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terribly reduced optic lobes, isoform BE [Drosophila melanogaster].


LOCUS       NP_001401050            3738 aa            linear   INV 26-DEC-2023
ACCESSION   NP_001401050
VERSION     NP_001401050.1
DBLINK      BioProject: PRJNA164
            BioSample: SAMN02803731
DBSOURCE    REFSEQ: accession NM_001414087.1
KEYWORDS    RefSeq.
SOURCE      Drosophila melanogaster (fruit fly)
  ORGANISM  Drosophila melanogaster
            Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
            Pterygota; Neoptera; Endopterygota; Diptera; Brachycera;
            Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
REFERENCE   1  (residues 1 to 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 3738)
  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 UYK33049.
            
            ##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..3738
                     /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..3738
                     /product="terribly reduced optic lobes, isoform BE"
                     /name="CG33950 gene product from transcript CG33950-RBE"
                     /note="CG33950-PBE; trol-PBE; 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=413955
     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          621..682
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          632..636
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          646..649
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          665..669
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          716..750
                     /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(721,729,740..741)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(733,736,740,746..747)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            743..747
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          756..790
                     /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(761,769,780..781)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(773,776,780,786..787)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            783..787
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          799..833
                     /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(804,812,823..824)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(816,819,823,829..830)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            826..830
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          851..926
                     /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          854..860
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:143220"
     Region          867..872
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:143220"
     Region          890..894
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:143220"
     Region          903..909
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:143220"
     Region          918..924
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:143220"
     Region          1025..1155
                     /region_name="Laminin_B"
                     /note="Laminin B (Domain IV); pfam00052"
                     /db_xref="CDD:459652"
     Region          1212..1266
                     /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(1212,1214,1226,1236,1238,1247)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          1390..1526
                     /region_name="Laminin_B"
                     /note="Laminin B (Domain IV); pfam00052"
                     /db_xref="CDD:459652"
     Region          <1527..1553
                     /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          1561..1610
                     /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(1562,1564,1571,1578,1581,1590)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          <1646..1676
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Region          1742..1876
                     /region_name="Laminin_B"
                     /note="Laminin B (Domain IV); pfam00052"
                     /db_xref="CDD:459652"
     Region          1965..2033
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          2068..2138
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          2167..2235
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          2264..2348
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2281..2285
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2294..2298
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2313..2317
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2327..2332
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2340..2343
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2366..2439
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          2371..2375
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2384..2388
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2405..2409
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2419..2424
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2432..2435
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2442..2530
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2462..2466
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2475..2479
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2496..2500
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2510..2515
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2523..2526
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2575..2632
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2578..2582
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2590..2593
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2610..2613
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2658..2734
