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LOCUS NP_001245500 4150 aa linear INV 26-DEC-2023 ACCESSION NP_001245500 VERSION NP_001245500.2 DBLINK BioProject: PRJNA164 BioSample: SAMN02803731 DBSOURCE REFSEQ: accession NM_001258571.3 KEYWORDS RefSeq. SOURCE Drosophila melanogaster (fruit fly) ORGANISM Drosophila melanogaster Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora. REFERENCE 1 (residues 1 to 4150) AUTHORS Matthews,B.B., Dos Santos,G., Crosby,M.A., Emmert,D.B., St Pierre,S.E., Gramates,L.S., Zhou,P., Schroeder,A.J., Falls,K., Strelets,V., Russo,S.M. and Gelbart,W.M. CONSRTM FlyBase Consortium TITLE Gene Model Annotations for Drosophila melanogaster: Impact of High-Throughput Data JOURNAL G3 (Bethesda) 5 (8), 1721-1736 (2015) PUBMED 26109357 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 4150) AUTHORS Crosby,M.A., Gramates,L.S., Dos Santos,G., Matthews,B.B., St Pierre,S.E., Zhou,P., Schroeder,A.J., Falls,K., Emmert,D.B., Russo,S.M. and Gelbart,W.M. CONSRTM FlyBase Consortium TITLE Gene Model Annotations for Drosophila melanogaster: The Rule-Benders JOURNAL G3 (Bethesda) 5 (8), 1737-1749 (2015) PUBMED 26109356 REMARK Publication Status: Online-Only REFERENCE 3 (residues 1 to 4150) AUTHORS Hoskins,R.A., Carlson,J.W., Wan,K.H., Park,S., Mendez,I., Galle,S.E., Booth,B.W., Pfeiffer,B.D., George,R.A., Svirskas,R., Krzywinski,M., Schein,J., Accardo,M.C., Damia,E., Messina,G., Mendez-Lago,M., de Pablos,B., Demakova,O.V., Andreyeva,E.N., Boldyreva,L.V., Marra,M., Carvalho,A.B., Dimitri,P., Villasante,A., Zhimulev,I.F., Rubin,G.M., Karpen,G.H. and Celniker,S.E. TITLE The Release 6 reference sequence of the Drosophila melanogaster genome JOURNAL Genome Res 25 (3), 445-458 (2015) PUBMED 25589440 REFERENCE 4 (residues 1 to 4150) AUTHORS Hoskins,R.A., Carlson,J.W., Kennedy,C., Acevedo,D., Evans-Holm,M., Frise,E., Wan,K.H., Park,S., Mendez-Lago,M., Rossi,F., Villasante,A., Dimitri,P., Karpen,G.H. and Celniker,S.E. TITLE Sequence finishing and mapping of Drosophila melanogaster heterochromatin JOURNAL Science 316 (5831), 1625-1628 (2007) PUBMED 17569867 REFERENCE 5 (residues 1 to 4150) AUTHORS Smith,C.D., Shu,S., Mungall,C.J. and Karpen,G.H. TITLE The Release 5.1 annotation of Drosophila melanogaster heterochromatin JOURNAL Science 316 (5831), 1586-1591 (2007) PUBMED 17569856 REMARK Erratum:[Science. 2007 Sep 7;317(5843):1325] REFERENCE 6 (residues 1 to 4150) AUTHORS Quesneville,H., Bergman,C.M., Andrieu,O., Autard,D., Nouaud,D., Ashburner,M. and Anxolabehere,D. TITLE Combined evidence annotation of transposable elements in genome sequences JOURNAL PLoS Comput Biol 1 (2), 166-175 (2005) PUBMED 16110336 REFERENCE 7 (residues 1 to 4150) AUTHORS Hoskins,R.A., Smith,C.D., Carlson,J.W., Carvalho,A.B., Halpern,A., Kaminker,J.S., Kennedy,C., Mungall,C.J., Sullivan,B.A., Sutton,G.G., Yasuhara,J.C., Wakimoto,B.T., Myers,E.W., Celniker,S.E., Rubin,G.M. and Karpen,G.H. TITLE Heterochromatic sequences in a Drosophila whole-genome shotgun assembly JOURNAL Genome Biol 3 (12), RESEARCH0085 (2002) PUBMED 12537574 REFERENCE 8 (residues 1 to 4150) AUTHORS Kaminker,J.S., Bergman,C.M., Kronmiller,B., Carlson,J., Svirskas,R., Patel,S., Frise,E., Wheeler,D.A., Lewis,S.E., Rubin,G.M., Ashburner,M. and Celniker,S.E. TITLE The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective JOURNAL Genome Biol 3 (12), RESEARCH0084 (2002) PUBMED 12537573 REFERENCE 9 (residues 1 to 4150) AUTHORS Misra,S., Crosby,M.A., Mungall,C.J., Matthews,B.B., Campbell,K.S., Hradecky,P., Huang,Y., Kaminker,J.S., Millburn,G.H., Prochnik,S.E., Smith,C.D., Tupy,J.L., Whitfied,E.J., Bayraktaroglu,L., Berman,B.P., Bettencourt,B.R., Celniker,S.E., de