ID I3K5L4_ORENI Unreviewed; 799 AA.
AC I3K5L4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Discoidin domain receptor tyrosine kinase 1 {ECO:0000313|Ensembl:ENSONIP00000016409.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000016409.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000016409.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001171};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; I3K5L4; -.
DR Ensembl; ENSONIT00000016424.2; ENSONIP00000016409.2; ENSONIG00000013047.2.
DR GeneTree; ENSGT00940000159733; -.
DR HOGENOM; CLU_008873_2_0_1; -.
DR Proteomes; UP000005207; Linkage group LG11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:UniProt.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.60.120.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR048525; DDR1-2_DS-like.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF333; EPITHELIAL DISCOIDIN DOMAIN-CONTAINING RECEPTOR 1; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF21114; DDR1-2_DS-like; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00023137}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..170
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 513..791
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 88819 MW; 8335D4FCFDC3E482 CRC64;
RPPNPRLFMS PSANPCRYAL GMEDGTIPDS DITASSAWSD STEAKHGRLS TGEGDGAWCP
LGSVFPSGSE YLQIDLRRLH FLALVGTQGR HADGHGQEFA RSYRLRYSRD GEKWITWKDR
WGQDVVSGNE NTYDVVLKDL GPPIVARMVR FYPLADRVMS VCLRVELYGC LWNDGLKAYT
APVGHVMQLP GMSVYLNDST YDGSTEQGIQ FGGLGQLCDG VLGGDDFTKT KELRVWPGYD
YLGWSREALG QGSVDIEFHF EKPRVFHHMQ VHSNNRHTQG VRVFSKVECL FKPGILQPWS
SPALTLPVPL EDLKDPSSRP ISLPLGGRPA QILRCKFYFA DRWLLISEIS FLSGPAFAAV
TPRAGLPVAK DDSSNTAILI GCLVGIILLL LAVIVVILWR QYWKKLLGKV GSLSSDELRV
HLSVPSDNVV INNTHSYSSP QEEPPPYPGS PPYPSLSPPV SPPMPPSVPH YAEADIVSLQ
GVSGNNTYAV PALASSSPGA DAAPLPELPR QCLIFKEKLG EGQFGEVHLC EIESPQDLPT
LEFPFNVRKG RPLLVAVKIL RPDASKNARN DFLKEVKILS RLKDPNIIRL LGVCVSSDPL
CMVTEYMECG DLNQYLSQRV LLDKTGYPAL ISMASQIASG MKFLSSLNFV HRDLATRNCL
VGERHIKIAD FGMSRNLYAG DYYRIQGRAV LPIRWMAWEC ILMGKFTTAS DVWAFGVTLW
EMLSVCQEQP YSTLTDEQVI DNAGEFFRDQ GRQVYLSRPA VCPQGLYELM LSCWNRDCKV
RPSFAYIHSF LTEDAMNMV
//