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LOCUS NP_001284822 3805 aa linear INV 26-DEC-2023 ACCESSION NP_001284822 VERSION NP_001284822.1 DBLINK BioProject: PRJNA164 BioSample: SAMN02803731 DBSOURCE REFSEQ: accession NM_001297893.2 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 3805) 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 AHN59293. ##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..3805 /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..3805 /product="terribly reduced optic lobes, isoform AS" /name="CG33950 gene product from transcript CG33950-RAS" /note="CG33950-PAS; trol-PAS; 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=420832 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 529..563 /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(534,542,553..554) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(546,549,553,559..560) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 556..560 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 569..603 /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(574,582,593..594) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(586,589,593,599..600) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 596..600 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 637..672 /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(642,650,661..662) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(654,657,661,668..669) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 665..669 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 698..759 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 709..713 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 723..726 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 742..746 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 793..827 /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(798,806,817..818) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(810,813,817,823..824) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 820..824 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 833..867 /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(838,846,857..858) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(850,853,857,863..864) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 860..864 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 876..910 /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(881,889,900..901) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(893,896,900,906..907) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 903..907 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 928..1003 /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 931..937 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143220" Region 944..949 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143220" Region 967..971 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143220" Region 980..986 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143220" Region 995..1001 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143220" Region 1102..1232 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 1289..1343 /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(1289,1291,1303,1313,1315,1324) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region 1467..1603 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region <1604..1630 /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 1638..1687 /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(1639,1641,1648,1655,1658,1667) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region <1723..1753 /region_name="Laminin_EGF" /note="Laminin EGF domain; pfam00053" /db_xref="CDD:395007" Region 1819..1953 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 2042..2110 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2135..2205 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2234..2302 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2331..2415 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2348..2352 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143259" Region 2361..2365 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143259" Region 2380..2384 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143259" Region 2394..2399 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143259" Region 2407..2410 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143259" Region 2433..2506 /region_name="I-set" /note="Immunoglobulin I-set domain; pfam07679" /db_xref="CDD:400151" Region 2438..2442 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2451..2455 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2472..2476 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2486..2491 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2499..2502 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 2509..2597 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2529..2533 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2542..2546 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2563..2567 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2577..2582 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2590..2593 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 2642..2699 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2645..2649 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2657..2660 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2677..2680 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2725..2801 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 2734..2738 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2747..2751 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2781..2786 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2819..