PIK1_CAEEL
ID PIK1_CAEEL Reviewed; 485 AA.
AC G5ECP4; F5GUH7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Pelle-like serine/threonine-protein kinase pik-1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q05652};
GN Name=pik-1 {ECO:0000312|WormBase:K09B11.1a};
GN ORFNames=K09B11.1 {ECO:0000312|WormBase:K09B11.1a};
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=11516642; DOI=10.1016/s0960-9822(01)00241-x;
RA Pujol N., Link E.M., Liu L.X., Kurz C.L., Alloing G., Tan M.W., Ray K.P.,
RA Solari R., Johnson C.D., Ewbank J.J.;
RT "A reverse genetic analysis of components of the Toll signaling pathway in
RT Caenorhabditis elegans.";
RL Curr. Biol. 11:809-821(2001).
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).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ACTL-1, AND TISSUE SPECIFICITY.
RX PubMed=28099418; DOI=10.1038/nature20818;
RA Chen C., Itakura E., Nelson G.M., Sheng M., Laurent P., Fenk L.A.,
RA Butcher R.A., Hegde R.S., de Bono M.;
RT "IL-17 is a neuromodulator of Caenorhabditis elegans sensory responses.";
RL Nature 542:43-48(2017).
CC -!- FUNCTION: Through association with the adapter actl-1, may act
CC downstream of the receptor complex composed of ilcr-1 and ilcr-2, which
CC is a signaling complex that modulates neuronal activity and animal
CC behavior in response to sensory neuron input.
CC {ECO:0000269|PubMed:28099418}.
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:Q05652};
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:Q05652};
CC -!- SUBUNIT: Interacts with actl-1. {ECO:0000269|PubMed:28099418}.
CC -!- INTERACTION:
CC G5ECP4; Q18008: actl-1; NbExp=3; IntAct=EBI-324661, EBI-324674;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:K09B11.1a};
CC IsoId=G5ECP4-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:K09B11.1b};
CC IsoId=G5ECP4-2; Sequence=VSP_059828;
CC -!- TISSUE SPECIFICITY: Expressed in the nervous system.
CC {ECO:0000269|PubMed:28099418}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. Pelle subfamily. {ECO:0000305}.
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DR EMBL; AF348167; AAK37545.1; -; mRNA.
DR EMBL; BX284604; CAB05550.2; -; Genomic_DNA.
DR EMBL; BX284604; CCA65582.1; -; Genomic_DNA.
DR PIR; T23534; T23534.
DR RefSeq; NP_001255742.1; NM_001268813.1. [G5ECP4-1]
DR RefSeq; NP_001255743.1; NM_001268814.1. [G5ECP4-2]
DR AlphaFoldDB; G5ECP4; -.
DR SMR; G5ECP4; -.
DR IntAct; G5ECP4; 3.
DR STRING; 6239.K09B11.1a; -.
DR EPD; G5ECP4; -.
DR PaxDb; G5ECP4; -.
DR EnsemblMetazoa; K09B11.1a.1; K09B11.1a.1; WBGene00004029. [G5ECP4-1]
DR EnsemblMetazoa; K09B11.1a.2; K09B11.1a.2; WBGene00004029. [G5ECP4-1]
DR EnsemblMetazoa; K09B11.1b.1; K09B11.1b.1; WBGene00004029. [G5ECP4-2]
DR GeneID; 178306; -.
DR KEGG; cel:CELE_K09B11.1; -.
DR CTD; 178306; -.
DR WormBase; K09B11.1a; CE31033; WBGene00004029; pik-1. [G5ECP4-1]
DR WormBase; K09B11.1b; CE45959; WBGene00004029; pik-1. [G5ECP4-2]
DR eggNOG; KOG1187; Eukaryota.
DR GeneTree; ENSGT00940000169271; -.
DR HOGENOM; CLU_000288_21_15_1; -.
DR InParanoid; G5ECP4; -.
DR OMA; YLNTIRH; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; G5ECP4; -.
DR SignaLink; G5ECP4; -.
DR PRO; PR:G5ECP4; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004029; Expressed in embryo and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP 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:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0009605; P:response to external stimulus; IEA:UniProt.
DR CDD; cd08307; Death_Pelle; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037924; Pelle_death.
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; SSF47986; SSF47986; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..485
FT /note="Pelle-like serine/threonine-protein kinase pik-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445233"
FT DOMAIN 185..485
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 115..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 191..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059828"
SQ SEQUENCE 485 AA; 54000 MW; 3A83F59848F0EF2A CRC64;
MDDSLGVSEV VMIPFMKREV LQQICAILDT DNTWETIAPY MPGIELRDVE GCKRYSSYNQ
SPSELLLRIW SSKGYSTTHL YQLFAKTKLI RLMRMMRSQV HEKYHYLENK VTNSTSRVSK
QMVQPPGSQS ASRLKKTEIK ESSPSPAAAA ASQLSRSNTD DTLRVAIEGT LPVTYCELLE
ATNGFAVSNV IGKGGYGTVY KGELKGTGGI VAVKRLHSGN DTSQNGSRER LRQSLTELRT
LARFRHDNIL PIYAYSLEGS EPCLVYQFMS NGSLEDRLLC RKGSVPLTWI QRKEISIGAG
RGLGFLHSFG KTPIIHGDIK TANILLDKHM EPKIGDFGLC RDGHVEAEAM EKHPLIASHI
KGTLAYLAPE FITSKILTTK LDVYSFGIVL LEIASGQRAY SDSRETRGLV EYCQVNKELA
AHRKIPVREI FIDRRAPPLV GDEEKSFLDA LIEVGLAGAN NDRKVRPTMS QIVEYLCKNS
IPPVV
