ID H2MJU7_ORYLA Unreviewed; 861 AA.
AC H2MJU7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Discoidin domain receptor tyrosine kinase 2 {ECO:0000313|Ensembl:ENSORLP00000018947.2};
GN Name=DDR2 {ECO:0000313|Ensembl:ENSORLP00000018947.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000018947.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000018947.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018947.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000018947.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018947.2};
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 STRING; 8090.ENSORLP00000038179; -.
DR Ensembl; ENSORLT00000018948.2; ENSORLP00000018947.2; ENSORLG00000015116.2.
DR Ensembl; ENSORLT00000046856.1; ENSORLP00000038179.1; ENSORLG00000015116.2.
DR eggNOG; KOG1094; Eukaryota.
DR GeneTree; ENSGT00940000154842; -.
DR HOGENOM; CLU_008873_2_0_1; -.
DR OrthoDB; 2999496at2759; -.
DR TreeFam; TF317840; -.
DR Proteomes; UP000001038; Chromosome 4.
DR Bgee; ENSORLG00000015116; Expressed in muscle tissue and 7 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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:SF295; DISCOIDIN DOMAIN-CONTAINING RECEPTOR 2; 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:UP000001038};
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..861
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041117504"
FT TRANSMEM 401..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..185
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 568..856
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 496..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 98039 MW; 84B14F960ED1D5FF CRC64;
MKKLSESLLH LLSCFHLLAA VTSQVNPDVC RYPLGMSGGQ IRDEDISASS QWSESTAARH
GRLDCEEGDG AWCPETTVEP DNLKEFIQID LNLLHFITLV GTQGRHAGGM GNEFAQMYMI
KYSRDGSRWI SWRNRQGKQV IEGNRNTYDT VLRDLDPPII ARFVRFMPVT DHSMNVCMRV
ELYGCKWLDG LVSYNAPAGE QMKLPAFPVF FNDSVYDGAI THMMTEGLGQ LSDGVMGLDD
FTQSHVYQAW PGYDYVGWNN ESFPSGFVEI MFEFDRPRNF TTMKVHCNNM FSQHIKIFRQ
VVCYFRSDSD WESTVLSFSP VVDENDPSAR FITVELTNRM ANAIKCQFYF KDAWMLFSEI
TFQSDRAMYN TTLVPPTIGP PTNTPPEDDP THKIDDSNTR ILIGCLVAII FILLAIIIII
LWRQVWQKLM EKASRRMLDD ELTASLSIQT EVFGHNHSQS RVTNEQESNA AYERIFPLGP
DYQEPSRLIN KLPEFAQSSE EPASTSTASS KSTTTTALVQ DGAPHYAEAD IVNLQGVTGS
NTYAIPAVTL DLLSGKDVAV EEFPRKLLTF KEKLGEGQFG EVHLCEAEGM QEFLHEEYLF
DIPEDQPVLV AVKMLRSDAN GNARNDFLKE IKIMSRLKDP NIIRLLAVCI YSNPLCMITE
YMENGDLNQF LSRHEPEGQL ALLSNTATVS FSNLCYMATQ IASGMKYLSS LNFVHRDLAT
RNCLVGKNYT IKIADFGMSR NLYSGDYYRI QGRAVLPIRW MSWESILLGK FTTASDVWAF
GVTLWEILNF CKEQPYSQLT DEQVIENTGE FFRDQKRQIY LPQPVLCSDS LYKIMLTCWR
RNAKERPSFQ EIHRRLSDLE S
//
