7LESS_DROVI
ID 7LESS_DROVI Reviewed; 2594 AA.
AC P20806;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein sevenless;
DE EC=2.7.10.1;
GN Name=sev;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2115169; DOI=10.1073/pnas.87.14.5351;
RA Michael W.M., Bowtell D.D.L., Rubin G.M.;
RT "Comparison of the sevenless genes of Drosophila virilis and Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5351-5353(1990).
CC -!- FUNCTION: Receptor for an extracellular signal required to instruct a
CC cell to differentiate into a R7 photoreceptor. The ligand for Sev is
CC the Boss (Bride of Sevenless) protein.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: It is unclear whether the potential membrane spanning region
CC near the N-terminus is present as a transmembrane domain in the native
CC protein or serves as a cleaved signal sequence.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; M34545; AAA28883.1; -; Genomic_DNA.
DR EMBL; M34544; AAA28883.1; JOINED; Genomic_DNA.
DR EMBL; M34543; AAA28883.1; JOINED; Genomic_DNA.
DR PIR; A35774; A35774.
DR AlphaFoldDB; P20806; -.
DR SMR; P20806; -.
DR STRING; 7244.FBpp0230353; -.
DR PRIDE; P20806; -.
DR eggNOG; KOG1095; Eukaryota.
DR BRENDA; 2.7.10.1; 2005.
DR ChiTaRS; sev; fly.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:EnsemblMetazoa.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008288; F:boss receptor activity; IEA:EnsemblMetazoa.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0045500; P:sevenless signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.120.10.30; -; 2.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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 Pfam; PF00041; fn3; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 7.
DR SMART; SM00135; LY; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; SSF49265; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 8.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Sensory transduction;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
KW Vision.
FT CHAIN 1..2594
FT /note="Protein sevenless"
FT /id="PRO_0000058929"
FT TOPO_DOM 1..2141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2142..2162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2163..2594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 358..462
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 468..560
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 838..938
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 1024..1066
FT /note="LDL-receptor class B"
FT DOMAIN 1227..1317
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1324..1430
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1711..1814
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1821..1920
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1922..2010
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2014..2132
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2224..2495
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2543..2568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2355
