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LOCUS NP_001245499 4299 aa linear INV 26-DEC-2023 ACCESSION NP_001245499 VERSION NP_001245499.2 DBLINK BioProject: PRJNA164 BioSample: SAMN02803731 DBSOURCE REFSEQ: accession NM_001258570.3 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 4299) 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 AFH07213. On Jul 15, 2014 this sequence version replaced NP_001245499.1. ##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..4299 /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..4299 /product="terribly reduced optic lobes, isoform AQ" /name="CG33950 gene product from transcript CG33950-RAQ" /note="CG33950-PAQ; trol-PAQ; 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=476476 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 773..807 /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(779,787,798..799) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(791,794,798,804..805) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 801..805 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 812..847 /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(817,826,837..838) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(830,833,837,843..844) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 840..844 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 862..896 /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(867,875,886..887) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(879,882,886,892..893) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 889..893 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 916..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 981..1013 /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(986,994,1005..1006) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(998,1001,1005,1011..1012) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1008..1012 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1030..1063 /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(1035,1042,1053..1054) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1046,1049,1053,1059..1060) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1056..1060 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1069..1099 /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(1070,1078,1089..1090) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1082,1085,1089,1095..1096) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1092..1096 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1100..1134 /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(1105,1113,1124..1125) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1117,1120,1124,1130..1131) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1127..1131 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1140..1174 /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(1145,1153,1164..1165) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1157,1160,1164,1170..1171) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1167..1171 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1192..1253 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 1203..1207 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 1217..1220 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 1236..1240 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 1287..1321 /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(1292,1300,1311..1312) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1304,1307,1311,1317..1318) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1314..1318 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1327..1361 /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(1332,1340,1351..1352) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1344,1347,1351,1357..1358) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1354..1358 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1370..1404 /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(1375,1383,1394..1395) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1387,1390,1394,1400..1401) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1397..1401 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1422..1497 /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 1425..1431 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143220" Region 1438..1443 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143220" Region 1461..1465 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143220" Region 1474..1480 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143220" Region 1489..1495 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143220" Region 1596..1726 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 1783..1837 /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(1783,1785,1797,1807,1809,1818) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region 1961..2097 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region <2098..2124 /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 2132..2181 /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(2133,2135,2142,2149,2152,2161) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region <2217..2247 /region_name="Laminin_EGF" /note="Laminin EGF domain; pfam00053" /db_xref="CDD:395007" Region 2313..2447 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 2536..2604 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2629..2699 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2728..2796 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2825..2909 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2842..2846 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143259" Region 2855..2859 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143259" Region 2874..2878 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143259" Region 2888..2893 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143259" Region 2901..2904 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143259" Region 2927..3000 /region_name="I-set" /note="Immunoglobulin I-set domain; pfam07679" /db_xref="CDD:400151" Region 2932..2936 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2945..2949 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2966..2970 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2980..2985 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2993..2996 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3003..3091 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3023..3027 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3036..3040 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3057..3061 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3071..3076 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3084..3087 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3136..3193 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3139..3143 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3151..3154 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3171..3174 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3219..3295 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3228..3232 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3241..3245 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3275..3280 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3313..