ID RET_MOUSE STANDARD; PRT; 1115 AA. AC P35546; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Proto-oncogene tyrosine-protein kinase receptor ret precursor DE (EC 2.7.1.112) (C-ret). GN RET. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93205390; PubMed=8455936; RA Iwamoto T., Taniguchi M., Asai N., Ohkusu K., Nakashima I., RA Takahashi M.; RT "cDNA cloning of mouse ret proto-oncogene and its sequence similarity RT to the cadherin superfamily."; RL Oncogene 8:1087-1091(1993). RN [2] RP INTERACTION WITH DOK2; DOK4 AND DOK5, PHOSPHORYLATION, AND MUTAGENESIS RP OF TYR-1063. RX MEDLINE=21363571; PubMed=11470823; RA Grimm J., Sachs M., Britsch S., Di Cesare S., Schwarz-Romond T., RA Alitalo K., Birchmeier W.; RT "Novel p62dok family members, dok-4 and dok-5, are substrates of the RT c-Ret receptor tyrosine kinase and mediate neuronal RT differentiation."; RL J. Cell Biol. 154:345-354(2001). CC -!- FUNCTION: Probable receptor with tyrosine-protein kinase activity; CC important for development. CC -!- CATALYTIC ACTIVITY: ATP + a protein tyrosine = ADP + protein CC tyrosine phosphate. CC -!- SUBUNIT: Phosphorylated form interacts with the PBT domain of CC DOK2, DOK4 and DOK5. CC -!- SUBCELLULAR LOCATION: Type I membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in peripheral nerve cells and CC hematopoietic cells. CC -!- PTM: Phosphorylated. CC -!- SIMILARITY: Belongs to the Tyr family of protein kinases. CC -!- SIMILARITY: Contains 1 cadherin domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X67812; CAA48013.1; -. DR PIR; I48735; S29926. DR HSSP; P11362; 1FGK. DR MGD; MGI:97902; Ret. DR GO; GO:0001657; P:ureteric bud development; IMP. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00028; Cadherin; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00112; CA; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50268; CADHERIN_2; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. KW Transferase; Tyrosine-protein kinase; ATP-binding; Proto-oncogene; KW Transmembrane; Phosphorylation; Glycoprotein; Signal. FT SIGNAL 1 28 Potential. FT CHAIN 29 1115 Proto-oncogene tyrosine-protein kinase FT receptor ret. FT DOMAIN 29 637 Extracellular (Potential). FT TRANSMEM 638 659 Potential. FT DOMAIN 660 1115 Cytoplasmic (Potential). FT DOMAIN 168 273 Cadherin. FT DOMAIN 725 1017 Protein kinase. FT NP_BIND 731 739 ATP (By similarity). FT BINDING 759 759 ATP (By similarity). FT ACT_SITE 875 875 Proton acceptor (By similarity). FT MOD_RES 1063 1063 Phosphotyrosine. FT CARBOHYD 89 89 N-linked (GlcNAc...) (Potential). FT CARBOHYD 98 98 N-linked (GlcNAc...) (Potential). FT CARBOHYD 151 151 N-linked (GlcNAc...) (Potential). FT CARBOHYD 156 156 N-linked (GlcNAc...) (Potential). FT CARBOHYD 199 199 N-linked (GlcNAc...) (Potential). FT CARBOHYD 345 345 N-linked (GlcNAc...) (Potential). FT CARBOHYD 360 360 N-linked (GlcNAc...) (Potential). FT CARBOHYD 378 378 N-linked (GlcNAc...) (Potential). FT CARBOHYD 396 396 N-linked (GlcNAc...) (Potential). FT CARBOHYD 450 450 N-linked (GlcNAc...) (Potential). FT CARBOHYD 470 470 N-linked (GlcNAc...) (Potential). FT CARBOHYD 556 556 N-linked (GlcNAc...) (Potential). FT MUTAGEN 1063 1063 Y->F: Abolishes interaction with DOK FT proteins. SQ SEQUENCE 1115 AA; 123728 MW; 4D75576095C7D2C8 CRC64; MAKATSGAAG LGLKLILLLP LLGEAPLGLY FSRDAYWERL YVDQPAGTPL LYVHALRDAP GEVPSFRLGQ HLYGVYRTRL HENDWIRINE TTGLLYLNQS LDHSSWEQLS IRNGGFPLLT IFLQVFLGST AQREGECHWP GCTRVYFSFI NDTFPNCSSF KAQDLCIPET AVSSRVRENX PPGTFYHFHM LPVQFLCPNI SVKYSLLGGD SLPFRCDPDC LEVSTRWALD RELREKYVLE ALCIVAGPGA NKETVTLSFP VTVYDEDDSA PTFSGGVGTA SAVVEFKRKE GTVVATLQVF DADVVPASGE LVRRYTNTLL SGDSWAQQTF RVEHSPIETL VQVNNNSVRA TMHNYKLILN RSLSISESRV LQLAVLVNDS DFQGPGAGGI LVLHFNVSVL PVTLNLPRAY SFPVNKRARR YAQIGKVCVE NCQEFSGVSI QYKLQPSSIN CTALGVVTSP EDTSGTLFVN DTEALRRPEC TKLQYTVVAT DRQTRRQTQA SLVVTVEGTS ITEEVGCPKS CAVNKRRPEC EECGGLGSPT GRCEWRQGDG KGITRNFSTC SPSTRTCPDG HCDAVESRDA NICPQDCLRA DIVGGHERGE RQGIKAGYGI CNCFPDEKKC FCEPEDSQGP LCDALCRTII TAALFSLIIS ILLSIFCVCH HHKHGHKPPI ASAEMTFCRP AQGFPISYSS SGTRRPSLDS TENQVPVDSF KIPEDPKWEF PRKNLVLGKT LGEGEFGKVV XATAFRLKGR AGYTTVAVKX LKENASQSEL RDLLSEFNLL KQVNHPHVIK LYGACSQDGP LLLIVEYAKY GSLRGFLRDS RKIGPAYVSG GGSRNSSSLD HPDERVLTMG DLISFAWQIS RGMQYLAEMK LVHRDLAARN ILVAEGRKMK ISDFGLSRDV YEEDSYVKKS KGRIPVKWMA IESLFDHIYT TQSDVWSFGV LLWEIVTLGG NPYPGIPPER LFNLLKTGHR MERPDNCSEE MYRLMLQCWK QEPDKRPVFA DISKDLEKMM VKSRDYLDLA ASTPSDSLLY DDGLSEEETP LVDCNNAPLP RSLPSTWIEN KLYGMSDPNW PGESPVPLTR ADGTSTGFPR YANDSVYANW MVSPSAAKLM DTFDS //