ID A0A3P8STB1_AMPPE Unreviewed; 1001 AA.
AC A0A3P8STB1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Discoidin domain receptor tyrosine kinase 1 {ECO:0000313|Ensembl:ENSAPEP00000015545.1};
GN Name=DDR1 {ECO:0000313|Ensembl:ENSAPEP00000015545.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000015545.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000015545.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000015545.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3P8STB1; -.
DR Ensembl; ENSAPET00000015951.1; ENSAPEP00000015545.1; ENSAPEG00000011027.1.
DR GeneTree; ENSGT00940000159733; -.
DR OMA; DVQVFSH; -.
DR Proteomes; UP000265080; Chromosome 7.
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 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00023137}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1001
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017945726"
FT TRANSMEM 465..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..190
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 694..993
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 51..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..646
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 110920 MW; B260612B7072F878 CRC64;
MAFTTLRLCP VAMVTVLAVL VLSSEEHEWH FNPAQCRYAL GMEDGTIPDS DITASSAWSD
STEAKHGRLS TGEGDGAWCP AGAVFPSGSE YLQIDLQRLH FLALVGTQGR HADGHGQEFA
RSYRLRYSRD GQKWITWKDR WGQEVVSGNE NTYDVVLKDL GPPIVARMVR FYPLADRVMS
VCLRVELYGC VWNDGLKAYT APVGHVMHLP GMPIYLNDST YDGSMEQGMQ FGGLGQLCDG
VLGGDDFIQT KELRVWPGYD YLGWSREALG QGSVDIEFHF EKPRLFHNMQ VHSNNRHTQG
VRVFSKVECL FKPGILQPWS SPALTLPVPL EDLKDPSSRP VSLPLGAQAA QILRCKFYFA
DRWLLISEIS FLSEPFEEDV KDADSFPPNF PKFGNTSTFS PPVNQTTSAP TSSSSSNTAQ
PSDPPFTTTF IMDTTGNWTL AGPEFAGVTP RAGLPVAKDD SSNTAILIGC LVGIILLLLA
VIAVILWRQY WKKILGKAQG SLSSDELRVH LSVPSDNVVI NNTHSYSSRY QRIHTFPDDR
DHDREGEGEY QEPSALLRTR DHRDSTALLL NNPAYHLLLP DPRKGLRAVV VPSSTQAEEK
SLNVAQACGL DLNMEKGFPP AHDEPPPYPG SPPYPSLSPP VSPPLPPSVP HYAEADIVSL
QGVSGNNTYA VPALTSSSPG AEAAPLPELP RQCLIFKEKL GEGQFGEVHL CEIENPQDLP
NLEFPFNVRK GRPLLVAVKI LRPDASKNAR NDFLKEVKIL SRLKDPNIIR LLGVCVSSDP
LCMVTEYMEC GDLNQYLSHR VLLDKSGPSH NTPTISYPAL ISMASQIASG MKFLSSLNFV
HRDLATRNCL VGGERGERGE DRGGECHIKI ADFGMSRNLY AGDYYRIQGR AVLPIRWMAW
ECILMGKFTT ASDVWAFGVT LWEMLSVCQE QPYSSLTDEQ VIDNAGEFFR DQGRQVYLSR
PAVCPQGLYE LMLSCWNRDC KLRPSFASIH SFLTEDAMNM V
//
