ID RET_MOUSE STANDARD; PRT; 1115 AA. AC P35546; Q8BQ34; Q9QXH9; DT 01-JUN-1994 (Rel. 29, Created) DT 25-OCT-2004 (Rel. 45, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE Proto-oncogene tyrosine-protein kinase receptor ret precursor DE (EC 2.7.1.112) (C-ret). GN Name=Ret; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). 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 NUCLEOTIDE SEQUENCE (ISOFORM 1). RC STRAIN=A; RA Phua C.Y.D., Too H.P.; RT "Molecular characterization of mouse neuro-2a c-ret proto-oncogene."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 2). RC STRAIN=BALB/c; RA Wang Y.-Z., Yoong L.-F., Too H.-P.; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion; RX MEDLINE=22354683; PubMed=12466851; DOI=10.1038/nature01266; RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S., RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H., RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T., RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W., RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S., RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S., RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J., RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D., RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L., RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A., RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H., RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G., RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S., RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M., RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K., RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N., RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K., RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S., RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I., RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A., RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J., RA Birney E., Hayashizaki Y.; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6; TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP INTERACTIONS WITH DOK2; DOK4 AND DOK5, PHOSPHORYLATION, AND RP MUTAGENESIS OF TYR-1063. RX MEDLINE=21363571; PubMed=11470823; DOI=10.1083/jcb.200102032; 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 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 + a 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P35546-1; Sequence=Displayed; CC Name=2; Synonyms=Ret9; CC IsoId=P35546-2; Sequence=VSP_011304; CC -!- TISSUE SPECIFICITY: Expressed in peripheral nerve cells and CC hematopoietic cells. CC -!- PTM: Phosphorylated. CC -!- SIMILARITY: Belongs to the Tyr protein kinase family. 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; -; mRNA. DR EMBL; AF209436; AAF21033.1; -; mRNA. DR EMBL; AY326397; AAP88379.1; -; mRNA. DR EMBL; AK051633; BAC34699.1; -; mRNA. DR EMBL; BC059012; AAH59012.1; -; mRNA. DR PIR; I48735; S29926. DR PDB; 1UEF; X-ray; C/D=1055-1067. DR Ensembl; ENSMUSG00000030110; Mus musculus. DR MGI; MGI:97902; Ret. DR GO; GO:0005615; C:extracellular space; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kin...; TAS. DR GO; GO:0001838; P:embryonic epithelial tube formation; IDA. DR GO; GO:0000165; P:MAPKKK cascade; IGI. DR GO; GO:0009653; P:morphogenesis; TAS. DR GO; GO:0007399; P:neurogenesis; IMP. 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 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 3D-structure; Alternative splicing; ATP-binding; Glycoprotein; Kinase; KW Nucleotide-binding; Phosphorylation; Proto-oncogene; Signal; KW Transferase; Transmembrane; Tyrosine-protein kinase. FT SIGNAL 1 28 Potential. FT CHAIN 29 1115 Proto-oncogene tyrosine-protein kinase FT receptor ret. FT TOPO_DOM 29 637 Extracellular (Potential). FT TRANSMEM 638 659 Potential. FT TOPO_DOM 660 1115 Cytoplasmic (Potential). FT DOMAIN 168 273 Cadherin. FT DOMAIN 725 1017 Protein kinase. FT NP_BIND 731 739 ATP (By similarity). FT ACT_SITE 875 875 Proton acceptor (By similarity). FT BINDING 759 759 ATP (By similarity). FT MOD_RES 807 807 Phosphotyrosine (by autocatalysis) (By FT similarity). FT MOD_RES 810 810 Phosphotyrosine (by autocatalysis) (By FT similarity). FT MOD_RES 901 901 Phosphotyrosine (by autocatalysis) (By FT similarity). FT MOD_RES 906 906 Phosphotyrosine (by autocatalysis) (By FT similarity). FT MOD_RES 982 982 Phosphotyrosine (by autocatalysis) (By FT similarity). FT MOD_RES 1016 1016 Phosphotyrosine (by autocatalysis) (By FT similarity). FT MOD_RES 1063 1063 Phosphotyrosine (by autocatalysis). FT MOD_RES 1091 1091 Phosphotyrosine (by autocatalysis) (By FT similarity). FT MOD_RES 1097 1097 Phosphotyrosine (by autocatalysis) (By FT similarity). 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 VARSPLIC 1065 1115 MSDPNWPGESPVPLTRADGTSTGFPRYANDSVYANWMVSPS FT AAKLMDTFDS -> RISHAFTRF (in isoform 2). FT /FTId=VSP_011304. FT MUTAGEN 1063 1063 Y->F: Abolishes interaction with DOK FT proteins. FT CONFLICT 174 174 F -> S (in Ref. 1). SQ SEQUENCE 1115 AA; 123874 MW; A5CF1EF45A640413 CRC64; MAKATSGAAG LGLKLILLLP LLGEAPLGLY FSRDAYWERL YVDQPAGTPL LYVHALRDAP GEVPSFRLGQ HLYGVYRTRL HENDWIRINE TTGLLYLNQS LDHSSWEQLS IRNGGFPLLT IFLQVFLGST AQREGECHWP GCTRVYFSFI NDTFPNCSSF KAQDLCIPET AVSFRVRENR 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 KATAFRLKGR AGYTTVAVKM 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 //