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LOCUS NP_001162648 4411 aa linear INV 26-DEC-2023 ACCESSION NP_001162648 VERSION NP_001162648.3 DBLINK BioProject: PRJNA164 BioSample: SAMN02803731 DBSOURCE REFSEQ: accession NM_001169177.4 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 4411) 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 ACZ95185. On Jul 15, 2014 this sequence version replaced NP_001162648.2. ##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..4411 /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..4411 /product="terribly reduced optic lobes, isoform AH" /name="CG33950 gene product from transcript CG33950-RAH" /note="CG33950-PAH; trol-PAH; 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=489002 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 957..990 /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(962,969,980..981) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(973,976,980,986..987) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 983..987 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 993..1027 /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(998,1006,1017..1018) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1010,1013,1017,1023..1024) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1020..1024 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1032..1065 /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(1037,1044,1055..1056) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1048,1051,1055,1061..1062) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1058..1062 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1093..1125 /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(1098,1106,1117..1118) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1110,1113,1117,1123..1124) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1120..1124 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1142..1175 /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(1147,1154,1165..1166) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1158,1161,1165,1171..1172) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1168..1172 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1181..1211 /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(1182,1190,1201..1202) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1194,1197,1201,1207..1208) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1204..1208 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1212..1246 /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(1217,1225,1236..1237) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1229,1232,1236,1242..1243) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1239..1243 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1252..1286 /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(1257,1265,1276..1277) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1269,1272,1276,1282..1283) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1279..1283 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1304..1365 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 1315..1319 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 1329..1332 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 1348..1352 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 1399..1433 /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(1404,1412,1423..1424) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1416,1419,1423,1429..1430) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1426..1430 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1439..1473 /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(1444,1452,1463..1464) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1456,1459,1463,1469..1470) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1466..1470 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1482..1516 /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(1487,1495,1506..1507) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1499,1502,1506,1512..1513) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1509..1513 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1534..1609 /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 1537..1543 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143220" Region 1550..1555 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143220" Region 1573..1577 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143220" Region 1586..1592 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143220" Region 1601..1607 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143220" Region 1708..1838 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 1895..1949 /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(1895,1897,1909,1919,1921,1930) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region 2073..2209 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region <2210..2236 /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 2244..2293 /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(2245,2247,2254,2261,2264,2273) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region <2329..2359 /region_name="Laminin_EGF" /note="Laminin EGF domain; pfam00053" /db_xref="CDD:395007" Region 2425..2559 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 2648..2716 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2741..2811 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2840..2908 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2937..3021 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2954..2958 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143259" Region 2967..2971 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143259" Region 2986..2990 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143259" Region 3000..3005 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143259" Region 3013..3016 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143259" Region 3039..3112 /region_name="I-set" /note="Immunoglobulin I-set domain; pfam07679" /db_xref="CDD:400151" Region 3044..3048 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3057..3061 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3078..3082 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3092..3097 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3105..3108 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3115..3203 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3135..3139 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3148..3152 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3169..3173 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3183..3188 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3196..3199 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3248..3305 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3251..3255 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3263..3266 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3283..3286 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3331..3407 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3340..3344 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3353..3357 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3387..3392 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3425..