>2880 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 2824..2828 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2835..2847 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2863..2867 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2929..2991 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2941..2945 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2953..2958 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2974..2978 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3022..3088 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3030..3034 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 3043..3047 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 3062..3066 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 3076..3081 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 3090..3093 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 3110..3255 /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 3278..3310 /region_name="EGF" /note="EGF-like domain; pfam00008" /db_xref="CDD:394967" Region 3358..3511 /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 3570..3602 /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 3611..3764 /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..3805 /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_001297893.2:185..11602" /db_xref="FLYBASE:FBpp0309654" /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 edeneecrcy anqfrcnngd 541 cvsgsapcng ysecsdhsde lncggtqecl pnqfrcnsgq cvsssvrcng rtdcqdssde 601 qncghrhtev sqglettgvf ttsttsttam tplriicppt sfkcengpci slglkcngrv 661 dcpydgsdea dcgqisndid padsndrrpn qlnlktypds qiikesrevi frcrdegpar 721 akvkwsrpgg rplppgftdr ngrleipnir vedagtyvce avgyasyipg qqvtvnlnve 781 ryndvgsrpe sacteyqatc mngecidkss icdgnpdcsd asdeqscslg lkcqpnqfmc 841 snskcvdrtw rcdgendcgd nsdetscdpe psgapcryne fqcrsghcip ksfqcdnvpd 901 ctdgtdevgc maplpirppp qsvslleyev leltcvatgt ptptivwrln wghvpdkces 961 ksyggtgtlr cpdmrpqdsg aysceiintr gthfvnpdti vtvrpvrtdv ceagffnmla 1021 rkaeecvqcf cfgvakacds anlftyaihp pilshrvvsv elsplrqivi neaapgqdll 1081 tllhgvqfra tnvhfsgret pylalpadym gnqlksyggn lryevnyrgs grpvngpdvi 1141 itgnrftlty rvrtqpgqnn rvsipfvpgg wqkpdgrkas reeimmilan vdnilirlgy 1201 ldstarevdl inialdsagt adkglgsasl vekcqcppgy vgdscescas gyvrqpggpw 1261 lghcvpfipd scpsgtygdp rrgvpckecp cpltgsnnfa sgcqqspdgd vvcrcnegyt 1321 grrceqcaag yqgnplaagg icrripdtsc nvdgtysvhs ngtcqckdsv igeqcdtcks 1381 ksfhlnsfty tgciecfcsg vgldcdsstw yrdqvtstfg rsrvdhgfvl vtnymqptpd 1441 tvpvsmaaep nalsfigsad qsgntlywsl paaflgnkls syggkltytl sysplpngim 1501 srnsapdvvi ksgedlrlih yrksqvvpsv antysveike sawqrgdevv anrehvlmal 1561 sditaiyika tyttstkeas lrqvtldvat ptnlgtprav eveqcrcpeg ylglsceqca 1621 pgyardpegg iylglcrpce cnghskycns dtgdceecsd ntegpscerc aagyvgdatr 1681 gtiydcqpde gypipsppap gnqtlectay cqiegiydcr gneclckrnv igdqcdqcrp 1741 gtyglsaqnq dgckecycsg lasqcrsaal yrqlipvdfi lnaplitdes gavqdtenli 1801 pdisrnmyty thtsylpkyw slrgsvlgnq lfsyggrlsy slivesygny erghdivlig 1861 nglkliwsrp dgnenqeeyn vrlhedeqwt rqdresarpa srsdfmtvls dlqhilirat 1921 prvptqstsi gnvilesavt trtpgathas dielcqcpsg yvgtscesca plhyrdasgs 1981 cslcpcdvsn tescdlvsgg yvecrckarw kgdrcreidt ndptdigted pvltqiivsi 2041 qkpeitivpv ggsmtlscsg rmrwsnspvi vnwykensrl penvevqggn lylydlqvsd 2101 sgvyicqavn netasvfkdt vsititkkdq lspaeivnlp shvtfeeyvn neiicevlgn 2161 paprvtwarv dghadaqstr tydnrlifds prksdegryr cqaendqnrd ekyvivyvqs 2221 nppqpppqqd rlyitpeein glagesfqln cqftsvaslr ydwshngrsl sssparnvei 2281 rgntlevrda sesdsgvytc vaydvrtrrn ftesarvnid rreeqpfgnk piiesleqni 2341 liiqgedysi tceasgspyp sikwakvhdf mpenvhisgn vltiygarfe nrgvyscvae 2401 ndhgsdlsst sidieprerp svkivsaplq tfsvgapasl yctvegipdp tvewvrvdgq 2461 plsprhkiqs pgymviddiq ledsgdyecr aknivgeatg vatitvqept lvqiipdnrd 2521 lrltegdels ltcvgsgvpn pevewvnema lkrdlyspps ntailkiyrv tkadagiytc 2581 hgkneagsde ahvrvevqer rgdiggvddd sdrdpinynp pqqqnpgihq pgsnqllatd 2641 igdnvtltcd mfqplntrwe rvdgaplprn aytiknrlei vrveqqnlgq yrcngigrdg 2701 nvktyfvkel vlmplprirf ypnipltvea gqnldvhcqv envrpedvhw stdnnrplps 2761 svrivgsvlr fvsitqaaag eyrcsafnqy gnrsqiarva vkkpadfhqv pqsqlqrhre 2821 geniqlqctv tdqygvraqd nvefnwfrdd rrplpnnart dsqilvltnl rpedagryic 2881 nsydvdrgqq lpevsidlqv ltatpppnsp iylppqlpak srdyslkldd qssnlrages 2941 tdvecyssdd tytdvvwers dgaplsnnvr qvgnrlvisn vspsdagnyv ckcktdegdl 3001 yttsykleve dqphelkssk ivyakvgana dlqcgadesr qptyrwsrqy gqlqagrslm 3061 neklsldsvq andagtyict aqyadgetad fpnilvvtga ipqfrqeprs ymsfptlpns 3121 sfkfnfeltf rpengdglll fngqtrgsgd yialslkdry aefrfdfggk pmlvraeepl 3181 alnewhtvrv srfkrdgyiq vdeqhpvafp tlqqipqldl iedlyiggvp nwellpadav 3241 sqqvgfvgci srltlqgrtv elireakyke gitdcrpcaq gpcqnkgvcl esqteqaytc 3301 icqpgwtgrd caiegtqctp gvcgagrcen tendmeclcp lnrsgdrcqy neilnehsln 3361 fkgnsfaayg tpkvtkvnit lsvrpasled svilytaest lpsgdylalv lrgghaelli 3421 ntaarldpvv vrsaeplpln rwtrieirrr lgegilrvgd gperkakapg sdrilslkth 3481 lyvggydrst vkvnrdvnit kgfdgcisrl ynfqkpvnll adikdaaniq scgetnmigg 3541 dedsdneppv ppptpdvhen elqpyamapc asdpcenggs cseqedvavc scpfgfsgkh 3601 cqehlqlgfn asfrgdgyve lnrshfqpal eqsytsmgiv fttnkpngll fwwgqeagee 3661 ytgqdfiaaa vvdgyveysm rldgeeavir nsdirvdnge rhiviakrde ntailevdrm 3721 lhsgetrpts kksmklpgnv fvggapdlev ftgfrykhnl ngcivvvege tvgqinlssa 3781 avngvnanvc panddplggt eppvv