ID A0A3Q1H5A9_9TELE Unreviewed; 1001 AA.
AC A0A3Q1H5A9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Discoidin domain receptor tyrosine kinase 1 {ECO:0000313|Ensembl:ENSAPOP00000024150.1};
GN Name=DDR1 {ECO:0000313|Ensembl:ENSAPOP00000024150.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000024150.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000024150.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q1H5A9; -.
DR Ensembl; ENSAPOT00000009482.1; ENSAPOP00000024150.1; ENSAPOG00000006420.1.
DR GeneTree; ENSGT00940000159733; -.
DR InParanoid; A0A3Q1H5A9; -.
DR OrthoDB; 2999496at2759; -.
DR Proteomes; UP000257200; Unplaced.
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:UP000257200};
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_5018693512"
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 395..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..643
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 622..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 110969 MW; C982233A24B6B50C CRC64;
MAFTTLRLCP VAVVAVLAVL VLSSEEHEWH FNPAQCRYAL GMEDGTIPDS DITASSAWSD
STEAKHGRLS TGEGDGAWCP AGAVFPSGSE YLQIDLHRLH FLALVGTQGR HADGHGQEFA
RSYRLRYSRD GQKWITWKDR WGQEVVSGNE NTYDVVLKDL GPPIVARMVR FYPLADRVMS
VCLRVELYGC VWNDGLKAYT APVGHVMHLP GMSIYLNDST YDGSTEQGMQ FGGLGQLCDG
VLGGDDFIET KELRVWPGYD YLGWSREALG QGSVDIEFHF EKPRVFHNMQ VHSNNRHTQG
VRVFSKVECL FKPGILQPWS SPALTLPVPL EDLKDPSSRP ISLPLGAQAA QILRCKFYFA
DRWLLISEIS FLSEPFEEDV KDADSFPPNF PKFGNTSTFP PPVNQTTSTP ASSSSSNTAR
PSDPPFTTTF MMDSTGNWTL AGPEFAGVTS RAGLPVAKDD SSNTAILIGC LVGIILLLLA
VIAVILWRQY WKKILGKAQG SLSSDELRVH LSVPSDNVVI NNTHSYSSRY QRIHTFPDDR
DHDREGEGEY QEPSALLRTR DHRDSTALLL NNPAYHLLLP DPRKGPRAVL VPSSTQAQEK
SLNVAQACGL DLDMEKGFPL AHDEPPPYPG SPPYPSLSPP VSPPLPPSVP HYAEADIVSL
QGVSGNNTYA VPALTSSSPG AEAALLPELP RQCLIFKEKL GEGQFGEVHL CEIENPQDLP
ILEFPFNVRK GRPLLVAVKI LRPDASKNAR NDFLKEVKIL SRLKDPNIIR LLGVCVSSDP
LCMVTEYMEC GDLNQYLSHR VLLDKSGPSH NTPTISYPAL ISMASQIASG MKFLSSLNFV
HRDLATRNCL VGGERGERGE DRGGERHIKI ADFGMSRNLY AGDYYRIQGR AVLPIRWMAW
ECILMGKFTT ASDVWAFGVT LWEMLSVCQE QPYSNLTDEQ VIDNAGEFFR DQGRQVYLSR
PAVCPQGLYE LMLSCWNRDC KLRPSFASIH SFLTEDAMNM V
//