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          2667..2671
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2680..2684
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2714..2719
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2752..>2813
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          2757..2761
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2768..2780
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2796..2800
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2862..2924
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2874..2878
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2886..2891
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2907..2911
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2955..3021
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          2963..2967
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2976..2980
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2995..2999
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3009..3014
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          3023..3026
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          3043..3188
                     /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          3211..3243
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          3291..3444
                     /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          3503..3535
                     /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          3544..3697
                     /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..3738
                     /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_001414087.1:185..11401"
                     /db_xref="FLYBASE:FBpp0428428"
                     /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 qncaadsndr rpnqlnlkty pdsqiikesr evifrcrdeg parakvkwsr pggrplppgf
      661 tdrngrleip nirvedagty vceavgyasy ipgqqvtvnl nveryndvgs rpesacteyq
      721 atcmngecid kssicdgnpd csdasdeqsc slglkcqpnq fmcsnskcvd rtwrcdgend
      781 cgdnsdetsc dpepsgapcr ynefqcrsgh cipksfqcdn vpdctdgtde vgcmaplpir
      841 pppqsvslle yevleltcva tgtptptivw rlnwghvpdk cesksyggtg tlrcpdmrpq
      901 dsgaysceii ntrgthfvnp dtivtvrpvr tdvceagffn mlarkaeecv qcfcfgvaka
      961 cdsanlftya ihppilshrv vsvelsplrq ivineaapgq dlltllhgvq fratnvhfsg
     1021 retpylalpa dymgnqlksy ggnlryevny rgsgrpvngp dviitgnrft ltyrvrtqpg
     1081 qnnrvsipfv pggwqkpdgr kasreeimmi lanvdnilir lgyldstare vdlinialds
     1141 agtadkglgs aslvekcqcp pgyvgdsces casgyvrqpg gpwlghcvpf ipdscpsgty
     1201 gdprrgvpck ecpcpltgsn nfasgcqqsp dgdvvcrcne gytgrrceqc aagyqgnpla
     1261 aggicrripd tscnvdgtys vhsngtcqck dsvigeqcdt cksksfhlns ftytgciecf
     1321 csgvgldcds stwyrdqvts tfgrsrvdhg fvlvtnymqp tpdtvpvsma aepnalsfig
     1381 sadqsgntly wslpaaflgn klssyggklt ytlsysplpn gimsrnsapd vviksgedlr
     1441 lihyrksqvv psvantysve ikesawqrgd evvanrehvl malsditaiy ikatyttstk
     1501 easlrqvtld vatptnlgtp raveveqcrc pegylglsce qcapgyardp eggiylglcr
     1561 pcecnghsky cnsdtgdcee csdntegpsc ercaagyvgd atrgtiydcq pdegypipsp
     1621 papgnqtlec taycqiegiy dcrgneclck rnvigdqcdq crpgtyglsa qnqdgckecy
     1681 csglasqcrs aalyrqlipv dfilnaplit desgavqdte nlipdisrnm ytythtsylp
     1741 kywslrgsvl gnqlfsyggr lsyslivesy gnyerghdiv lignglkliw srpdgnenqe
     1801 eynvrlhede qwtrqdresa rpasrsdfmt vlsdlqhili ratprvptqs tsignviles
     1861 avttrtpgat hasdielcqc psgyvgtsce scaplhyrda sgscslcpcd vsntescdlv
     1921 sggyvecrck arwkgdrcre idtndptdig tedpvltqii vsiqkpeiti vpvggsmtls
     1981 csgrmrwsns pvivnwyken srlpenvevq ggnlylydlq vsdsgvyicq avnnetasvf
     2041 kdtvsititr yaqemlarye kdqlspaeiv nlpshvtfee yvnneiicev lgnpaprvtw
     2101 arvdghadaq strtydnrli fdsprksdeg ryrcqaendq nrdekyvivy vqsnppqppp
     2161 qqdrlyitpe einglagesf qlncqftsva slrydwshng rslsssparn veirgntlev
     2221 rdasesdsgv ytcvaydvrt rrnftesarv nidrreeqpf gnkpiiesle qniliiqged
     2281 ysitceasgs pypsikwakv hdfmpenvhi sgnvltiyga rfenrgvysc vaendhgsdl
     2341 sstsidiepr erpsvkivsa plqtfsvgap aslyctvegi pdptvewvrv dgqplsprhk
     2401 iqspgymvid diqledsgdy ecraknivge atgvatitvq eptlvqiipd nrdlrltegd
     2461 elsltcvgsg vpnpevewvn emalkrdlys ppsntailki yrvtkadagi ytchgkneag
     2521 sdeahvrvev qerrgdiggv dddsdrdpin ynppqqqnpg ihqpgsnqll atdigdnvtl
     2581 tcdmfqplnt rwervdgapl prnaytiknr leivrveqqn lgqyrcngig rdgnvktyfv
     2641 kelvlmplpr irfypniplt veagqnldvh cqvenvrped vhwstdnnrp lpssvrivgs
     2701 vlrfvsitqa aageyrcsaf nqygnrsqia rvavkkpadf hqvpqsqlqr hregeniqlq
     2761 ctvtdqygvr aqdnvefnwf rddrrplpnn artdsqilvl tnlrpedagr yicnsydvdr
     2821 gqqlpevsid lqvltatppp nspiylppql paksrdyslk lddqssnlra gestdvecys
     2881 sddtytdvvw ersdgaplsn nvrqvgnrlv isnvspsdag nyvckcktde gdlyttsykl
     2941 evedqphelk sskivyakvg anadlqcgad esrqptyrws rqygqlqagr slmneklsld
     3001 svqandagty ictaqyadge tadfpnilvv tgaipqfrqe prsymsfptl pnssfkfnfe
     3061 ltfrpengdg lllfngqtrg sgdyialslk dryaefrfdf ggkpmlvrae eplalnewht
     3121 vrvsrfkrdg yiqvdeqhpv afptlqqipq ldliedlyig gvpnwellpa davsqqvgfv
     3181 gcisrltlqg rtvelireak ykegitdcrp caqgpcqnkg vclesqteqa ytcicqpgwt
     3241 grdcaiegtq ctpgvcgagr centendmec lcplnrsgdr cqyneilneh slnfkgnsfa
     3301 aygtpkvtkv nitlsvrpas ledsvilyta estlpsgdyl alvlrgghae llintaarld
     3361 pvvvrsaepl plnrwtriei rrrlgegilr vgdgperkak apgsdrilsl kthlyvggyd
     3421 rstvkvnrdv nitkgfdgci srlynfqkpv nlladikdaa niqscgetnm iggdedsdne
     3481 ppvppptpdv henelqpyam apcasdpcen ggscseqedv avcscpfgfs gkhcqehlql
     3541 gfnasfrgdg yvelnrshfq paleqsytsm givfttnkpn gllfwwgqea geeytgqdfi
     3601 aaavvdgyve ysmrldgeea virnsdirvd ngerhiviak rdentailev drmlhsgetr
     3661 ptskksmklp gnvfvggapd levftgfryk hnlngcivvv egetvgqinl ssaavngvna
     3721 nvcpanddpl ggteppvv