OLD1_CAEEL
ID OLD1_CAEEL Reviewed; 502 AA.
AC Q17833;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Tyrosine-protein kinase receptor old-1 {ECO:0000305|PubMed:9768365};
DE EC=2.7.10.1 {ECO:0000305};
DE AltName: Full=Overexpression longevity determinant protein 1 {ECO:0000312|WormBase:C08H9.5};
DE Flags: Precursor;
GN Name=old-1 {ECO:0000312|WormBase:C08H9.5};
GN Synonyms=tkr-1 {ECO:0000312|WormBase:C08H9.5};
GN ORFNames=C08H9.5 {ECO:0000312|WormBase:C08H9.5};
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|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 [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=9768365; DOI=10.1016/s0960-9822(98)70448-8;
RA Murakami S., Johnson T.E.;
RT "Life extension and stress resistance in Caenorhabditis elegans modulated
RT by the tkr-1 gene.";
RL Curr. Biol. 8:1091-1094(1998).
RN [3] {ECO:0000305}
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11591319; DOI=10.1016/s0960-9822(01)00453-5;
RA Murakami S., Johnson T.E.;
RT "The OLD-1 positive regulator of longevity and stress resistance is under
RT DAF-16 regulation in Caenorhabditis elegans.";
RL Curr. Biol. 11:1517-1523(2001).
CC -!- FUNCTION: Receptor tyrosine kinase which plays a role in promoting
CC longevity and resistance to stresses including UV irradiation and high
CC temperatures, probably downstream of daf-16.
CC {ECO:0000269|PubMed:11591319, ECO:0000269|PubMed:9768365}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: By UV irradiation, high temperatures, starvation and old
CC age. {ECO:0000269|PubMed:11591319}.
CC -!- DISRUPTION PHENOTYPE: Increased life span and resistance to UV
CC irradiation and high temperatures. {ECO:0000269|PubMed:11591319}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BX284602; CAA91146.3; -; Genomic_DNA.
DR RefSeq; NP_496130.2; NM_063729.2.
DR AlphaFoldDB; Q17833; -.
DR SMR; Q17833; -.
DR STRING; 6239.C08H9.5; -.
DR PaxDb; Q17833; -.
DR EnsemblMetazoa; C08H9.5.1; C08H9.5.1; WBGene00003862.
DR GeneID; 191737; -.
DR KEGG; cel:CELE_C08H9.5; -.
DR CTD; 191737; -.
DR WormBase; C08H9.5; CE45789; WBGene00003862; old-1.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000166715; -.
DR HOGENOM; CLU_000288_7_40_1; -.
DR InParanoid; Q17833; -.
DR OMA; PINEKIM; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; Q17833; -.
DR Reactome; R-CEL-109704; PI3K Cascade.
DR Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CEL-186763; Downstream signal transduction.
DR Reactome; R-CEL-186797; Signaling by PDGF.
DR Reactome; R-CEL-210993; Tie2 Signaling.
DR Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-CEL-9607240; FLT3 Signaling.
DR PRO; PR:Q17833; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003862; Expressed in larva and 1 other tissue.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR InterPro; IPR020766; Kin-15/Old-1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF503; PTHR24416:SF503; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Signal; Stress response; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..502
FT /note="Tyrosine-protein kinase receptor old-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434506"
FT TOPO_DOM 20..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 175..473
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 99..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 181..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 502 AA; 58385 MW; 4606D76C554888B9 CRC64;
MKGTLIFVVF YSSYGFAHCN TILRSSSLSR NFEDSLRRIP RSTDKDETGF EDSNVQEVIF
ILLYCLFVAL AILICGLIIF YNSRKRELRA NRSRGDEYLL EPTSADHKRR NSSNIVPPEP
TPYPITSGES DLRQTPSRLS NVECPPELEL APINEKIMYL HYYAEVEINE EDLDISKGRP
LGSGEFGIIR KGFLRSKNSK NEEKESRLEV AVKLPLNEYN QIQQELIYDE LKVMCAVGKH
PNILALVGGI TFGERKMIVS EFVENGDLLS FLRDNRIYFT NDQWTLETEQ DSLSLVDLLS
FAFQIAKGME YLIHVPCVHR DLALRNVLIK KNRIIRIADF GLARRHKNKD YYKTQSVDTP
LPIHWMAPES IDKLLFTQKS DVWSYGVCLY ELFSLGKSPY ENVIKYDQRD FYWKYVLSYL
NEGKRLAQPA HADAEIYNVM KLCWDLDMNS RTTFLDCIEF FEKELKTTSN EYFLDLTRKL
RSETNNQLRL SNWLSDEKHC DS
