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Database: UniProt
Entry: W5L9M9_ASTMX
LinkDB: W5L9M9_ASTMX
Original site: W5L9M9_ASTMX 
ID   W5L9M9_ASTMX            Unreviewed;       973 AA.
AC   W5L9M9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Discoidin domain receptor tyrosine kinase 1 {ECO:0000313|Ensembl:ENSAMXP00000016541.1};
GN   Name=DDR1 {ECO:0000313|Ensembl:ENSAMXP00000016541.1};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000016541.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000016541.1}
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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; XP_007255956.1; XM_007255894.2.
DR   AlphaFoldDB; W5L9M9; -.
DR   Ensembl; ENSAMXT00000016541.2; ENSAMXP00000016541.1; ENSAMXG00000016066.2.
DR   eggNOG; KOG1094; Eukaryota.
DR   GeneTree; ENSGT00940000159733; -.
DR   HOGENOM; CLU_008873_2_0_1; -.
DR   OMA; DVQVFSH; -.
DR   OrthoDB; 2999496at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000016066; Expressed in olfactory epithelium and 13 other cell types or tissues.
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:UP000018467};
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..973
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004865958"
FT   TRANSMEM        444..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..189
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          667..965
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          50..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   973 AA;  108019 MW;  340A4E0F652D36D2 CRC64;
     MATGMLPMLP LLFAALLVSL TAAQDHEWDF DSAKCRYALG MEDGTIPDSD ISASSSWSDS
     TEAKHGRLST GEGDGAWCPA GAVFPSGSEF LQVNLHKLHF LSLVGTQGRH ADGHGREFAR
     SYRLRYSRDG RQWITWKDRW GQEVISGNEN TYDVVLKDLG PPIIARMVRF YPLADRVMSV
     CLRVELYGCV WNDGLKAYAA PMGHVMHLSG SPIYLNDSIY DGSIEAGTLF GGLGQLCDGV
     LGGDDFMESK ELRVWPGYDY VGWSREALGQ PTVDIEFHFE KTRIFHVMQV HSNNRHTQGV
     RVFSEVVCEF KASLLDHWTE PALKLRVPLE DLKDPSSRSV DLPLGGRPAQ ILRCHFAFAD
     RWLLISEISF NSEPFEGSSV FPSGAPPPPP SSTPRSRFFT SSSSPPSSFS PSTSNSTGQS
     LGDDFAAVTP KAGPVAKDDS SNTAILIGCL VGIILLLLAV IVVILWRQYW KKLLNKAQGS
     LSSDELRVHL SVPSDNVVIN NTNTHTYSSR YQRIHTFPDD RDRDAEYQEP STVLRPREQR
     DSTALLLNNP AYHLLLSGLR HDPNRLSNSC RETEKPQNLP QACALDLDDK ALPVQEGPPP
     YPGAPPPLLS GAHYAEASGG GASVPHYAEA DIISLQGVSG NNTYAVPALS ATPTDCPPLP
     ELPRERLIFK EKLGEGQFGE VHLCEIENPQ DLPNLEFPFN VRKGRPLLVA VKILRPDASK
     NARNDFLKEV KILSRLKDPN IIRLLGVCVS SDPLCMVTEY MESGDLNQYL SQRVLLDKTG
     PLHNTPTISY PALISMASQI ASGMKFLASL NFVHRDLATR NCLVGGERGD GEDRMGERHI
     KIADFGMSRN LYAGDYYRIQ GRAVLPIRWM AWECILMGKF TTASDVWAFG VTLWEMLSVC
     QEQPYSHMTD EQVIDNAGEF FRDHGRQIYL TRPAVCPQGL YELMLSCWNR DCKLRPSFTH
     MHSFLAEDAM NMV
//
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