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3-phosphoinositide-dependent protein kinase 1 (EC 2.7.11.1) (Pdk-class protein kinase 1)

 PDPK1_CAEEL             Reviewed;         636 AA.
Q9Y1J3; Q9UA36;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
27-SEP-2017, entry version 136.
RecName: Full=3-phosphoinositide-dependent protein kinase 1;
EC=2.7.11.1;
AltName: Full=Pdk-class protein kinase 1;
Name=pdk-1; ORFNames=H42K12.1;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), MUTAGENESIS OF GLY-297
AND ALA-305, DEVELOPMENTAL STAGE, AND FUNCTION.
STRAIN=Bristol N2;
PubMed=10364160; DOI=10.1101/gad.13.11.1438;
Paradis S., Ailion M., Toker A., Thomas J.H., Ruvkun G.;
"A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3
kinase signals that regulate diapause in Caenorhabditis elegans.";
Genes Dev. 13:1438-1452(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, AND INTERACTION WITH SGK-1; AKT-1 AND AKT-2.
PubMed=15068796; DOI=10.1016/S1534-5807(04)00095-4;
Hertweck M., Goebel C., Baumeister R.;
"C. elegans SGK-1 is the critical component in the Akt/PKB kinase
complex to control stress response and life span.";
Dev. Cell 6:577-588(2004).
[4]
MUTAGENESIS OF GLY-297.
PubMed=16950159; DOI=10.1016/j.neuron.2006.07.024;
Tomioka M., Adachi T., Suzuki H., Kunitomo H., Schafer W.R., Iino Y.;
"The insulin/PI 3-kinase pathway regulates salt chemotaxis learning in
Caenorhabditis elegans.";
Neuron 51:613-625(2006).
[5]
MUTAGENESIS OF GLY-297.
PubMed=22069193; DOI=10.1242/dev.069062;
Christensen R., de la Torre-Ubieta L., Bonni A., Colon-Ramos D.A.;
"A conserved PTEN/FOXO pathway regulates neuronal morphology during C.
elegans development.";
Development 138:5257-5267(2011).
-!- FUNCTION: Involved in the daf-2/insulin receptor-like transduction
pathway, which controls longevity and prevents developmental
arrest at the dauer stage (PubMed:10364160). Phosphorylates and
activates sgk-1, akt-1 and akt-2 (PubMed:15068796).
{ECO:0000269|PubMed:10364160, ECO:0000269|PubMed:15068796}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts directly with sgk-1, akt-1 and akt-2.
{ECO:0000269|PubMed:15068796}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a;
IsoId=Q9Y1J3-1; Sequence=Displayed;
Name=b;
IsoId=Q9Y1J3-2; Sequence=VSP_017049, VSP_017050;
-!- DEVELOPMENTAL STAGE: Expressed in late stage embryos and
throughout life. At L1, expressed in neurons, intestinal cells and
hypodermal cells. In adults, expressed in the somatic gonad.
{ECO:0000269|PubMed:10364160}.
-!- DOMAIN: The PIF-pocket is a small lobe in the catalytic domain
required by the enzyme for the binding to the hydrophobic motif of
its substrates. It is an allosteric regulatory site that can
accommodate small compounds acting as allosteric inhibitors.
{ECO:0000250|UniProtKB:O15530}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PDPK1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF130406; AAD42307.1; -; mRNA.
EMBL; AF130407; AAD42308.1; -; mRNA.
EMBL; FO080926; CCD67851.1; -; Genomic_DNA.
EMBL; FO080926; CCD67852.1; -; Genomic_DNA.
RefSeq; NP_001024742.1; NM_001029571.2. [Q9Y1J3-2]
RefSeq; NP_001024743.1; NM_001029572.2. [Q9Y1J3-1]
UniGene; Cel.8028; -.
ProteinModelPortal; Q9Y1J3; -.
SMR; Q9Y1J3; -.
BioGrid; 45427; 2.
DIP; DIP-27322N; -.
IntAct; Q9Y1J3; 5.
MINT; MINT-1039329; -.
STRING; 6239.H42K12.1b; -.
iPTMnet; Q9Y1J3; -.
EPD; Q9Y1J3; -.
PaxDb; Q9Y1J3; -.
PeptideAtlas; Q9Y1J3; -.
EnsemblMetazoa; H42K12.1b; H42K12.1b; WBGene00003965. [Q9Y1J3-1]
GeneID; 180475; -.
KEGG; cel:CELE_H42K12.1; -.
UCSC; H42K12.1b; c. elegans. [Q9Y1J3-1]
CTD; 180475; -.
WormBase; H42K12.1a; CE28739; WBGene00003965; pdk-1. [Q9Y1J3-2]
WormBase; H42K12.1b; CE28740; WBGene00003965; pdk-1. [Q9Y1J3-1]
eggNOG; KOG0592; Eukaryota.
eggNOG; ENOG410XRT8; LUCA.
