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LOCUS NP_001027038 4479 aa linear INV 26-DEC-2023 ACCESSION NP_001027038 VERSION NP_001027038.3 DBLINK BioProject: PRJNA164 BioSample: SAMN02803731 DBSOURCE REFSEQ: accession NM_001031867.4 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 4479) 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 AAF45787. On Jul 15, 2014 this sequence version replaced NP_001027038.2. ##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..4479 /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..4479 /product="terribly reduced optic lobes, isoform AT" /name="CG33950 gene product from transcript CG33950-RAT" /note="CG33950-PAT; trol-PAT; 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=496816 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 2781..2851 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2880..2948 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2977..3061 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2994..2998 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143259" Region 3007..3011 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143259" Region 3026..3030 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143259" Region 3040..3045 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143259" Region 3053..3056 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143259" Region 3079..3152 /region_name="I-set" /note="Immunoglobulin I-set domain; pfam07679" /db_xref="CDD:400151" Region 3084..3088 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3097..3101 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3118..3122 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3132..3137 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3145..3148 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3155..3243 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3175..3179 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3188..3192 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3209..3213 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3223..3228 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3236..3239 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3288..3345 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3291..3295 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3303..3306 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3323..3326 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3371..3447 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3380..3384 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3393..3397 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3427..3432 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3465..>3526 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3470..3474 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3481..3493 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3509..3513 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3603..3665 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3615..3619 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3627..3632 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3648..3652 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3696..3762 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3704..3708 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3717..3721 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3736..3740 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3750..3755 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3764..3767 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3784..3929 /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 3952..3984 /region_name="EGF" /note="EGF-like domain; pfam00008" /db_xref="CDD:394967" Region 4032..4185 /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 4244..4276 /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 4285..4438 /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..4479 /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_001031867.4:185..13624" /db_xref="FLYBASE:FBpp0309655" /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 itkkdqlspa eivnlpshvt feeyvnneii cevlgnpapr vtwarvdgha 2821 daqstrtydn rlifdsprks degryrcqae ndqnrdekyv ivyvqsnppq pppqqdrlyi 2881 tpeeinglag esfqlncqft svaslrydws hngrslsssp arnveirgnt levrdasesd 2941 sgvytcvayd vrtrrnftes arvnidrree qpfgnkpiie sleqniliiq gedysitcea 3001 sgspypsikw akvhdfmpen vhisgnvlti ygarfenrgv yscvaendhg sdlsstsidi 3061 eprerpsvki vsaplqtfsv gapaslyctv egipdptvew vrvdgqplsp rhkiqspgym 3121 viddiqleds gdyecrakni vgeatgvati tvqeptlvqi ipdnrdlrlt egdelsltcv 3181 gsgvpnpeve wvnemalkrd lysppsntai lkiyrvtkad agiytchgkn eagsdeahvr 3241 vevqerrgdi ggvdddsdrd pinynppqqq npgihqpgsn qllatdigdn vtltcdmfqp 3301 lntrwervdg aplprnayti knrleivrve qqnlgqyrcn gigrdgnvkt yfvkelvlmp 3361 lprirfypni pltveagqnl dvhcqvenvr pedvhwstdn nrplpssvri vgsvlrfvsi 3421 tqaaageyrc safnqygnrs qiarvavkkp adfhqvpqsq lqrhregeni qlqctvtdqy 3481 gvraqdnvef nwfrddrrpl pnnartdsqi lvltnlrped agryicnsyd vdrgqqlpev 3541 sidlqvlrap qypynrfkgg vslkdtpcmv lyicaaatpp pnspiylppq lpaksrdysl 3601 klddqssnlr agestdvecy ssddtytdvv wersdgapls nnvrqvgnrl visnvspsda 3661 gnyvckcktd egdlyttsyk levedqphel ksskivyakv ganadlqcga desrqptyrw 3721 srqygqlqag rslmneklsl dsvqandagt yictaqyadg etadfpnilv vtgaipqfrq 3781 eprsymsfpt lpnssfkfnf eltfrpengd glllfngqtr gsgdyialsl kdryaefrfd 3841 fggkpmlvra eeplalnewh tvrvsrfkrd gyiqvdeqhp vafptlqqip qldliedlyi 3901 ggvpnwellp adavsqqvgf vgcisrltlq grtvelirea kykegitdcr pcaqgpcqnk 3961 gvclesqteq aytcicqpgw tgrdcaiegt qctpgvcgag rcentendme clcplnrsgd 4021 rcqyneilne hslnfkgnsf aaygtpkvtk vnitlsvrpa sledsvilyt aestlpsgdy 4081 lalvlrggha ellintaarl dpvvvrsaep lplnrwtrie irrrlgegil rvgdgperka 4141 kapgsdrils lkthlyvggy drstvkvnrd vnitkgfdgc isrlynfqkp vnlladikda 4201 aniqscgetn miggdedsdn eppvppptpd vhenelqpya mapcasdpce nggscseqed 4261 vavcscpfgf sgkhcqehlq lgfnasfrgd gyvelnrshf qpaleqsyts mgivfttnkp 4321 ngllfwwgqe ageeytgqdf iaaavvdgyv eysmrldgee avirnsdirv dngerhivia 4381 krdentaile vdrmlhsget rptskksmkl pgnvfvggap dlevftgfry khnlngcivv 4441 vegetvgqin lssaavngvn anvcpanddp lggteppvv