kin- CC 29 and 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 CC body size, and deregulated entry into the dauer developmental CC stage. Exhibit 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 CC Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {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; AF403714; AAK97497.1; -; mRNA. DR EMBL; FO081451; CCD71675.1; -; Genomic_DNA. DR PIR; T16504; T16504. DR RefSeq; NP_508493.1; NM_076092.5. DR UniGene; Cel.17940; -. DR ProteinModelPortal; Q21017; -. DR SMR; Q21017; 13-341. DR IntAct; Q21017; 2. DR MINT; MINT-4299353; -. DR STRING; 6239.F58H12.1; -. DR PaxDb; Q21017; -. DR PRIDE; Q21017; -. DR EnsemblMetazoa; F58H12.1; F58H12.1; 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; COG0515; -. DR GeneTree; ENSGT00750000117510; -. DR HOGENOM; HOG000016583; -. DR InParanoid; Q21017; -. DR OMA; TPTISAH; -. DR OrthoDB; EOG70ZZMM; -. DR SignaLink; Q21017; -. DR NextBio; 909952; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase. DR GO; GO:0043053; P:dauer entry; IMP:WormBase. DR GO; GO:0040024; P:dauer larval development; IMP:WormBase. DR GO; GO:0050907; P:detection of chemical stimulus involved in sensory perception; IMP:WormBase. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; TAS:WormBase. 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. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom. 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; Complete proteome; Cytoplasm; Developmental protein; KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 822 Serine/threonine-protein kinase kin-29. FT /FTId=PRO_0000398619. FT DOMAIN 16 267 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 22 30 ATP. {ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159}. FT ACT_SITE 138 138 Proton acceptor. FT {ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027}. FT BINDING 45 45 ATP. {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 //