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LOCUS NP_001401049 4489 aa linear INV 26-DEC-2023 ACCESSION NP_001401049 VERSION NP_001401049.1 DBLINK BioProject: PRJNA164 BioSample: SAMN02803731 DBSOURCE REFSEQ: accession NM_001414086.1 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 4489) 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 UYK33048. ##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..4489 /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..4489 /product="terribly reduced optic lobes, isoform BD" /name="CG33950 gene product from transcript CG33950-RBD" /note="CG33950-PBD; trol-PBD; 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=498100 Region 447..480 /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(452,459,470..471) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(463,466,470,476..477) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 473..477 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 532..564 /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(537,545,556..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 571..606 /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(576,585,596..597) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(589,592,596,602..603) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 599..603 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 616..650 /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(621,629,640..641) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(633,636,640,646..647) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 643..647 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 704..739 /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(709,718,729..730) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(722,725,729,735..736) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 732..736 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 813..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(819,827,838..839) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(831,834,838,844..845) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 841..845 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 852..887 /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(857,866,877..878) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(870,873,877,883..884) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 880..884 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 902..936 /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(907,915,926..927) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(919,922,926,932..933) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 929..933 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 956..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(961,969,980..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 997..1030 /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(1002,1009,1020..1021) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1013,1016,1020,1026..1027) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1023..1027 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1033..1067 /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(1038,1046,1057..1058) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1050,1053,1057,1063..1064) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1060..1064 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1072..1105 /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(1077,1084,1095..1096) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1088,1091,1095,1101..1102) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1098..1102 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1133..1165 /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(1138,1146,1157..1158) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1150,1153,1157,1163..1164) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1160..1164 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1182..1215 /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(1187,1194,1205..1206) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1198,1201,1205,1211..1212) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1208..1212 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1221..1251 /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(1222,1230,1241..1242) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1234,1237,1241,1247..1248) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1244..1248 /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 1292..1326 /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(1297,1305,1316..1317) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1309,1312,1316,1322..1323) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1319..1323 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1344..1405 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 1355..1359 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 1369..1372 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 