GeneTree; ENSGT00550000074819; -.
HOGENOM; HOG000233026; -.
InParanoid; Q9Y1J3; -.
KO; K06276; -.
OMA; HAYIPAT; -.
OrthoDB; EOG091G06CX; -.
PhylomeDB; Q9Y1J3; -.
Reactome; R-CEL-114604; GPVI-mediated activation cascade.
Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
Reactome; R-CEL-165158; Activation of AKT2.
Reactome; R-CEL-202424; Downstream TCR signaling.
Reactome; R-CEL-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-CEL-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-CEL-389513; CTLA4 inhibitory signaling.
Reactome; R-CEL-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-CEL-444257; RSK activation.
Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-CEL-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-CEL-5625740; RHO GTPases activate PKNs.
Reactome; R-CEL-6804757; Regulation of TP53 Degradation.
SignaLink; Q9Y1J3; -.
PRO; PR:Q9Y1J3; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00003965; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IMP:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0040024; P:dauer larval development; IMP:WormBase.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007611; P:learning or memory; IMP:WormBase.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IMP:WormBase.
GO; GO:0050920; P:regulation of chemotaxis; IMP:WormBase.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; IGI:UniProtKB.
CDD; cd01262; PH_PDK1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR033931; PDK1-typ_PH.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF14593; PH_3; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00233; PH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50729; SSF50729; 2.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Coiled coil; Complete proteome;
Cytoplasm; Developmental protein; Kinase; Nucleotide-binding;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 636 3-phosphoinositide-dependent protein
kinase 1.
/FTId=PRO_0000086503.
DOMAIN 69 364 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 79 81 ATP. {ECO:0000250|UniProtKB:O15530}.
NP_BIND 152 154 ATP. {ECO:0000250|UniProtKB:O15530}.
REGION 100 149 PIF-pocket.
{ECO:0000250|UniProtKB:O15530}.
COILED 550 631 {ECO:0000255}.
ACT_SITE 197 197 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 98 98 ATP. {ECO:0000250|UniProtKB:O15530}.
BINDING 158 158 ATP. {ECO:0000250|UniProtKB:O15530}.
BINDING 201 201 ATP; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O15530}.
BINDING 215 215 ATP. {ECO:0000250|UniProtKB:O15530}.
VAR_SEQ 259 260 Missing (in isoform b).
{ECO:0000303|PubMed:10364160}.
/FTId=VSP_017049.
VAR_SEQ 427 428 Missing (in isoform b).
{ECO:0000303|PubMed:10364160}.
/FTId=VSP_017050.
MUTAGEN 297 297 G->R: In sa680; developmental arrest at
dauer stage, extended life span,
increased body size, low fertility, and
defects in egg-laying and social
behavior. Fails to avoid NaCl after
exposure to NaCl under starvation
conditions. Restores normal AIY
interneuron neurite outgrowth in a daf-18
(mg198) background mutant.
{ECO:0000269|PubMed:10364160,
ECO:0000269|PubMed:16950159,
ECO:0000269|PubMed:22069193}.
MUTAGEN 305 305 A->V: In mg142; no obvious phenotype.
{ECO:0000269|PubMed:10364160}.
SEQUENCE 636 AA; 71917 MW; 5885237039D80AF2 CRC64;
MEDLTPTNTS LDTTTTNNDT TSDREAAPTT LNLTPTASES ENSLSPVTAE DLIAKSIKEG
CPKRTSNDFM FLQSMGEGAY SQVFRCREVA TDAMFAVKVL QKSYLNRHQK MDAIIREKNI
LTYLSQECGG HPFVTQLYTH FHDQARIYFV IGLVENGDLG ESLCHFGSFD MLTSKFFASE
ILTGLQFLHD NKIVHRDMKP DNVLIQKDGH ILITDFGSAQ AFGGLQLSQE GFTDANQASS
RSSDSGSPPP TRFYSDEEVP EENTARRTTF VGTALYVSPE MLADGDVGPQ TDIWGLGCIL
FQCLAGQPPF RAVNQYHLLK RIQELDFSFP EGFPEEASEI IAKILVRDPS TRITSQELMA
HKFFENVDWV NIANIKPPVL HAYIPATFGE PEYYSNIGPV EPGLDDRALF RLMNLGNDAS
ASQPSTFRPS NVEHRGDPFV SEIAPRANSE AEKNRAARAQ KLEEQRVKNP FHIFTNNSLI
LKQGYLEKKR GLFARRRMFL LTEGPHLLYI DVPNLVLKGE VPWTPCMQVE LKNSGTFFIH
TPNRVYYLFD LEKKADEWCK AINDVRKRYS VTIEKTFNSA MRDGTFGSIY GKKKSRKEMM
REQKALRRKQ EKEEKKALKA EQVSKKLSMQ MDKKSP


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