KIN29_CAEEL
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 03-AUG-2022, entry version 157.
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}.
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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 3 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: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 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 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