1388..1392 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" 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 1479..1513 /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(1484,1492,1503..1504) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1496,1499,1503,1509..1510) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1506..1510 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1522..1556 /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(1527,1535,1546..1547) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1539,1542,1546,1552..1553) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1549..1553 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1574..1649 /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 1577..1583 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143220" Region 1590..1595 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143220" Region 1613..1617 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143220" Region 1626..1632 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143220" Region 1641..1647 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143220" Region 1748..1878 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 1935..1989 /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(1935,1937,1949,1959,1961,1970) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region 2113..2249 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region <2250..2276 /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 2284..2333 /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(2285,2287,2294,2301,2304,2313) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region <2369..2399 /region_name="Laminin_EGF" /note="Laminin EGF domain; pfam00053" /db_xref="CDD:395007" Region 2465..2599 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 2688..2756 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2791..2861 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2890..2958 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2987..3071 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3004..3008 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3017..3021 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3036..3040 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3050..3055 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3063..3066 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3089..3162 /region_name="I-set" /note="Immunoglobulin I-set domain; pfam07679" /db_xref="CDD:400151" Region 3094..3098 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3107..3111 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3128..3132 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3142..3147 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3155..3158 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3165..3253 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3185..3189 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3198..3202 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3219..3223 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3233..3238 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3246..3249 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3298..3355 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3301..3305 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3313..3316 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3333..3336 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3381..3457 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3390..3394 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3403..3407 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3437..3442 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3475..>3536 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3480..3484 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3491..3503 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3519..3523 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3613..3675 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3625..3629 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3637..3642 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3658..3662 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3706..3772 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3714..3718 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3727..3731 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3746..3750 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3760..3765 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3774..3777 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3794..3939 /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 3962..3994 /region_name="EGF" /note="EGF-like domain; pfam00008" /db_xref="CDD:394967" Region 4042..4195 /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 4254..4286 /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 4295..4448 /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..4489 /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_001414086.1:185..13654" /db_xref="FLYBASE:FBpp0428427" /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 gvfsftessv teesvrhldv gfvephitlf 361 heqntgyddf drkpttetqd ieeeaidvtl pqeevegsgs ddsscrgdat ftcprsgkti 421 cdemrcdrei qcpdgedeey cnypnvcted qfkcddkcle lkkrcdgsid cldqtdeagc 481 inapepepep epepepepes epeaepepep epepesepeq epepqvpean ecqanefrcn 541 ngdcidarkr cnnvsdcseg edeneecpaa csgmeyqcrd gtrcisvsqq cdghsdcsdg 601 ddeehcdgsg ydseecrfde fhcgtgecip mrqvcdniyd cndysdevnc vegeeedrvg 661 ipighqpwrp askhddwlhe mdtseyqvyq psnvyekans qnpcasnqfr cttsnvcipl 721 hlrcdgfyhc ndmsdeksce qyqrhtttrr pltlatptsr ittqgpglle rrntttatea 781 srwpwatktt tiatttsnpi ttvgvanspp qtcleniefa chnrdcisie svcdgipdcg 841 rnededdalc kcsgdkykcq rgggcipksq vcdgkpqchd rsdesachlh grlnktrlgv 901 kclesqyqcg dgscisgykr cngihdcada sdeynciydy edtydtdpnn nplnecdile 961 fecdysqclp lekkcdgyad cedmsdelec qsytdhcles efecdsyclp rdqlcngipn 1021 cqdgsdernc tfcredaylc ntgecvadnq rcngiadcad gsderhcari ycppnklacn 1081 gtcvsrrikc dgirdcldgy demycpetnn hyptqnvnvi rpklgpnpip kscrphewqc 1141 anlecidssl qcneikdcsd gsdeelsvcf gtattrlkps dcspeqfycd escynrsvrc 1201 nghvdcsdgs devgcslpcp qhqcpsgrcy tesercdrhr hcedgsdean ccyanqfrcn 1261 ngdcvsgsap cngysecsdh sdelncggtq eclpnqfrcn sgqcvsssvr cngrtdcqds 1321 sdeqncaads ndrrpnqlnl ktypdsqiik esrevifrcr degparakvk wsrpggrplp 1381 pgftdrngrl eipnirveda gtyvceavgy asyipgqqvt vnlnverynd vgsrpesact 1441 eyqatcmnge cidkssicdg npdcsdasde qscslglkcq pnqfmcsnsk cvdrtwrcdg 1501 endcgdnsde tscdpepsga pcrynefqcr sghcipksfq cdnvpdctdg tdevgcmapl 1561 pirpppqsvs lleyevlelt cvatgtptpt ivwrlnwghv pdkcesksyg gtgtlrcpdm 1621 rpqdsgaysc eiintrgthf vnpdtivtvr pvrtdvceag ffnmlarkae ecvqcfcfgv 1681 akacdsanlf tyaihppils hrvvsvelsp lrqivineaa pgqdlltllh gvqfratnvh 1741 fsgretpyla lpadymgnql ksyggnlrye vnyrgsgrpv ngpdviitgn rftltyrvrt 1801 qpgqnnrvsi pfvpggwqkp dgrkasreei mmilanvdni lirlgyldst arevdlinia 1861 ldsagtadkg lgsaslvekc qcppgyvgds cescasgyvr qpggpwlghc vpfipdscps 1921 gtygdprrgv pckecpcplt gsnnfasgcq qspdgdvvcr cnegytgrrc eqcaagyqgn 1981 plaaggicrr ipdtscnvdg tysvhsngtc qckdsvigeq cdtcksksfh lnsftytgci 2041 ecfcsgvgld cdsstwyrdq vtstfgrsrv dhgfvlvtny mqptpdtvpv smaaepnals 2101 figsadqsgn tlywslpaaf lgnklssygg kltytlsysp lpngimsrns apdvviksge 2161 dlrlihyrks qvvpsvanty sveikesawq rgdevvanre hvlmalsdit aiyikatytt 2221 stkeaslrqv tldvatptnl gtpraveveq crcpegylgl sceqcapgya rdpeggiylg 2281 lcrpcecngh skycnsdtgd ceecsdnteg pscercaagy vgdatrgtiy dcqpdegypi 2341 psppapgnqt lectaycqie giydcrgnec lckrnvigdq cdqcrpgtyg lsaqnqdgck 2401 ecycsglasq crsaalyrql ipvdfilnap litdesgavq dtenlipdis rnmytythts 2461 ylpkywslrg svlgnqlfsy ggrlsysliv esygnyergh divlignglk liwsrpdgne 2521 nqeeynvrlh edeqwtrqdr esarpasrsd fmtvlsdlqh iliratprvp tqstsignvi 2581 lesavttrtp gathasdiel cqcpsgyvgt scescaplhy rdasgscslc pcdvsntesc 2641 dlvsggyvec rckarwkgdr creidtndpt digtedpvlt qiivsiqkpe itivpvggsm 2701 tlscsgrmrw snspvivnwy kensrlpenv evqggnlyly dlqvsdsgvy icqavnneta 2761 svfkdtvsit itryaqemla ryekdqlspa eivnlpshvt feeyvnneii cevlgnpapr 2821 vtwarvdgha daqstrtydn rlifdsprks degryrcqae ndqnrdekyv ivyvqsnppq 2881 pppqqdrlyi tpeeinglag esfqlncqft svaslrydws hngrslsssp arnveirgnt 2941 levrdasesd sgvytcvayd vrtrrnftes arvnidrree qpfgnkpiie sleqniliiq 3001 gedysitcea sgspypsikw akvhdfmpen vhisgnvlti ygarfenrgv yscvaendhg 3061 sdlsstsidi eprerpsvki vsaplqtfsv gapaslyctv egipdptvew vrvdgqplsp 3121 rhkiqspgym viddiqleds gdyecrakni vgeatgvati tvqeptlvqi ipdnrdlrlt 3181 egdelsltcv gsgvpnpeve wvnemalkrd lysppsntai lkiyrvtkad agiytchgkn 3241 eagsdeahvr vevqerrgdi ggvdddsdrd pinynppqqq npgihqpgsn qllatdigdn 3301 vtltcdmfqp lntrwervdg aplprnayti knrleivrve qqnlgqyrcn gigrdgnvkt 3361 yfvkelvlmp lprirfypni pltveagqnl dvhcqvenvr pedvhwstdn nrplpssvri 3421 vgsvlrfvsi tqaaageyrc safnqygnrs qiarvavkkp adfhqvpqsq lqrhregeni 3481 qlqctvtdqy gvraqdnvef nwfrddrrpl pnnartdsqi lvltnlrped agryicnsyd 3541 vdrgqqlpev sidlqvlrap qypynrfkgg vslkdtpcmv lyicaaatpp pnspiylppq 3601 lpaksrdysl klddqssnlr agestdvecy ssddtytdvv wersdgapls nnvrqvgnrl 3661 visnvspsda gnyvckcktd egdlyttsyk levedqphel ksskivyakv ganadlqcga 3721 desrqptyrw srqygqlqag rslmneklsl dsvqandagt yictaqyadg etadfpnilv 3781 vtgaipqfrq eprsymsfpt lpnssfkfnf eltfrpengd glllfngqtr gsgdyialsl 3841 kdryaefrfd fggkpmlvra eeplalnewh tvrvsrfkrd gyiqvdeqhp vafptlqqip 3901 qldliedlyi ggvpnwellp adavsqqvgf vgcisrltlq grtvelirea kykegitdcr 3961 pcaqgpcqnk gvclesqteq aytcicqpgw tgrdcaiegt qctpgvcgag rcentendme 4021 clcplnrsgd rcqyneilne hslnfkgnsf aaygtpkvtk vnitlsvrpa sledsvilyt 4081 aestlpsgdy lalvlrggha ellintaarl dpvvvrsaep lplnrwtrie irrrlgegil 4141 rvgdgperka kapgsdrils lkthlyvggy drstvkvnrd vnitkgfdgc isrlynfqkp 4201 vnlladikda aniqscgetn miggdedsdn eppvppptpd vhenelqpya mapcasdpce 4261 nggscseqed vavcscpfgf sgkhcqehlq lgfnasfrgd gyvelnrshf qpaleqsyts 4321 mgivfttnkp ngllfwwgqe ageeytgqdf iaaavvdgyv eysmrldgee avirnsdirv 4381 dngerhivia krdentaile vdrmlhsget rptskksmkl pgnvfvggap dlevftgfry 4441 khnlngcivv vegetvgqin lssaavngvn anvcpanddp lggteppvv