Grey,A.D., Drysdale,R.A., Harris,N.L., Richter,J., Russo,S., Schroeder,A.J., Shu,S.Q., Stapleton,M., Yamada,C., Ashburner,M., Gelbart,W.M., Rubin,G.M. and Lewis,S.E. TITLE Annotation of the Drosophila melanogaster euchromatic genome: a systematic review JOURNAL Genome Biol 3 (12), RESEARCH0083 (2002) PUBMED 12537572 REFERENCE 10 (residues 1 to 4150) AUTHORS Celniker,S.E., Wheeler,D.A., Kronmiller,B., Carlson,J.W., Halpern,A., Patel,S., Adams,M., Champe,M., Dugan,S.P., Frise,E., Hodgson,A., George,R.A., Hoskins,R.A., Laverty,T., Muzny,D.M., Nelson,C.R., Pacleb,J.M., Park,S., Pfeiffer,B.D., Richards,S., Sodergren,E.J., Svirskas,R., Tabor,P.E., Wan,K., Stapleton,M., Sutton,G.G., Venter,C., Weinstock,G., Scherer,S.E., Myers,E.W., Gibbs,R.A. and Rubin,G.M. TITLE Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence JOURNAL Genome Biol 3 (12), RESEARCH0079 (2002) PUBMED 12537568 REFERENCE 11 (residues 1 to 4150) AUTHORS Adams,M.D., Celniker,S.E., Holt,R.A., Evans,C.A., Gocayne,J.D., Amanatides,P.G., Scherer,S.E., Li,P.W., Hoskins,R.A., Galle,R.F., George,R.A., Lewis,S.E., Richards,S., Ashburner,M., Henderson,S.N., Sutton,G.G., Wortman,J.R., Yandell,M.D., Zhang,Q., Chen,L.X., Brandon,R.C., Rogers,Y.H., Blazej,R.G., Champe,M., Pfeiffer,B.D., Wan,K.H., Doyle,C., Baxter,E.G., Helt,G., Nelson,C.R., Gabor,G.L., Abril,J.F., Agbayani,A., An,H.J., Andrews-Pfannkoch,C., Baldwin,D., Ballew,R.M., Basu,A., Baxendale,J., Bayraktaroglu,L., Beasley,E.M., Beeson,K.Y., Benos,P.V., Berman,B.P., Bhandari,D., Bolshakov,S., Borkova,D., Botchan,M.R., Bouck,J., Brokstein,P., Brottier,P., Burtis,K.C., Busam,D.A., Butler,H., Cadieu,E., Center,A., Chandra,I., Cherry,J.M., Cawley,S., Dahlke,C., Davenport,L.B., Davies,P., de Pablos,B., Delcher,A., Deng,Z., Mays,A.D., Dew,I., Dietz,S.M., Dodson,K., Doup,L.E., Downes,M., Dugan-Rocha,S., Dunkov,B.C., Dunn,P., Durbin,K.J., Evangelista,C.C., Ferraz,C., Ferriera,S., Fleischmann,W., Fosler,C., Gabrielian,A.E., Garg,N.S., Gelbart,W.M., Glasser,K., Glodek,A., Gong,F., Gorrell,J.H., Gu,Z., Guan,P., Harris,M., Harris,N.L., Harvey,D., Heiman,T.J., Hernandez,J.R., Houck,J., Hostin,D., Houston,K.A., Howland,T.J., Wei,M.H., Ibegwam,C., Jalali,M., Kalush,F., Karpen,G.H., Ke,Z., Kennison,J.A., Ketchum,K.A., Kimmel,B.E., Kodira,C.D., Kraft,C., Kravitz,S., Kulp,D., Lai,Z., Lasko,P., Lei,Y., Levitsky,A.A., Li,J., Li,Z., Liang,Y., Lin,X., Liu,X., Mattei,B., McIntosh,T.C., McLeod,M.P., McPherson,D., Merkulov,G., Milshina,N.V., Mobarry,C., Morris,J., Moshrefi,A., Mount,S.M., Moy,M., Murphy,B., Murphy,L., Muzny,D.M., Nelson,D.L., Nelson,D.R., Nelson,K.A., Nixon,K., Nusskern,D.R., Pacleb,J.M., Palazzolo,M., Pittman,G.S., Pan,S., Pollard,J., Puri,V., Reese,M.G., Reinert,K., Remington,K., Saunders,R.D., Scheeler,F., Shen,H., Shue,B.C., Siden-Kiamos,I., Simpson,M., Skupski,M.P., Smith,T., Spier,E., Spradling,A.C., Stapleton,M., Strong,R., Sun,E., Svirskas,R., Tector,C., Turner,R., Venter,E., Wang,A.H., Wang,X., Wang,Z.Y., Wassarman,D.A., Weinstock,G.M., Weissenbach,J., Williams,S.M., WoodageT, Worley,K.C., Wu,D., Yang,S., Yao,Q.A., Ye,J., Yeh,R.F., Zaveri,J.S., Zhan,M., Zhang,G., Zhao,Q., Zheng,L., Zheng,X.H., Zhong,F.N., Zhong,W., Zhou,X., Zhu,S., Zhu,X., Smith,H.O., Gibbs,R.A., Myers,E.W., Rubin,G.M. and Venter,J.C. TITLE The genome sequence of Drosophila melanogaster JOURNAL Science 287 (5461), 2185-2195 (2000) PUBMED 10731132 REFERENCE 12 (residues 1 to 4150) AUTHORS Celniker,S., Carlson,J., Wan,K., Pfeiffer,B., Frise,E., George,R., Hoskins,R., Stapleton,M., Pacleb,J., Park,S., Svirskas,R., Smith,E., Yu,C. and