ID 7LESS_DROME Reviewed; 2554 AA. AC P13368; Q9TYI0; Q9U5V7; Q9VZ36; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 16-DEC-2008, entry version 99. DE RecName: Full=Protein sevenless; DE EC=2.7.10.1; GN Name=sev; Synonyms=HD-265; ORFNames=CG18085; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF RP LYS-2242. RC STRAIN=Canton-S; RX MEDLINE=88282538; PubMed=2840202; DOI=10.1016/0092-8674(88)90193-6; RA Basler K., Hafen E.; RT "Control of photoreceptor cell fate by the sevenless protein requires RT a functional tyrosine kinase domain."; RL Cell 54:299-311(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Oregon-R; RX MEDLINE=88329706; PubMed=3138161; RA Bowtell D.L.L., Simon M.A., Rubin G.M.; RT "Nucleotide sequence and structure of the sevenless gene of Drosophila RT melanogaster."; RL Genes Dev. 2:620-634(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2349-2408. RX MEDLINE=98401146; PubMed=9731193; DOI=10.1006/bbrc.1998.9003; RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.; RT "Sampling the genomic pool of protein tyrosine kinase genes using the RT polymerase chain reaction with genomic DNA."; RL Biochem. Biophys. Res. Commun. 249:660-667(1998). RN [6] RP IDENTIFICATION OF FN-III REPEATS. RX MEDLINE=90199889; PubMed=2317871; DOI=10.1016/0092-8674(90)90209-W; RA Norton P.A., Hynes R.O., Ress D.J.G.; RT "Sevenless: seven found?"; RL Cell 61:15-16(1990). RN [7] RP INTERACTION WITH DAB. RX MEDLINE=98336289; PubMed=9671493; RA Le N., Simon M.A.; RT "Disabled is a putative adaptor protein that functions during RT signaling by the sevenless receptor tyrosine kinase."; RL Mol. Cell. Biol. 18:4844-4854(1998). CC -!- FUNCTION: Receptor for an extracellular signal required to CC instruct a cell to differentiate into an R7 photoreceptor. The CC ligand for sev is the boss (bride of sevenless) protein on the CC surface of the neighboring R8 cell. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- SUBUNIT: May form a complex with drk and Sos. Binds the CC phosphotyrosine interaction domain (PID) of Dab. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein CC (Potential). CC -!- DOMAIN: It is unclear whether the potential membrane spanning CC region near the N-terminus is present as a transmembrane domain in CC the native protein or serves as a cleaved signal sequence. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Insulin receptor subfamily. CC -!- SIMILARITY: Contains 7 fibronectin type-III domains. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J03158; AAA28882.1; -; Genomic_DNA. DR EMBL; X13666; CAA31960.1; ALT_INIT; mRNA. DR EMBL; X13666; CAB55310.1; -; mRNA. DR EMBL; AE014298; AAF47992.2; -; Genomic_DNA. DR EMBL; AJ002917; CAA05752.1; -; Genomic_DNA. DR PIR; A28912; TVFF7L. DR RefSeq; NP_511114.2; -. DR UniGene; Dm.2618; -. DR HSSP; P08069; 1JQH. DR IntAct; P13368; 5. DR Ensembl; CG18085; Drosophila melanogaster. DR GeneID; 32039; -. DR KEGG; dme:Dmel_CG18085; -. DR FlyBase; FBgn0003366; sev. DR HOGENOM; P13368; -. DR NextBio; 776500; -. DR ArrayExpress; P13368; -. DR GermOnline; CG18085; Drosophila melanogaster. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kin...; IEA:InterPro. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; TAS:FlyBase. DR GO; GO:0046534; P:positive regulation of photoreceptor cell d...; IMP:FlyBase. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR GO; GO:0045467; P:R7 cell development; NAS:FlyBase. DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0008293; P:torso signaling pathway; NAS:FlyBase. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR008957; Fibronectin_typ-III-like_fold. DR InterPro; IPR003961; FN_III. DR InterPro; IPR000033; LDLR. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_bd_CS. DR InterPro; IPR002011; Recept_tyr_kinase-II_CS. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1. DR Gene3D; G3DSA:2.60.40.30; FN_III-like; 3. DR Pfam; PF00041; fn3; 6. DR Pfam; PF07714; Pkinase_Tyr; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00060; FN3; 7. DR SMART; SM00135; LY; 2. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50853; FN3; 7. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Kinase; KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Repeat; KW Sensory transduction; Transferase; Transmembrane; KW Tyrosine-protein kinase; Vision. FT CHAIN 1 2554 Protein sevenless. FT /FTId=PRO_0000058928. FT TOPO_DOM 1 2123 Extracellular (Potential). FT TRANSMEM 2124 2147 Potential. FT TOPO_DOM 2148 2554 Cytoplasmic (Potential). FT DOMAIN 311 431 Fibronectin type-III 1. FT DOMAIN 436 528 Fibronectin type-III 2. FT DOMAIN 822 921 Fibronectin type-III 3. FT DOMAIN 1298 1392 Fibronectin type-III 4. FT DOMAIN 1680 1794 Fibronectin type-III 5. FT DOMAIN 1797 1897 Fibronectin type-III 6. FT DOMAIN 1898 1988 Fibronectin type-III 7. FT DOMAIN 2209 2485 Protein kinase. FT NP_BIND 2215 2223 ATP (By similarity). FT COMPBIAS 2038 2046 Poly-Arg. FT ACT_SITE 2343 2343 Proton acceptor (By similarity). FT BINDING 2242 2242 ATP (By similarity). FT MOD_RES 2380 2380 Phosphotyrosine; by autocatalysis (By FT similarity). FT CARBOHYD 30 30 N-linked (GlcNAc...) (Potential). FT CARBOHYD 129 129 N-linked (GlcNAc...) (Potential). FT CARBOHYD 481 481 N-linked (GlcNAc...) (Potential). FT CARBOHYD 505 505 N-linked (GlcNAc...) (Potential). FT CARBOHYD 617 617 N-linked (GlcNAc...) (Potential). FT CARBOHYD 647 647 N-linked (GlcNAc...) (Potential). FT CARBOHYD 966 966 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1228 1228 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1313 1313 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1353 1353 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1550 1550 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1557 1557 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1639 1639 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1725 1725 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1756 1756 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1804 1804 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1889 1889 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1947 1947 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2073 2073 N-linked (GlcNAc...) (Potential). FT MUTAGEN 2242 2242 K->M: Inactivates the protein. FT CONFLICT 392 392 V -> M (in Ref. 1; AAA28882). FT CONFLICT 663 