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LOCUS NP_001027035 3887 aa linear INV 26-DEC-2023 ACCESSION NP_001027035 VERSION NP_001027035.3 DBLINK BioProject: PRJNA164 BioSample: SAMN02803731 DBSOURCE REFSEQ: accession NM_001031864.4 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 3887) 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 AAN09078. On Jul 15, 2014 this sequence version replaced NP_001027035.2. ##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..3887 /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..3887 /product="terribly reduced optic lobes, isoform AO" /name="CG33950 gene product from transcript CG33950-RAO" /note="CG33950-PAO; trol-PAO; 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=430153 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 534..568 /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(540,548,559..560) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(552,555,559,565..566) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 562..566 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 573..608 /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(578,587,598..599) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(591,594,598,604..605) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 601..605 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 618..651 /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(623,630,641..642) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(634,637,641,647..648) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 644..648 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 657..687 /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(658,666,677..678) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(670,673,677,683..684) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 680..684 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 688..722 /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(693,701,712..713) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(705,708,712,718..719) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 715..719 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 728..762 /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(733,741,752..753) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(745,748,752,758..759) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 755..759 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 780..841 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 791..795 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 805..808 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 824..828 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 875..909 /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(880,888,899..900) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(892,895,899,905..906) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 902..906 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 915..949 /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(920,928,939..940) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(932,935,939,945..946) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 942..946 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 958..992 /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(963,971,982..983) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(975,978,982,988..989) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 985..989 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1010..1085 /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 1013..1019 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143220" Region 1026..1031 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143220" Region 1049..1053 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143220" Region 1062..1068 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143220" Region 1077..1083 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143220" Region 1184..1314 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 1371..1425 /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(1371,1373,1385,1395,1397,1406) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region 1549..1685 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region <1686..1712 /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 1720..1769 /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(1721,1723,1730,1737,1740,1749) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region <1805..1835 /region_name="Laminin_EGF" /note="Laminin EGF domain; pfam00053" /db_xref="CDD:395007" Region 1901..2035 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 2124..2192 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2217..2287 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2316..2384 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2413..2497 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2430..2434 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143259" Region 2443..2447 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143259" Region 2462..2466 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143259" Region 2476..2481 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143259" Region 2489..2492 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143259" Region 2515..2588 /region_name="I-set" /note="Immunoglobulin I-set domain; pfam07679" /db_xref="CDD:400151" Region 2520..2524 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2533..2537 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2554..2558 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2568..2573 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2581..2584 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 2591..2679 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2611..2615 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2624..2628 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2645..2649 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2659..2664 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2672..2675 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 2724..2781 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2727..2731 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2739..2742 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2759..2762 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2807..2883 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 2816..2820 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2829..2833 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2863..2868 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2901..