Rubin,G. CONSRTM Berkeley Drosophila Genome Project TITLE Drosophila melanogaster release 4 sequence JOURNAL Unpublished REFERENCE 13 (residues 1 to 4150) CONSRTM NCBI Genome Project TITLE Direct Submission JOURNAL Submitted (20-DEC-2023) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA REFERENCE 14 (residues 1 to 4150) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (13-DEC-2023) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 15 (residues 1 to 4150) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (19-OCT-2022) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 16 (residues 1 to 4150) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (20-APR-2020) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 17 (residues 1 to 4150) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (22-APR-2019) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 18 (residues 1 to 4150) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (24-MAY-2018) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 19 (residues 1 to 4150) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (07-DEC-2016) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 20 (residues 1 to 4150) AUTHORS Celniker,S., Carlson,J., Kennedy,C., Wan,K., Frise,E., Hoskins,R., Park,S., Svirskas,R. and Karpen,G. TITLE Direct Submission JOURNAL Submitted (10-AUG-2006) Berkeley Drosophila Genome Project, Lawrence Berkeley National Laboratory, One #Cyclotron RoadOne Cyclotron Road, MS 64-121, Berkeley, CA 94720, USA REMARK Direct Submission REFERENCE 21 (residues 1 to 4150) AUTHORS Celniker,S., Carlson,J., Wan,K., Frise,E., Hoskins,R., Park,S., Svirskas,R. and Rubin,G. TITLE Direct Submission JOURNAL Submitted (10-AUG-2006) Berkeley Drosophila Genome Project, Lawrence Berkeley National Laboratory, One Cyclotron Road, MS 64-121, Berkeley, CA 94720, USA REMARK Direct Submission REFERENCE 22 (residues 1 to 4150) AUTHORS Smith,C.D., Shu,S., Mungall,C.J. and Karpen,G.H. CONSRTM Drosophila Heterochromatin Genome Project TITLE Direct Submission JOURNAL Submitted (01-AUG-2006) Drosophila Heterochromatin Genome Project, Ernest Orlando Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Mailstop 64-121, Berkeley, CA 94720, USA REFERENCE 23 (residues 1 to 4150) AUTHORS Adams,M.D., Celniker,S.E., Gibbs,R.A., Rubin,G.M. and Venter,C.J. TITLE Direct Submission JOURNAL Submitted (21-MAR-2000) Celera Genomics, 45 West Gude Drive, Rockville, MD 20850, USA COMMENT REVIEWED REFSEQ: This record has been curated by FlyBase. The reference sequence is identical to AFH07214. On Jul 15, 2014 this sequence version replaced NP_001245500.1. ##Genome-Annotation-Data-START## Annotation Provider :: FlyBase Annotation Status :: Full annotation Annotation Version :: Release 6.54 URL :: http://flybase.org ##Genome-Annotation-Data-END## Method: conceptual translation. FEATURES Location/Qualifiers source 1..4150 /organism="Drosophila melanogaster" /db_xref="taxon:7227" /chromosome="X" /genotype="y[1]; Gr22b[1] Gr22d[1] cn[1] CG33964[R4.2] bw[1] sp[1]; LysC[1] MstProx[1] GstD5[1] Rh6[1]" Protein 1..4150 /product="terribly reduced optic lobes, isoform AR" /name="CG33950 gene product from transcript CG33950-RAR" /note="CG33950-PAR; trol-PAR; lethal (1) G0271; Trol/perlecan; mRNA-like ncRNA in embryogenesis 7; lethal (1) G0211; lethal (1) G0181; lethal (1) G0412; terribly reduced optic lobes; dPerlecan; lethal (1) G0023; lethal (1) G0374; lethal (1) G0019; lethal (1) G0021" /calculated_mol_wt=459913 Region 407..440 