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 2230..2238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2391
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2594 AA; 289133 MW; 77D8A356CBAD0BBD CRC64;
MFWREDAAQQ QQQQQQQQQQ QQQQQQPPHP PKRLSFSFNV KIAVNVNTKM STTHINQERS
KQQTTTGSRS RSRSNSNSSV SCKGDGDRRV RRHTTRLVGL RQQLLHLGRQ LNPGQFLVTG
HGGISTILIA NLLLLLLLSL CCNVCCRSHI EPDQNLTPTT TSPAAVAVVP MLLPLAQTHM
RPQLDSDVVE KVAVWTKHVG AAPPSIAEGI AISSVVRMPP SIQTPTETVR RQEQQRQQQQ
QQQEAAAAAA ADAAIDERIV LERVTRDCVQ RCIVEEDLFL DEFGIKCEKA DNSDKCYKTR
CNKGCAQWYR ALKEIEPCQE ACASTQFYPY DMPCIGACET AQRDYWHMQR LAMARLVETT
QPQLLEMTDE SSTLTIKWAM QFPENYLASR PFNIQYQQVD NQSEPEWHNL ADYDCDEYYV
CEILEALVPY TRYKFRFELP FGESSEDVLY SPATPVYETP MEGAPISAPI IVALLALDEH
HVFVHWRPGR YSNAPIEGYR VLLTSAGNTS REQLLPAQRT SCIFAQLQPL TNYTVALTMI
NKQGEGPSTV VSIVTKSPLE PQQLQSVLLA SEHSIIWQSL EPAGETRLLY TSEPAAISDF
TFSQREQRLW LLDELGQLHS QLLDETTTSA ARRLRLELPS NGSSQWTPRK LSLDWLQRRL
YIAAQANSSD GAEGGFELFS SNLEGGDVQM AGVQLGLVVE QLELDALNGW LFWCDADSLW
RLDLSSKQQL RLTQPAGAPG RFMLEPQRWL LHVLLPQENQ LLELSYDGGH KHALALSNDS
WRGFAWSSDQ AQLLLANETQ LQLLDGQTLV PLANWSPDGG CCALLPLERR RQPLSLEPPA
PRELRALLGA QGAHITWQPP AANPYQTATA AARNFSYELE VLDVASQSAY NIRNIRVPHF
GLERLQADNL YQLRVRANNA AGRAGVWTAP LATRTWPLGD HRLRWATQRG SLYTTNELGG
QLQPLPVQLA SSPGPLALVN ASVAYYVSGR EQSLHCVNLL QPQLSCTDER LEHVGAVAYD
WRGGLLYWTD LARDCVQRLD PFSGERELLP IFGARHLALD SAQGHLYYSS SAHLARRSLS
ALSTHQPELE YYHVNGLAGQ ISGFCLDLPQ RHIYWLVAGN SALHLYRTAL SAGGSQAAVP
LQLLTTLPAA DALPHTLQHL APLGALLWLA ADGRGAHLLR LAAQLETDTD TMRLLPEGLV
EPLSAVQLLE RSAGPPPPPP DEGVRPLAVP PDSVHIDEGG HWNDFRVRWQ PAASGGNHSV
CYKLLLEHGS ERLITLELLT PFARITQLAQ APLGLRISIT PHTAWRAGST TRVQLDTPVA
APTQPRRLRV FVERQAAPLQ LAPNVSALLR WDVPEEHAGS QSLQYRISCW RGSELHSELL
LNQSTLEARV EHLQPEETYR FQVQAHVAAT GLAAGATSHA LHVSPEVQSV PRLLYANAEH
IGELDLDTGH RKQLVHTASP VEHLVVLQGE QRLLWVNEHV ELLSHVPGKA PAKLARMRAE
VLALTVDWVQ RIVYWAELDA ADGGCVIYSL DLCRFDGRIL QGERLWSTPR GQLLRDLVAL
PHARQLVWLQ HDLDSRNATL QGRSLANGSA LTFEGVTLPL WRLFEGSQEP LAETLNLVDH
LGRLCVYHVA RQLCTSSALR AQLNLLNDDI GQLAQDPGYL YALRNGSVRA YGRRRQQLEF
LLELQPDEVR LLRAYNYQAY PSRRCLLLPT TAAALESTPS SCEETQCSLQ LPALSAAPDC
PLPVPGLNYQ LNLSSSSRSA QLELRSLHSA AGLTLNISQL QPYQAYELRA QVGSYYQQQL
GQEPLQLPVL TLHTAAATPS APRNFSGRAL SPSELELSWL APLELRSASV YYTLHWQLQL
EDTEEQSQEQ PAQEQRVETA GVQRLTGLQP ARLYQVWLQA HATPSKYNSS GRLLIRSYAP
LPPLQLIELN AYGMTLAWPG TPDALSSLTL ECQSLREQLQ FNVAGNHTQM RLAPLQPKTR
YSCRLALAYA ATPGAPIYFG PSHEYETLGD APSAPGRPQL EHIAGEIFRV SWTPALDNGS
PILLYNLEAL QARRTNRRRR RRRETTLSLL PWAEEPLVIE DQWLDFCNTT ELSCIVRELH
TRRLLLFRVR ARNRPHGWGP YSEDSERIAE PFVSPEKRGS LVLAIIAPAA IVSSCVLALV
LVRKLQKRRH RAKKLLQQSR PSIWSNLSAL QTQQQLLAAR SRTFSMSLSD ADIALLPQIN
WNRLTLLRFL GSGAFGEVYE GQLQAEDEAQ PQRVAIKSLR KGASEFAELL QEAQLMSNFK
HENIVCLIGI CCDTDSISLI MEHMEAGDLL SYLRAARPSS QEALSKLQLP ELLSMCLDVA
NGCSYMEDMH FVHRDLACRN CLVSDGAAIG GRRIVKIGDF GLARDIYKSD YYRKEGEGLL
PVRWMALESL VDGLFSTQSD VWAFGVLCWE IFTLGQQPYA ARNNFEVLAH VKEGGRLQQP
ERCPEKLYAL LLQCWRSEPW ERPSFKRCLS TLQALSSDLR RTEMLATDET PLVSALCAFK
PDAKVRFDDA PQRLTLHLDA KDTVSTTDAD TTGSPTTPTA PTTPTTTTST IAVVSTAPSS
ENGQLYANEG ISGL
