YS3J_CAEEL
ID YS3J_CAEEL Reviewed; 867 AA.
AC Q19238; A0A4V0ILN4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Putative tyrosine-protein kinase F09A5.2;
DE EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
GN ORFNames=F09A5.2 {ECO:0000312|WormBase:F09A5.2b};
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 [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 -!- 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:PRU00159};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:F09A5.2b};
CC IsoId=Q19238-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F09A5.2a};
CC IsoId=Q19238-2; Sequence=VSP_060802;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BX284606; CAA93646.2; -; Genomic_DNA.
DR EMBL; BX284606; VTW47554.1; -; Genomic_DNA.
DR PIR; T20625; T20625.
DR RefSeq; NP_510182.1; NM_077781.3.
DR AlphaFoldDB; Q19238; -.
DR SMR; Q19238; -.
DR STRING; 6239.F09A5.2; -.
DR PaxDb; Q19238; -.
DR PRIDE; Q19238; -.
DR EnsemblMetazoa; F09A5.2a.1; F09A5.2a.1; WBGene00008599. [Q19238-2]
DR EnsemblMetazoa; F09A5.2b.1; F09A5.2b.1; WBGene00008599. [Q19238-1]
DR UCSC; F09A5.2; c. elegans. [Q19238-1]
DR WormBase; F09A5.2a; CE53176; WBGene00008599; -.
DR WormBase; F09A5.2b; CE53228; WBGene00008599; -.
DR eggNOG; KOG0200; Eukaryota.
DR HOGENOM; CLU_326319_0_0_1; -.
DR InParanoid; Q19238; -.
DR OrthoDB; 560553at2759; -.
DR PhylomeDB; Q19238; -.
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:Q19238; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00008599; Expressed in larva and 2 other tissues.
DR ExpressionAtlas; Q19238; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..867
FT /note="Putative tyrosine-protein kinase F09A5.2"
FT /id="PRO_0000088186"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 467..757
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 782..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 626
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 473..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 351..354
FT /note="HVTE -> Q (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060802"
SQ SEQUENCE 867 AA; 98103 MW; 28CCAEFE8E1775F2 CRC64;
MHHPKETLLI DSSNPSYSHL TEYRFDNLKR EESRSTSLFG DRRRVMKILS GFSLIIIVVF
IFATSHEQAL STTGDLTSST QSTTHGGVVF TYPTTRKSPG KGCVLNSQRS TPKNLKQYTG
NISDACLAGI KSSNCKTWLM TNAVILKYSD DVVSNCPSIL EFVNKTSLSC SGKSQIQYMY
PQSDSASSDC NHSYDFNSNA LNRAIYNFNY SKTLISTSYA NTPGFAMYTF LLKIMNCVNK
NGIKLDAGIL NIFTDMTYID LCESDVFMSS FPDTLNKLIE AGYIVKFYFL NQNLQDTQKN
VENVLAGCKY MNSRSYCEIV DWSYHSENPN EFEICIPDSQ PSGKKEDFNW HVTELLLIIG
IPCISLTICC IAFFVCCLKC AKLKMAMMRM NVFSNDTHQN PDEMELKKRW IGMRKKFNKD
VENGSCKELN TQKWSHFASA NNYMDIQALA NANKKDIWEI DTKNLLVQED HLLGNGAFAN
VYKGIVKGKI PLLVVNNSLN MTVESENNGH YEAAIKKLPA HADEQNHLDF FHEIDFMKRL
GHHPHVISML GCVSNPYEPL IVVEYCARGD LLKFLRRHKD YVLMNKTDDC PIEADMCLRI
KDLVSIAWQV ADGMSYLASK NFIHRDLAAR NILLTKSLTA KVSDFGLCRY MDSALYTAKG
GRLPIKWMSV EALKLYEFST KTDVWSFGVL LFEIFSMGDV PYPTIQQVDM LEHLLAGGRL
SQPLKCPNEI FNIMQKCWAE KPEDRPEFNE MRGEITVMLN LDDESYGYLS VESQGGPKYT
QLTMQDSKET APCSTPGGSQ DMDEDGDYDS GSEGHSQGTC AQLDQVLTER FGEEQKKEIK
QIFCEITSKS MRGKRRQSNS TVSTYQS