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(412,419,430..431) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(423,426,430,436..437) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 433..437 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 492..524 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(497,505,516..517) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(509,512,516,522..523) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 519..523 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 531..566 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(536,545,556..557) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(549,552,556,562..563) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 559..563 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 576..610 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(581,589,600..601) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(593,596,600,606..607) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 603..607 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 664..699 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(669,678,689..690) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(682,685,689,695..696) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 692..696 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 771..804 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(776,783,794..795) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(787,790,794,800..801) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 797..801 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 832..864 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(837,845,856..857) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(849,852,856,862..863) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 859..863 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 881..914 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(886,893,904..905) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(897,900,904,910..911) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 907..911 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 920..950 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(921,929,940..941) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(933,936,940,946..947) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 943..947 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 951..985 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(956,964,975..976) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(968,971,975,981..982) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 978..982 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 991..1025 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(996,1004,1015..1016) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1008,1011,1015,1021..1022) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1018..1022 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1043..1104 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 1054..1058 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 1068..1071 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 1087..1091 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 1138..1172 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(1143,1151,1162..1163) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1155,1158,1162,1168..1169) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1165..1169 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1178..1212 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(1183,1191,1202..1203) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1195,1198,1202,1208..1209) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1205..1209 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1221..1255 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(1226,1234,1245..1246) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1238,1241,1245,1251..1252) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1248..1252 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1273..1348 /region_name="Ig_Perlecan_like" /note="Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; cd05743" /db_xref="CDD:143220" Region 1276..1282 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143220" Region 1289..1294 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143220" Region 1312..1316 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143220" Region 1325..1331 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143220" Region 1340..1346 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143220" Region 1447..1577 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 1634..1688 /region_name="EGF_Lam" /note="Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in...; cd00055" /db_xref="CDD:238012" Site order(1634,1636,1648,1658,1660,1669) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region 1812..1948 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region <1949..1975 /region_name="EGF_Lam" /note="Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in...; cd00055" /db_xref="CDD:238012" Region 1983..2032 /region_name="EGF_Lam" /note="Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in...; cd00055" /db_xref="CDD:238012" Site order(1984,1986,1993,2000,2003,2012) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region <2068..2098 /region_name="Laminin_EGF" /note="Laminin EGF domain; pfam00053" /db_xref="CDD:395007" Region 2164..2298 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 2387..2455 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2480..2550 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2579..2647 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2676..2760 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2693..2697 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143259" Region 2706..2710 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143259" Region 2725..2729 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143259" Region 2739..2744 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143259" Region 2752..2755 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143259" Region 2778..2851 /region_name="I-set" /note="Immunoglobulin I-set domain; pfam07679" /db_xref="CDD:400151" Region 2783..2787 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2796..2800 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2817..2821 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2831..2836 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2844..2847 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 2854..2942 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2874..2878 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2887..2891 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2908..2912 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2922..2927 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2935..2938 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 2987..3044 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2990..2994 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3002..3005 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3022..3025 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3070..3146 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3079..3083 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3092..3096 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3126..3131 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3164..