>2962 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 2906..2910 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2917..2929 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2945..2949 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3011..3073 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3023..3027 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3035..3040 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3056..3060 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3104..3170 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3112..3116 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3125..3129 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3144..3148 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3158..3163 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3172..3175 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3192..3337 /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 3360..3392 /region_name="EGF" /note="EGF-like domain; pfam00008" /db_xref="CDD:394967" Region 3440..3593 /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 3652..3684 /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 3693..3846 /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..3887 /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_001031864.4:185..11848" /db_xref="FLYBASE:FBpp0309650" /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 edeneechsp pqtclenief 541 achnrdcisi esvcdgipdc grnededdal ckcsgdkykc qrgggcipks qvcdgkpqch 601 drsdesacpt trlkpsdcsp eqfycdescy nrsvrcnghv dcsdgsdevg cslpcpqhqc 661 psgrcytese rcdrhrhced gsdeanccya nqfrcnngdc vsgsapcngy secsdhsdel 721 ncggtqeclp nqfrcnsgqc vsssvrcngr tdcqdssdeq ncaadsndrr pnqlnlktyp 781 dsqiikesre vifrcrdegp arakvkwsrp ggrplppgft drngrleipn irvedagtyv 841 ceavgyasyi pgqqvtvnln veryndvgsr pesacteyqa tcmngecidk ssicdgnpdc 901 sdasdeqscs lglkcqpnqf mcsnskcvdr twrcdgendc gdnsdetscd pepsgapcry 961 nefqcrsghc ipksfqcdnv pdctdgtdev gcmaplpirp ppqsvslley evleltcvat 1021 gtptptivwr lnwghvpdkc esksyggtgt lrcpdmrpqd sgaysceiin trgthfvnpd 1081 tivtvrpvrt dvceagffnm larkaeecvq cfcfgvakac dsanlftyai hppilshrvv 1141 svelsplrqi vineaapgqd lltllhgvqf ratnvhfsgr etpylalpad ymgnqlksyg 1201 gnlryevnyr gsgrpvngpd viitgnrftl tyrvrtqpgq nnrvsipfvp ggwqkpdgrk 1261 asreeimmil anvdnilirl gyldstarev dlinialdsa gtadkglgsa slvekcqcpp 1321 gyvgdscesc asgyvrqpgg pwlghcvpfi pdscpsgtyg dprrgvpcke cpcpltgsnn 1381 fasgcqqspd gdvvcrcneg ytgrrceqca agyqgnplaa ggicrripdt scnvdgtysv 1441 hsngtcqckd svigeqcdtc ksksfhlnsf tytgciecfc sgvgldcdss twyrdqvtst 1501 fgrsrvdhgf vlvtnymqpt pdtvpvsmaa epnalsfigs adqsgntlyw slpaaflgnk 1561 lssyggklty tlsysplpng imsrnsapdv viksgedlrl ihyrksqvvp svantysvei 1621 kesawqrgde vvanrehvlm alsditaiyi katyttstke aslrqvtldv atptnlgtpr 1681 aveveqcrcp egylglsceq capgyardpe ggiylglcrp cecnghskyc nsdtgdceec 1741 sdntegpsce rcaagyvgda trgtiydcqp degypipspp apgnqtlect aycqiegiyd 1801 crgneclckr nvigdqcdqc rpgtyglsaq nqdgckecyc sglasqcrsa alyrqlipvd 1861 filnaplitd esgavqdten lipdisrnmy tythtsylpk ywslrgsvlg nqlfsyggrl 1921 syslivesyg nyerghdivl ignglkliws rpdgnenqee ynvrlhedeq wtrqdresar 1981 pasrsdfmtv lsdlqhilir atprvptqst signvilesa vttrtpgath asdielcqcp 2041 sgyvgtsces caplhyrdas gscslcpcdv sntescdlvs ggyvecrcka rwkgdrcrei 2101 dtndptdigt edpvltqiiv siqkpeitiv pvggsmtlsc sgrmrwsnsp vivnwykens 2161 rlpenvevqg gnlylydlqv sdsgvyicqa vnnetasvfk dtvsititkk dqlspaeivn 2221 lpshvtfeey vnneiicevl gnpaprvtwa rvdghadaqs trtydnrlif dsprksdegr 2281 yrcqaendqn rdekyvivyv qsnppqpppq qdrlyitpee inglagesfq lncqftsvas 2341 lrydwshngr slsssparnv eirgntlevr dasesdsgvy tcvaydvrtr rnftesarvn 2401 idrreeqpfg nkpiiesleq niliiqgedy sitceasgsp ypsikwakvh dfmpenvhis 2461 gnvltiygar fenrgvyscv aendhgsdls stsidiepre rpsvkivsap lqtfsvgapa 2521 slyctvegip dptvewvrvd gqplsprhki qspgymvidd iqledsgdye craknivgea 2581 tgvatitvqe ptlvqiipdn rdlrltegde lsltcvgsgv pnpevewvne malkrdlysp 2641 psntailkiy rvtkadagiy tchgkneags deahvrvevq errgdiggvd ddsdrdpiny 2701 nppqqqnpgi hqpgsnqlla tdigdnvtlt cdmfqplntr wervdgaplp rnaytiknrl 2761 eivrveqqnl gqyrcngigr dgnvktyfvk elvlmplpri rfypnipltv eagqnldvhc 2821 qvenvrpedv hwstdnnrpl pssvrivgsv lrfvsitqaa ageyrcsafn qygnrsqiar 2881 vavkkpadfh qvpqsqlqrh regeniqlqc tvtdqygvra qdnvefnwfr ddrrplpnna 2941 rtdsqilvlt nlrpedagry icnsydvdrg qqlpevsidl qvltatpppn spiylppqlp 3001 aksrdyslkl ddqssnlrag estdvecyss ddtytdvvwe rsdgaplsnn vrqvgnrlvi 3061 snvspsdagn yvckcktdeg dlyttsykle vedqphelks skivyakvga nadlqcgade 3121 srqptyrwsr qygqlqagrs lmneklslds vqandagtyi ctaqyadget adfpnilvvt 3181 gaipqfrqep rsymsfptlp nssfkfnfel tfrpengdgl llfngqtrgs gdyialslkd 3241 ryaefrfdfg gkpmlvraee plalnewhtv rvsrfkrdgy iqvdeqhpva fptlqqipql 3301 dliedlyigg vpnwellpad avsqqvgfvg cisrltlqgr tvelireaky kegitdcrpc 3361 aqgpcqnkgv clesqteqay tcicqpgwtg rdcaiegtqc tpgvcgagrc entendmecl 3421 cplnrsgdrc qyneilnehs lnfkgnsfaa ygtpkvtkvn itlsvrpasl edsvilytae 3481 stlpsgdyla lvlrgghael lintaarldp vvvrsaeplp lnrwtrieir rrlgegilrv 3541 gdgperkaka pgsdrilslk thlyvggydr stvkvnrdvn itkgfdgcis rlynfqkpvn 3601 lladikdaan iqscgetnmi ggdedsdnep pvppptpdvh enelqpyama pcasdpceng 3661 gscseqedva vcscpfgfsg khcqehlqlg fnasfrgdgy velnrshfqp aleqsytsmg 3721 ivfttnkpng llfwwgqeag eeytgqdfia aavvdgyvey smrldgeeav irnsdirvdn 3781 gerhiviakr dentailevd rmlhsgetrp tskksmklpg nvfvggapdl evftgfrykh 3841 nlngcivvve getvgqinls saavngvnan vcpanddplg gteppvv