DYF5_CAEEL
ID DYF5_CAEEL Reviewed; 489 AA.
AC B3WFY8; G5EG21;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Serine/threonine-protein kinase dyf-5 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9JKV2};
GN Name=dyf-5 {ECO:0000312|WormBase:M04C9.5b};
GN ORFNames=M04C9.5 {ECO:0000312|WormBase:M04C9.5b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:CAM58448.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAM58448.1};
RX PubMed=17420466; DOI=10.1073/pnas.0606974104;
RA Burghoorn J., Dekkers M.P., Rademakers S., de Jong T., Willemsen R.,
RA Jansen G.;
RT "Mutation of the MAP kinase DYF-5 affects docking and undocking of kinesin-
RT 2 motors and reduces their speed in the cilia of Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7157-7162(2007).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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).
CC -!- FUNCTION: Serine/threonine-protein kinase which is required for
CC ciliogenesis. Regulates the length and the morphology of sensory neuron
CC cilia. In addition, plays a role in the anterograde intraflagellar
CC transport (IFT) in the cilia by regulating the undocking of kinesin-II
CC motor complex (composed of klp-11, klp-20 and kap-1) before reaching
CC the distal segment and the docking of kinesin motor osm-3 onto IFT
CC cargos. {ECO:0000269|PubMed:17420466}.
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:Q9JKV2};
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:Q9JKV2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9JKV2};
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:17420466}. Cell
CC projection, dendrite {ECO:0000269|PubMed:17420466}. Cell projection,
CC axon {ECO:0000269|PubMed:17420466}. Cell projection, cilium
CC {ECO:0000269|PubMed:17420466}. Note=Enriched at the transition zone
CC between the base of the cilia and the dendrites and to a lesser extent
CC in the cilia. {ECO:0000269|PubMed:17420466}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:M04C9.5b};
CC IsoId=B3WFY8-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:M04C9.5a};
CC IsoId=B3WFY8-2; Sequence=VSP_058711, VSP_058712;
CC -!- TISSUE SPECIFICITY: Expressed in head neurons including amphid and
CC labial sensory neurons and 3 pairs of neurons in the tail including
CC phasmid sensory neurons. In male, expressed in the tail including the
CC sensory rays and the spicule. {ECO:0000269|PubMed:17420466}.
CC -!- DISRUPTION PHENOTYPE: Sensory neuron cilia are longer, not correctly
CC aligned in the amphid channel, more dispersed, misdirected and
CC sometimes turned back towards the transition zone. Abnormal
CC localization of kap-1 along the full cilia length. Abnormal
CC accumulation in the middle of cilia and in the distal segment and
CC reduced speed along the cilium axoneme of components of the IFT
CC machinery kap-1, osm-3, xbx-1, che-11 and osm-5. In a kap-1 mutant
CC background, 30 percent of mutants have branched cilia. In a kap-1 and
CC osm-3 double mutant background, loss of cilia formation.
CC {ECO:0000269|PubMed:17420466}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. RCK subfamily. {ECO:0000305}.
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DR EMBL; AM498742; CAM58448.1; -; mRNA.
DR EMBL; BX284601; CAB06021.2; -; Genomic_DNA.
DR EMBL; BX284601; CAQ76489.2; -; Genomic_DNA.
DR PIR; T23710; T23710.
DR RefSeq; NP_001129786.2; NM_001136314.2. [B3WFY8-1]
DR RefSeq; NP_492493.2; NM_060092.3. [B3WFY8-2]
DR AlphaFoldDB; B3WFY8; -.
DR SMR; B3WFY8; -.
DR STRING; 6239.M04C9.5b; -.
DR PaxDb; B3WFY8; -.
DR PeptideAtlas; B3WFY8; -.
DR EnsemblMetazoa; M04C9.5a.1; M04C9.5a.1; WBGene00001121. [B3WFY8-2]
DR EnsemblMetazoa; M04C9.5b.1; M04C9.5b.1; WBGene00001121. [B3WFY8-1]
DR GeneID; 187442; -.
DR KEGG; cel:CELE_M04C9.5; -.
DR CTD; 187442; -.
DR WormBase; M04C9.5a; CE40815; WBGene00001121; dyf-5. [B3WFY8-2]
DR WormBase; M04C9.5b; CE46107; WBGene00001121; dyf-5. [B3WFY8-1]
DR eggNOG; KOG0661; Eukaryota.
DR GeneTree; ENSGT00940000156581; -.
DR InParanoid; B3WFY8; -.
DR OMA; TRFEYAY; -.
DR OrthoDB; 76933at2759; -.
DR PhylomeDB; B3WFY8; -.
DR PRO; PR:B3WFY8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001121; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:WormBase.
DR GO; GO:0004707; F:MAP kinase activity; ISS:WormBase.
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; ISS:WormBase.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0035720; P:intraciliary anterograde transport; IMP:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; IDA:WormBase.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IGI:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:WormBase.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IGI:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..489
FT /note="Serine/threonine-protein kinase dyf-5"
FT /id="PRO_0000438690"
FT DOMAIN 11..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 366..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 444..471
FT /note="YIPSFGARQTGPTVSNQTNNHSANNSHS -> SSFCSSHKSLFLFVFLLPFG
FT ACLSSQYS (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058711"
FT VAR_SEQ 472..489
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058712"
SQ SEQUENCE 489 AA; 55787 MW; FBA0A4994B4C431E CRC64;
MSSAVKLADR YLMTKRLGDG TFGEVMLAKK IDTGDRVAIK RMKKKFYSWE EAMSLREVKS
LKKLNHPNII KLREVIREND ILYFVFEFMQ ENLYELMKDR DRYFPESVIR NIIYQVLQGL
AFMHKNGFFH RDMKPENIMC NGTELVKIAD FGLAREIRSK PPYTDYVSTR WYRAPEILLR
STSYNSPIDM WALGCIMAEL YILRPLFPGT SEMDQLFKII SILGTPNKDE WPEGYQLASA
MNFRFQQVVA TPMEQVVNTI SKEGMKLMMD MMLWNPEKRP NANQSLRYKY FQVAEKLGAP
VVSQPAPGSI RKTSAASVKS DTKAMTAKAA KKDYIGSENV SPQQPAKVID RHINRNLPLN
KETLFEKSDN KPLGPTKSNE AKPTAKEIYL SKSKYVPGQV SKDTHQNQIM TTNGLTGTTK
TTTFSAKKEG RTAVQTRFEY AYGYIPSFGA RQTGPTVSNQ TNNHSANNSH SPNKMSNTGR
VDWAAKYVK