>3225 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3169..3173 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3180..3192 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3208..3212 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3274..3336 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3286..3290 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3298..3303 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3319..3323 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3367..3433 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3375..3379 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3388..3392 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3407..3411 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3421..3426 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3435..3438 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3455..3600 /region_name="LamG" /note="Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of...; cd00110" /db_xref="CDD:238058" Region 3623..3655 /region_name="EGF" /note="EGF-like domain; pfam00008" /db_xref="CDD:394967" Region 3703..3856 /region_name="LamG" /note="Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of...; cd00110" /db_xref="CDD:238058" Region 3915..3947 /region_name="EGF_CA" /note="Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the...; cd00054" /db_xref="CDD:238011" Region 3956..4109 /region_name="LamG" /note="Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of...; cd00110" /db_xref="CDD:238058" CDS 1..4150 /gene="trol" /locus_tag="Dmel_CG33950" /gene_synonym="anon-WO0153538.72; BcDNA:GM02481; CG12497; CG33675; CG33950; CG7981; CT23996; Dmel\CG33950; EG:BACR25B3.1; EG:BACR25B3.10; EG:BACR25B3.11; EG:BACR25B3.2; GC7891; l(1)3Ac; l(1)9-96; l(1)G0019; l(1)G0021; l(1)G0023; l(1)G0181; l(1)G0211; l(1)G0271; l(1)G0374; l(1)G0412; l(1)trol; l(1)VA51; l(1)zw1; l(1)zwl; MRE7; pcan; Pcan; Pcn; Perl; Perlecan; Trol; TROL; Trol-A; Trol-B; troll; Troll; zw-1; ZW-1; zw1" /coded_by="NM_001258571.3:185..12637" /db_xref="FLYBASE:FBpp0309653" /db_xref="GeneID:45320" /db_xref="FLYBASE:FBgn0284408" ORIGIN 1 mmgspgsqas aiatsvgirs grrgqaggsl llrllavtfv laachapllt nakqisnlgd 61 dqdfmladde slqgindsew qlmgddiddg llddvdetlk pmetkseeed lptgnwfsqs 121 vhrvrrsinr lfgsddnqer grrqqrersq rnrdainrqk elrrrqkedh nrwkqmrmer 181 qlekqrlvkr tnhvvfnrat dprkrasdly deneasgyhe edttlyrtyf vvnepydney 241 rdresvqfqn lqklldddlr nffhsnyegn ddeeqeirst lerveptndn fkirvqlrie 301 lptsvndfgs klqqqlnvyn rienlsaatd gvfsftessd ieeeaidvtl pqeevegsgs 361 ddsscrgdat ftcprsgkti cdemrcdrei qcpdgedeey cnypnvcted qfkcddkcle 421 lkkrcdgsid cldqtdeagc inapepepep epepepepes epeaepepep epepesepeq 481 epepqvpean ecqanefrcn ngdcidarkr cnnvsdcseg edeneecpaa csgmeyqcrd 541 gtrcisvsqq cdghsdcsdg ddeehcdgsg ydseecrfde fhcgtgecip mrqvcdniyd 601 cndysdevnc vegeeedrvg ipighqpwrp askhddwlhe mdtseyqvyq psnvyekans 661 qnpcasnqfr cttsnvcipl hlrcdgfyhc ndmsdeksce qyqrhtttrr pltlatptsr 721 ittqgpglle rrntttatea srwpwatktt tiatttsnpi ttvgvatriy cppnklacng 781 tcvsrrikcd girdcldgyd emycpetnnh yptqnvnvir pklgpnpipk scrphewqca 841 nlecidsslq cneikdcsdg sdeelsvcfg tattrlkpsd cspeqfycde scynrsvrcn 901 ghvdcsdgsd evgcslpcpq hqcpsgrcyt esercdrhrh cedgsdeanc cyanqfrcnn 961 gdcvsgsapc ngysecsdhs delncggtqe clpnqfrcns gqcvsssvrc ngrtdcqdss 1021 deqncaadsn drrpnqlnlk typdsqiike srevifrcrd egparakvkw srpggrplpp 1081 gftdrngrle