>3486 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3430..3434 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3441..3453 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3469..3473 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3535..3597 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3547..3551 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3559..3564 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3580..3584 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3628..3694 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3636..3640 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3649..3653 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3668..3672 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3682..3687 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3696..3699 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3716..3861 /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 3884..3916 /region_name="EGF" /note="EGF-like domain; pfam00008" /db_xref="CDD:394967" Region 3964..4117 /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 4176..4208 /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 4217..4370 /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..4411 /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_001169177.4:185..13420" /db_xref="FLYBASE:FBpp0309644" /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 qsytdhcles 961 efecdsyclp rdqlcngipn cqdgsdernc tfcredaylc ntgecvadnq rcngiadcad 1021 gsderhcari ycppnklacn gtcvsrrikc dgirdcldgy demycpetnn hyptqnvnvi 1081 rpklgpnpip kscrphewqc anlecidssl qcneikdcsd gsdeelsvcf gtattrlkps 1141 dcspeqfycd escynrsvrc nghvdcsdgs devgcslpcp qhqcpsgrcy tesercdrhr 1201 hcedgsdean ccyanqfrcn ngdcvsgsap cngysecsdh sdelncggtq eclpnqfrcn 1261 sgqcvsssvr cngrtdcqds sdeqncaads ndrrpnqlnl ktypdsqiik esrevifrcr 1321 degparakvk wsrpggrplp pgftdrngrl eipnirveda gtyvceavgy asyipgqqvt 1381 vnlnverynd vgsrpesact eyqatcmnge cidkssicdg npdcsdasde qscslglkcq 1441 pnqfmcsnsk cvdrtwrcdg endcgdnsde tscdpepsga pcrynefqcr sghcipksfq 1501 cdnvpdctdg tdevgcmapl pirpppqsvs lleyevlelt cvatgtptpt ivwrlnwghv 1561 pdkcesksyg gtgtlrcpdm rpqdsgaysc eiintrgthf vnpdtivtvr pvrtdvceag 1621 ffnmlarkae ecvqcfcfgv akacdsanlf tyaihppils hrvvsvelsp lrqivineaa 1681 pgqdlltllh gvqfratnvh fsgretpyla lpadymgnql ksyggnlrye vnyrgsgrpv 1741 ngpdviitgn rftltyrvrt qpgqnnrvsi pfvpggwqkp dgrkasreei mmilanvdni 1801 lirlgyldst arevdlinia ldsagtadkg lgsaslvekc qcppgyvgds cescasgyvr 1861 qpggpwlghc vpfipdscps gtygdprrgv pckecpcplt gsnnfasgcq qspdgdvvcr 1921 cnegytgrrc eqcaagyqgn plaaggicrr ipdtscnvdg tysvhsngtc qckdsvigeq 1981 cdtcksksfh lnsftytgci ecfcsgvgld cdsstwyrdq vtstfgrsrv dhgfvlvtny 2041 mqptpdtvpv smaaepnals figsadqsgn tlywslpaaf lgnklssygg kltytlsysp 2101 lpngimsrns apdvviksge dlrlihyrks qvvpsvanty sveikesawq rgdevvanre 2161 hvlmalsdit aiyikatytt stkeaslrqv tldvatptnl gtpraveveq crcpegylgl 2221 sceqcapgya rdpeggiylg lcrpcecngh skycnsdtgd ceecsdnteg pscercaagy 2281 vgdatrgtiy dcqpdegypi psppapgnqt lectaycqie giydcrgnec lckrnvigdq 2341 cdqcrpgtyg lsaqnqdgck ecycsglasq crsaalyrql ipvdfilnap litdesgavq 2401 dtenlipdis rnmytythts ylpkywslrg svlgnqlfsy ggrlsysliv esygnyergh 2461 divlignglk liwsrpdgne nqeeynvrlh edeqwtrqdr esarpasrsd fmtvlsdlqh 2521 iliratprvp tqstsignvi lesavttrtp gathasdiel cqcpsgyvgt scescaplhy 2581 rdasgscslc pcdvsntesc dlvsggyvec rckarwkgdr creidtndpt digtedpvlt 2641 qiivsiqkpe itivpvggsm tlscsgrmrw snspvivnwy kensrlpenv evqggnlyly 2701 dlqvsdsgvy icqavnneta svfkdtvsit itkkdqlspa eivnlpshvt feeyvnneii 2761 cevlgnpapr vtwarvdgha daqstrtydn rlifdsprks degryrcqae ndqnrdekyv 2821 ivyvqsnppq pppqqdrlyi tpeeinglag esfqlncqft svaslrydws hngrslsssp 2881 arnveirgnt levrdasesd sgvytcvayd vrtrrnftes arvnidrree qpfgnkpiie 2941 sleqniliiq gedysitcea sgspypsikw akvhdfmpen vhisgnvlti ygarfenrgv 3001 yscvaendhg sdlsstsidi eprerpsvki vsaplqtfsv gapaslyctv egipdptvew 3061 vrvdgqplsp rhkiqspgym viddiqleds gdyecrakni vgeatgvati tvqeptlvqi 3121 ipdnrdlrlt egdelsltcv gsgvpnpeve wvnemalkrd lysppsntai lkiyrvtkad 3181 agiytchgkn eagsdeahvr vevqerrgdi ggvdddsdrd pinynppqqq npgihqpgsn 3241 qllatdigdn vtltcdmfqp lntrwervdg aplprnayti knrleivrve qqnlgqyrcn 3301 gigrdgnvkt yfvkelvlmp lprirfypni pltveagqnl dvhcqvenvr pedvhwstdn 3361 nrplpssvri vgsvlrfvsi tqaaageyrc safnqygnrs qiarvavkkp adfhqvpqsq 3421 lqrhregeni qlqctvtdqy gvraqdnvef nwfrddrrpl pnnartdsqi lvltnlrped 3481 agryicnsyd vdrgqqlpev sidlqvltat pppnspiylp pqlpaksrdy slklddqssn 3541 lragestdve cyssddtytd vvwersdgap lsnnvrqvgn rlvisnvsps dagnyvckck 3601 tdegdlytts yklevedqph elksskivya kvganadlqc gadesrqpty rwsrqygqlq 3661 agrslmnekl sldsvqanda gtyictaqya dgetadfpni lvvtgaipqf rqeprsymsf 3721 ptlpnssfkf nfeltfrpen gdglllfngq trgsgdyial slkdryaefr fdfggkpmlv 3781 raeeplalne whtvrvsrfk rdgyiqvdeq hpvafptlqq ipqldliedl yiggvpnwel 3841 lpadavsqqv gfvgcisrlt lqgrtvelir eakykegitd crpcaqgpcq nkgvclesqt 3901 eqaytcicqp gwtgrdcaie gtqctpgvcg agrcentend meclcplnrs gdrcqyneil 3961 nehslnfkgn sfaaygtpkv tkvnitlsvr pasledsvil ytaestlpsg dylalvlrgg 4021 haellintaa rldpvvvrsa eplplnrwtr ieirrrlgeg ilrvgdgper kakapgsdri 4081 lslkthlyvg gydrstvkvn rdvnitkgfd gcisrlynfq kpvnlladik daaniqscge 4141 tnmiggdeds dneppvpppt pdvhenelqp yamapcasdp cenggscseq edvavcscpf 4201 gfsgkhcqeh lqlgfnasfr gdgyvelnrs hfqpaleqsy tsmgivfttn kpngllfwwg 4261 qeageeytgq dfiaaavvdg yveysmrldg eeavirnsdi rvdngerhiv iakrdentai 4321 levdrmlhsg etrptskksm klpgnvfvgg apdlevftgf rykhnlngci vvvegetvgq 4381 inlssaavng vnanvcpand dplggteppv v