KIN15_CAEEL
ID KIN15_CAEEL Reviewed; 488 AA.
AC P34891;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Receptor-like tyrosine-protein kinase kin-15;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=kin-15; ORFNames=M176.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=8413302; DOI=10.1128/mcb.13.11.7133-7143.1993;
RA Morgan W.R., Greenwald I.;
RT "Two novel transmembrane protein tyrosine kinases expressed during
RT Caenorhabditis elegans hypodermal development.";
RL Mol. Cell. Biol. 13:7133-7143(1993).
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).
CC -!- FUNCTION: May be specifically involved in cell-cell interactions
CC regulating cell fusions that generate the hypodermis during
CC postembryonic development. It has a role in the development of the HYP7
CC hypodermal syncytium.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Hypodermal cells.
CC -!- DEVELOPMENTAL STAGE: Expressed during hypodermal development.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; L03524; AAA28151.1; -; Genomic_DNA.
DR EMBL; Z78412; CAB01648.2; -; Genomic_DNA.
DR PIR; C88264; C88264.
DR PIR; I44330; I44330.
DR RefSeq; NP_741035.2; NM_171855.3.
DR AlphaFoldDB; P34891; -.
DR SMR; P34891; -.
DR BioGRID; 39821; 1.
DR STRING; 6239.M176.6a; -.
DR PaxDb; P34891; -.
DR EnsemblMetazoa; M176.6a.1; M176.6a.1; WBGene00002199.
DR GeneID; 174498; -.
DR UCSC; M176.6b; c. elegans.
DR CTD; 174498; -.
DR WormBase; M176.6a; CE46897; WBGene00002199; kin-15.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; P34891; -.
DR OMA; HERIHYL; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; P34891; -.
DR BRENDA; 2.7.10.1; 1045.
DR PRO; PR:P34891; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002199; Expressed in material anatomical entity and 2 other tissues.
DR ExpressionAtlas; P34891; baseline and differential.
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; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..488
FT /note="Receptor-like tyrosine-protein kinase kin-15"
FT /id="PRO_0000024437"
FT TOPO_DOM 27..50
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 144..458
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 150..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 488 AA; 56545 MW; F891B9BEEA128977 CRC64;
MCLKMRYERI KYILLFSLMH LVYSNSTFES FTENPHISSQ ISNVLYMDQM FIIYILICIL
LILISVIVYL SKRYSQQMMQ SSDNITNRRS NPEVRNKSNI YDLPPLLDVT SVNEETPIVK
RPINERIENL EFDPRFEIDQ AKLEISEDKL GSGFFGEVCY GLLSMRTSNT ETDTLQKLSV
AVKQSNDPTQ ENQEKMIEDE TKLMCAIGRN PNILAIIGAV TANSGSARNL LIVEFVECGD
LLKFLEEKKS IFKDELVYEK NGYLLPKSIR RKTYMFNENE DDVIEESLDS LCTSDLLSFS
YQIAEGMEYL ASIPCVHRDL ALRNVLLNKN KTIRIADFGL ARKYQVDGYY RITKGVGTPM
PARWMAPEVM REGKCTEKSD VWSYGVSLYE MFSLGELPYS NVSNSDVFEH VVQGNQLPMP
QYCHPKMYDR MKQFWNFDAT FRPSFSKCVE FFEEHLSVSA TNLLEQIQKT LKSEAERQSK
LEDWIRRD