ipnirvedag tyvceavgya syipgqqvtv nlnveryndv gsrpesacte 1141 yqatcmngec idkssicdgn pdcsdasdeq scslglkcqp nqfmcsnskc vdrtwrcdge 1201 ndcgdnsdet scdpepsgap crynefqcrs ghcipksfqc dnvpdctdgt devgcmaplp 1261 irpppqsvsl leyevleltc vatgtptpti vwrlnwghvp dkcesksygg tgtlrcpdmr 1321 pqdsgaysce iintrgthfv npdtivtvrp vrtdvceagf fnmlarkaee cvqcfcfgva 1381 kacdsanlft yaihppilsh rvvsvelspl rqivineaap gqdlltllhg vqfratnvhf 1441 sgretpylal padymgnqlk syggnlryev nyrgsgrpvn gpdviitgnr ftltyrvrtq 1501 pgqnnrvsip fvpggwqkpd grkasreeim milanvdnil irlgyldsta revdlinial 1561 dsagtadkgl gsaslvekcq cppgyvgdsc escasgyvrq pggpwlghcv pfipdscpsg 1621 tygdprrgvp ckecpcpltg snnfasgcqq spdgdvvcrc negytgrrce qcaagyqgnp 1681 laaggicrri pdtscnvdgt ysvhsngtcq ckdsvigeqc dtcksksfhl nsftytgcie 1741 cfcsgvgldc dsstwyrdqv tstfgrsrvd hgfvlvtnym qptpdtvpvs maaepnalsf 1801 igsadqsgnt lywslpaafl gnklssyggk ltytlsyspl pngimsrnsa pdvviksged 1861 lrlihyrksq vvpsvantys veikesawqr gdevvanreh vlmalsdita iyikatytts 1921 tkeaslrqvt ldvatptnlg tpraveveqc rcpegylgls ceqcapgyar dpeggiylgl 1981 crpcecnghs kycnsdtgdc eecsdntegp scercaagyv gdatrgtiyd cqpdegypip 2041 sppapgnqtl ectaycqieg iydcrgnecl ckrnvigdqc dqcrpgtygl saqnqdgcke 2101 cycsglasqc rsaalyrqli pvdfilnapl itdesgavqd tenlipdisr nmytythtsy 2161 lpkywslrgs vlgnqlfsyg grlsyslive sygnyerghd ivlignglkl iwsrpdgnen 2221 qeeynvrlhe deqwtrqdre sarpasrsdf mtvlsdlqhi liratprvpt qstsignvil 2281 esavttrtpg athasdielc qcpsgyvgts cescaplhyr dasgscslcp cdvsntescd 2341 lvsggyvecr ckarwkgdrc reidtndptd igtedpvltq iivsiqkpei tivpvggsmt 2401 lscsgrmrws nspvivnwyk ensrlpenve vqggnlylyd lqvsdsgvyi cqavnnetas 2461 vfkdtvsiti tkkdqlspae ivnlpshvtf eeyvnneiic evlgnpaprv twarvdghad 2521 aqstrtydnr lifdsprksd egryrcqaen dqnrdekyvi vyvqsnppqp ppqqdrlyit 2581 peeinglage sfqlncqfts vaslrydwsh ngrslssspa rnveirgntl evrdasesds 2641 gvytcvaydv rtrrnftesa rvnidrreeq pfgnkpiies leqniliiqg edysitceas 2701 gspypsikwa kvhdfmpenv hisgnvltiy garfenrgvy scvaendhgs dlsstsidie 2761 prerpsvkiv saplqtfsvg apaslyctve gipdptvewv rvdgqplspr hkiqspgymv 2821 iddiqledsg dyecrakniv geatgvatit vqeptlvqii pdnrdlrlte gdelsltcvg 2881 sgvpnpevew vnemalkrdl ysppsntail kiyrvtkada giytchgkne agsdeahvrv 2941 evqerrgdig gvdddsdrdp inynppqqqn pgihqpgsnq llatdigdnv tltcdmfqpl 3001 ntrwervdga plprnaytik nrleivrveq qnlgqyrcng igrdgnvkty fvkelvlmpl 3061 prirfypnip ltveagqnld vhcqvenvrp edvhwstdnn rplpssvriv gsvlrfvsit 3121 qaaageyrcs afnqygnrsq iarvavkkpa dfhqvpqsql qrhregeniq lqctvtdqyg 3181 vraqdnvefn wfrddrrplp nnartdsqil vltnlrpeda gryicnsydv drgqqlpevs 3241 idlqvltatp ppnspiylpp qlpaksrdys lklddqssnl ragestdvec yssddtytdv 3301 vwersdgapl snnvrqvgnr lvisnvspsd agnyvckckt degdlyttsy klevedqphe 3361 lksskivyak vganadlqcg adesrqptyr wsrqygqlqa grslmnekls ldsvqandag 3421 tyictaqyad getadfpnil vvtgaipqfr qeprsymsfp tlpnssfkfn feltfrpeng 3481 dglllfngqt rgsgdyials lkdryaefrf dfggkpmlvr aeeplalnew htvrvsrfkr 3541 dgyiqvdeqh pvafptlqqi pqldliedly iggvpnwell padavsqqvg fvgcisrltl 3601 qgrtvelire akykegitdc rpcaqgpcqn kgvclesqte qaytcicqpg wtgrdcaieg 3661 tqctpgvcga grcentendm eclcplnrsg drcqyneiln ehslnfkgns faaygtpkvt 3721 kvnitlsvrp asledsvily taestlpsgd ylalvlrggh aellintaar ldpvvvrsae 3781 plplnrwtri eirrrlgegi lrvgdgperk akapgsdril slkthlyvgg ydrstvkvnr 3841 dvnitkgfdg cisrlynfqk pvnlladikd aaniqscget nmiggdedsd neppvppptp 3901 dvhenelqpy amapcasdpc enggscseqe dvavcscpfg fsgkhcqehl qlgfnasfrg 3961 dgyvelnrsh fqpaleqsyt smgivfttnk pngllfwwgq eageeytgqd fiaaavvdgy 4021 veysmrldge eavirnsdir vdngerhivi akrdentail evdrmlhsge trptskksmk 4081 lpgnvfvgga pdlevftgfr ykhnlngciv vvegetvgqi nlssaavngv nanvcpandd 4141 plggteppvv