663 A -> T (in Ref. 3; AAF47992). FT CONFLICT 1703 1703 N -> H (in Ref. 3; AAF47992). FT CONFLICT 1730 1731 RG -> KE (in Ref. 3; AAF47992). FT CONFLICT 1741 1741 V -> M (in Ref. 3; AAF47992). FT CONFLICT 1823 1823 E -> Q (in Ref. 2; CAA31960/CAB55310). FT CONFLICT 2271 2271 C -> R (in Ref. 1; AAA28882). SQ SEQUENCE 2554 AA; 287025 MW; 09E238A0F27684F8 CRC64; MTMFWQQNVD HQSDEQDKQA KGAAPTKRLN ISFNVKIAVN VNTKMTTTHI NQQAPGTSSS SSNSQNASPS KIVVRQQSSS FDLRQQLARL GRQLASGQDG HGGISTILII NLLLLILLSI CCDVCRSHNY TVHQSPEPVS KDQMRLLRPK LDSDVVEKVA IWHKHAAAAP PSIVEGIAIS SRPQSTMAHH PDDRDRDRDP SEEQHGVDER MVLERVTRDC VQRCIVEEDL FLDEFGIQCE KADNGEKCYK TRCTKGCAQW YRALKELESC QEACLSLQFY PYDMPCIGAC EMAQRDYWHL QRLAISHLVE RTQPQLERAP RADGQSTPLT IRWAMHFPEH YLASRPFNIQ YQFVDHHGEE LDLEQEDQDA SGETGSSAWF NLADYDCDEY YVCEILEALI PYTQYRFRFE LPFGENRDEV LYSPATPAYQ TPPEGAPISA PVIEHLMGLD DSHLAVHWHP GRFTNGPIEG YRLRLSSSEG NATSEQLVPA GRGSYIFSQL QAGTNYTLAL SMINKQGEGP VAKGFVQTHS ARNEKPAKDL TESVLLVGRR AVMWQSLEPA GENSMIYQSQ EELADIAWSK REQQLWLLNV HGELRSLKFE SGQMVSPAQQ LKLDLGNISS GRWVPRRLSF DWLHHRLYFA MESPERNQSS FQIISTDLLG ESAQKVGESF DLPVEQLEVD ALNGWIFWRN EESLWRQDLH GRMIHRLLRI RQPGWFLVQP QHFIIHLMLP QEGKFLEISY DGGFKHPLPL PPPSNGAGNG PASSHWQSFA LLGRSLLLPD SGQLILVEQQ GQAASPSASW PLKNLPDCWA VILLVPESQP LTSAGGKPHS LKALLGAQAA KISWKEPERN PYQSADAARS WSYELEVLDV ASQSAFSIRN IRGPIFGLQR LQPDNLYQLR VRAINVDGEP GEWTEPLAAR TWPLGPHRLR WASRQGSVIH TNELGEGLEV QQEQLERLPG PMTMVNESVG YYVTGDGLLH CINLVHSQWG CPISEPLQHV GSVTYDWRGG RVYWTDLARN CVVRMDPWSG SRELLPVFEA NFLALDPRQG HLYYATSSQL SRHGSTPDEA VTYYRVNGLE GSIASFVLDT QQDQLFWLVK GSGALRLYRA PLTAGGDSLQ MIQQIKGVFQ AVPDSLQLLR PLGALLWLER SGRRARLVRL AAPLDVMELP TPDQASPASA LQLLDPQPLP PRDEGVIPMT VLPDSVRLDD GHWDDFHVRW QPSTSGGNHS VSYRLLLEFG QRLQTLDLST PFARLTQLPQ AQLQLKISIT PRTAWRSGDT TRVQLTTPPV APSQPRRLRV FVERLATALQ EANVSAVLRW DAPEQGQEAP MQALEYHISC WVGSELHEEL RLNQSALEAR VEHLQPDQTY HFQVEARVAA TGAAAGAASH ALHVAPEVQA VPRVLYANAE FIGELDLDTR NRRRLVHTAS PVEHLVGIEG EQRLLWVNEH VELLTHVPGS APAKLARMRA EVLALAVDWI QRIVYWAELD ATAPQAAIIY RLDLCNFEGK ILQGERVWST PRGRLLKDLV ALPQAQSLIW LEYEQGSPRN GSLRGRNLTD GSELEWATVQ PLIRLHAGSL EPGSETLNLV DNQGKLCVYD VARQLCTASA LRAQLNLLGE DSIAGQLAQD SGYLYAVKNW SIRAYGRRRQ QLEYTVELEP EEVRLLQAHN YQAYPPKNCL LLPSSGGSLL KATDCEEQRC LLNLPMITAS EDCPLPIPGV RYQLNLTLAR GPGSEEHDHG VEPLGQWLLG AGESLNLTDL LPFTRYRVSG ILSSFYQKKL ALPTLVLAPL ELLTASATPS PPRNFSVRVL SPRELEVSWL PPEQLRSESV YYTLHWQQEL DGENVQDRRE WEAHERRLET AGTHRLTGIK PGSGYSLWVQ AHATPTKSNS SERLHVRSFA ELPELQLLEL GPYSLSLTWA GTPDPLGSLQ LECRSSAEQL RRNVAGNHTK MVVEPLQPRT RYQCRLLLGY AATPGAPLYH GTAEVYETLG DAPSQPGKPQ LEHIAEEVFR VTWTAARGNG APIALYNLEA LQARSDIRRR RRRRRRNSGG SLEQLPWAEE PVVVEDQWLD FCNTTELSCI VKSLHSSRLL LFRVRARSLE HGWGPYSEES ERVAEPFVSP EKRGSLVLAI IAPAAIVSSC VLALVLVRKV QKRRLRAKKL LQQSRPSIWS NLSTLQTQQQ LMAVRNRAFS TTLSDADIAL LPQINWSQLK LLRFLGSGAF GEVYEGQLKT EDSEEPQRVA IKSLRKGASE FAELLQEAQL MSNFKHENIV CLVGICFDTE SISLIMEHME AGDLLSYLRA ARATSTQEPQ PTAGLSLSEL LAMCIDVANG CSYLEDMHFV HRDLACRNCL VTESTGSTDR RRTVKIGDFG LARDIYKSDY YRKEGEGLLP VRWMSPESLV DGLFTTQSDV WAFGVLCWEI LTLGQQPYAA RNNFEVLAHV KEGGRLQQPP MCTEKLYSLL LLCWRTDPWE RPSFRRCYNT LHAISTDLRR TQMASATADT VVSCSRPEFK VRFDGQPLEE HREHNERPED ENLTLREVPL KDKQLYANEG VSRL //