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Database: UniProt
Entry: M3YJQ9_MUSPF
LinkDB: M3YJQ9_MUSPF
Original site: M3YJQ9_MUSPF 
ID   M3YJQ9_MUSPF            Unreviewed;       919 AA.
AC   M3YJQ9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 70.
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:ENSMPUP00000011566.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000011566.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000011566.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-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; AEYP01102818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012906003.1; XM_013050549.1.
DR   RefSeq; XP_012906005.1; XM_013050551.1.
DR   RefSeq; XP_012906006.1; XM_013050552.1.
DR   RefSeq; XP_012906007.1; XM_013050553.1.
DR   RefSeq; XP_012906008.1; XM_013050554.1.
DR   RefSeq; XP_012906009.1; XM_013050555.1.
DR   AlphaFoldDB; M3YJQ9; -.
DR   STRING; 9669.ENSMPUP00000011566; -.
DR   Ensembl; ENSMPUT00000011757.1; ENSMPUP00000011566.1; ENSMPUG00000011659.1.
DR   GeneID; 101672046; -.
DR   KEGG; mpuf:101672046; -.
DR   CTD; 780; -.
DR   eggNOG; KOG1094; Eukaryota.
DR   GeneTree; ENSGT00940000159733; -.
DR   HOGENOM; CLU_008873_2_0_1; -.
DR   InParanoid; M3YJQ9; -.
DR   OMA; DVQVFSH; -.
DR   OrthoDB; 2999496at2759; -.
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}; 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..919
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004044929"
FT   TRANSMEM        423..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..188
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          616..911
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          476..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..502
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   919 AA;  101491 MW;  1A075026414CF061 CRC64;
     MGPGALTSLP LLLLLLLVAT GDADMKGHFD PAKCRYALGM QDRTIPDGDI SASSSWSDST
     AARHSRLESS DGDGAWCPAG PVFPKEEEYL QVDLRRLHLV ALVGTQGRHA GGLGKEFSPS
     YRLRYSRDGH RWMDWRDRWG QEVILGNEDP GGVVLKDLGP PMVARLVRFY PRADRVMSVC
     LRVELYGCLW KDGLLSYTAP VGQTMYLSEA VHLNDSTYDG HTTHAVGGLL YGGLGQLADG
     VVGLDDFRKS QELRVWPGYD YVGWSNHSFP AGYVEMEFEF DRLRVFQAMQ VHCNNMHTLG
     ARLPGGVECR FKRGPAMAWE GEPVRHALGG SLGDPRARAV SVPLGGRVGR FLQCRFLFAG
     PWLLFSEISF ISDVMNDSSP ALGGTFPPAP WWPPGPPPTN FSSLELEPRG QQPVAKAEGS
     PTAILIGCLV AIILLLLLII ALMLWRLHWR RLLSKAERRV LEEELTVHLS VPGDTILINN
     RPGPLEPPPY QEPRPRGNPP HSAPSVPNSS ALLLSNPAYR LLLATYARPP RGPGPPTPAW
     AKPTNTQACS GDYMEPEKPG APLLPPPPQN SVPHYAEADI VTLQGVTGGN TYAVPALPPG
     AAGDGPPRVD FPRSQLRFKE KLGEGQFGEV HLCEVENPQD LVSLDFPLNV CKGHPLLVAV
     KILRPDATKN ARNDFLKEVK IMSRLKDPNI IRLLGVCVQD DPLCMITDYM ENGDLNQFLS
     AHQLEDKVAE GAPRDGEAAP GPTISYPMLL HVVAQIASGM RYLATLNFVH RDLATRNCLV
     GENFTIKIAD FGMSRNLYAG DYYRVQGRAV LPIRWMAWEC ILMGKFTTAS DVWAFGVTLW
     EVLMLCRAQP FGQLTDEQVI ENAGEFFRDQ GRQVYLSRPP ACPLGLYELM LRCWSREPEQ
     RPPFSQLHRF LAEDALNTV
//
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