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Database: UniProt
Entry: H0XYQ8_OTOGA
LinkDB: H0XYQ8_OTOGA
Original site: H0XYQ8_OTOGA 
ID   H0XYQ8_OTOGA            Unreviewed;       919 AA.
AC   H0XYQ8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=DDR1 {ECO:0000313|Ensembl:ENSOGAP00000021251.1};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000021251.1, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000021251.1}
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   EMBL; AAQR03060123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0XYQ8; -.
DR   STRING; 30611.ENSOGAP00000021251; -.
DR   Ensembl; ENSOGAT00000031988.1; ENSOGAP00000021251.1; ENSOGAG00000032934.1.
DR   eggNOG; KOG1094; Eukaryota.
DR   GeneTree; ENSGT00940000159733; -.
DR   HOGENOM; CLU_008873_2_0_1; -.
DR   InParanoid; H0XYQ8; -.
DR   OMA; DVQVFSH; -.
DR   TreeFam; TF317840; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR   GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IEA:Ensembl.
DR   GO; GO:0061564; P:axon development; IEA:Ensembl.
DR   GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0043583; P:ear development; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR   GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0001952; P:regulation of cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0010715; P:regulation of extracellular matrix disassembly; IEA:Ensembl.
DR   GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0061302; P:smooth muscle cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0044319; P:wound healing, spreading of cells; IEA:Ensembl.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd05096; PTKc_DDR1; 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   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:UP000005225};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..919
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003546210"
FT   TRANSMEM        417..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..185
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          610..911
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          470..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..496
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   919 AA;  101927 MW;  ADB754CB9BABBBFF CRC64;
     MGPGALSSLL LLLLVATGDA DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR
     HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL
     RYSRDGHRWM DWRDRWGQEV ISGNEDPEGV VLKDLGPPMI ARLVRFYPRA DRVMSVCLRV
     ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD
     FRKSQELRVW PGYDYVGWSN HSFPSGYLEM EFEFDRLRAF QAMQVHCNNM HTLGARLPGG
     VECHFKRGPA MAWEGEPMRH NLGGSLGDPR ARVVSVPLGG RVGRFLQCRF FFAGPWLLFS
     EISFISDVVN NSSPALGGTF PPAPWWPPGP PPTNFSSLEL EPRGQQPVAK AEGSPTAILI
     GCLVAIILLL LLIIALMLWR LHWRRLLSKA ERRVLEEELT VHLSVPGDTI LINNRPGPRE
     PPPYQEPRPR GNPPHSAPCV PSSSALLLSN PAYRLLLATY ARPPRGPGPP TPAWAKPTNT
     QACSGDYMEP EKPGAPLLPP PPQNSVPHYA EADIVTLQGV TGGNTYAVPA LPPGAVGDGP
     PRVDFPRSRL RFKEKLGEGQ FGEVHLCEVE NPQDLVSLDF PLNVRKGHPL LVAVKILRPD
     ATKNARSPCF SRNDFLKEVK IMSRLKDPNI IRLLGVCVQD DPLCMITDYM ENGDLNQFLS
     AHQLEDKAAE GDPGNGEDAQ GPTISYPMLL HVAAQIASGM RYLATLNFVH RDLATRNCLV
     GENFTIKIAD FGMSRNLYAG DYYRVQGRAV LPIRWMAWEC ILMGKFTTAS DVWAFGVTLW
     EVLMLCRAQP FGQLTDEQVI ENAGEFFRDQ GRQVYLSRPP ACPQGLYELM LRCWSRESEQ
     RPPFSQLHRF LAEDVLNTV
//
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