>3374 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3318..3322 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3329..3341 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3357..3361 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3423..3485 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3435..3439 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3447..3452 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3468..3472 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3516..3582 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3524..3528 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3537..3541 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3556..3560 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3570..3575 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3584..3587 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3604..3749 /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 3772..3804 /region_name="EGF" /note="EGF-like domain; pfam00008" /db_xref="CDD:394967" Region 3852..4005 /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 4064..4096 /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 4105..4258 /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..4299 /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_001258570.3:185..13084" /db_xref="FLYBASE:FBpp0309652" /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 ttvgvanspp qtcleniefa 781 chnrdcisie svcdgipdcg rnededdalc kcsgdkykcq rgggcipksq vcdgkpqchd 841 rsdesachlh grlnktrlgv kclesqyqcg dgscisgykr cngihdcada sdeynciydy 901 edtydtdpnn nplnecdile fecdysqclp lekkcdgyad cedmsdelec qsytetnnhy 961 ptqnvnvirp klgpnpipks crphewqcan lecidsslqc neikdcsdgs deelsvcfgt 1021 attrlkpsdc speqfycdes cynrsvrcng hvdcsdgsde vgcslpcpqh qcpsgrcyte 1081 sercdrhrhc edgsdeancc yanqfrcnng dcvsgsapcn gysecsdhsd elncggtqec 1141 lpnqfrcnsg qcvsssvrcn grtdcqdssd eqncaadsnd rrpnqlnlkt ypdsqiikes 1201 revifrcrde gparakvkws rpggrplppg ftdrngrlei pnirvedagt yvceavgyas 1261 yipgqqvtvn lnveryndvg srpesactey qatcmngeci dkssicdgnp dcsdasdeqs 1321 cslglkcqpn qfmcsnskcv drtwrcdgen dcgdnsdets cdpepsgapc rynefqcrsg 1381 hcipksfqcd nvpdctdgtd evgcmaplpi rpppqsvsll eyevleltcv atgtptptiv 1441 wrlnwghvpd kcesksyggt gtlrcpdmrp qdsgayscei intrgthfvn pdtivtvrpv 1501 rtdvceagff nmlarkaeec vqcfcfgvak acdsanlfty aihppilshr vvsvelsplr 1561 qivineaapg qdlltllhgv qfratnvhfs gretpylalp adymgnqlks yggnlryevn 1621 yrgsgrpvng pdviitgnrf tltyrvrtqp gqnnrvsipf vpggwqkpdg rkasreeimm 1681 ilanvdnili rlgyldstar evdliniald sagtadkglg saslvekcqc ppgyvgdsce 1741 scasgyvrqp ggpwlghcvp fipdscpsgt ygdprrgvpc kecpcpltgs nnfasgcqqs 1801 pdgdvvcrcn egytgrrceq caagyqgnpl aaggicrrip dtscnvdgty svhsngtcqc 1861 kdsvigeqcd tcksksfhln sftytgciec fcsgvgldcd sstwyrdqvt stfgrsrvdh 1921 gfvlvtnymq ptpdtvpvsm aaepnalsfi gsadqsgntl ywslpaaflg nklssyggkl 1981 tytlsysplp ngimsrnsap dvviksgedl rlihyrksqv vpsvantysv eikesawqrg 2041 devvanrehv lmalsditai yikatyttst keaslrqvtl dvatptnlgt praveveqcr 2101 cpegylglsc eqcapgyard peggiylglc rpcecnghsk ycnsdtgdce ecsdntegps 2161 cercaagyvg datrgtiydc qpdegypips ppapgnqtle ctaycqiegi ydcrgneclc 2221 krnvigdqcd qcrpgtygls aqnqdgckec ycsglasqcr saalyrqlip vdfilnapli 2281 tdesgavqdt enlipdisrn mytythtsyl pkywslrgsv lgnqlfsygg rlsyslives 2341 ygnyerghdi vlignglkli wsrpdgnenq eeynvrlhed eqwtrqdres arpasrsdfm 2401 tvlsdlqhil iratprvptq stsignvile savttrtpga thasdielcq cpsgyvgtsc 2461 escaplhyrd asgscslcpc dvsntescdl vsggyvecrc karwkgdrcr eidtndptdi 2521 gtedpvltqi ivsiqkpeit ivpvggsmtl scsgrmrwsn spvivnwyke nsrlpenvev 2581 qggnlylydl qvsdsgvyic qavnnetasv fkdtvsitit kkdqlspaei vnlpshvtfe 2641 eyvnneiice vlgnpaprvt warvdghada qstrtydnrl ifdsprksde gryrcqaend 2701 qnrdekyviv yvqsnppqpp pqqdrlyitp eeinglages fqlncqftsv aslrydwshn 2761 grslssspar nveirgntle vrdasesdsg vytcvaydvr trrnftesar vnidrreeqp 2821 fgnkpiiesl eqniliiqge dysitceasg spypsikwak vhdfmpenvh isgnvltiyg 2881 arfenrgvys cvaendhgsd lsstsidiep rerpsvkivs aplqtfsvga paslyctveg 2941 ipdptvewvr vdgqplsprh kiqspgymvi ddiqledsgd yecraknivg eatgvatitv 3001 qeptlvqiip dnrdlrlteg delsltcvgs gvpnpevewv nemalkrdly sppsntailk 3061 iyrvtkadag iytchgknea gsdeahvrve vqerrgdigg vdddsdrdpi nynppqqqnp 3121 gihqpgsnql latdigdnvt ltcdmfqpln trwervdgap lprnaytikn rleivrveqq 3181 nlgqyrcngi grdgnvktyf vkelvlmplp rirfypnipl tveagqnldv hcqvenvrpe 3241 dvhwstdnnr plpssvrivg svlrfvsitq aaageyrcsa fnqygnrsqi arvavkkpad 3301 fhqvpqsqlq rhregeniql qctvtdqygv raqdnvefnw frddrrplpn nartdsqilv 3361 ltnlrpedag ryicnsydvd rgqqlpevsi dlqvltatpp pnspiylppq lpaksrdysl 3421 klddqssnlr agestdvecy ssddtytdvv wersdgapls nnvrqvgnrl visnvspsda 3481 gnyvckcktd egdlyttsyk levedqphel ksskivyakv ganadlqcga desrqptyrw 3541 srqygqlqag rslmneklsl dsvqandagt yictaqyadg etadfpnilv vtgaipqfrq 3601 eprsymsfpt lpnssfkfnf eltfrpengd glllfngqtr gsgdyialsl kdryaefrfd 3661 fggkpmlvra eeplalnewh tvrvsrfkrd gyiqvdeqhp vafptlqqip qldliedlyi 3721 ggvpnwellp adavsqqvgf vgcisrltlq grtvelirea kykegitdcr pcaqgpcqnk 3781 gvclesqteq aytcicqpgw tgrdcaiegt qctpgvcgag rcentendme clcplnrsgd 3841 rcqyneilne hslnfkgnsf aaygtpkvtk vnitlsvrpa sledsvilyt aestlpsgdy 3901 lalvlrggha ellintaarl dpvvvrsaep lplnrwtrie irrrlgegil rvgdgperka 3961 kapgsdrils lkthlyvggy drstvkvnrd vnitkgfdgc isrlynfqkp vnlladikda 4021 aniqscgetn miggdedsdn eppvppptpd vhenelqpya mapcasdpce nggscseqed 4081 vavcscpfgf sgkhcqehlq lgfnasfrgd gyvelnrshf qpaleqsyts mgivfttnkp 4141 ngllfwwgqe ageeytgqdf iaaavvdgyv eysmrldgee avirnsdirv dngerhivia 4201 krdentaile vdrmlhsget rptskksmkl pgnvfvggap dlevftgfry khnlngcivv 4261 vegetvgqin lssaavngvn anvcpanddp lggteppvv