CRB_DROME
ID CRB_DROME Reviewed; 2146 AA.
AC P10040; Q0KI19; Q8MSX5; Q9VC97;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Protein crumbs;
DE AltName: Full=95F;
DE Flags: Precursor;
GN Name=crb; ORFNames=CG6383;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=2344615; DOI=10.1016/0092-8674(90)90189-l;
RA Tepass U., Theres C., Knust E.;
RT "Crumbs encodes an EGF-like protein expressed on apical membranes of
RT Drosophila epithelial cells and required for organization of epithelia.";
RL Cell 61:787-799(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1578-2146.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1661-1952.
RC TISSUE=Embryo;
RX PubMed=3107986; DOI=10.1002/j.1460-2075.1987.tb04818.x;
RA Knust E., Dietrich U., Tepass U., Bremer K.A., Weigel D., Vaessin H.,
RA Campos-Ortega J.A.;
RT "EGF homologous sequences encoded in the genome of Drosophila melanogaster,
RT and their relation to neurogenic genes.";
RL EMBO J. 6:761-766(1987).
RN [6]
RP FUNCTION, AND INTERACTION WITH PATJ.
RX PubMed=10102271; DOI=10.1016/s0092-8674(00)80593-0;
RA Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
RT "Discs Lost, a novel multi-PDZ domain protein, establishes and maintains
RT epithelial polarity.";
RL Cell 96:833-845(1999).
RN [7]
RP ERRATUM OF PUBMED:10102271.
RA Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
RL Cell 115:765-766(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PATJ.
RX PubMed=11076972; DOI=10.1083/jcb.151.4.891;
RA Tanentzapf G., Smith C., McGlade J., Tepass U.;
RT "Apical, lateral, and basal polarization cues contribute to the development
RT of the follicular epithelium during Drosophila oogenesis.";
RL J. Cell Biol. 151:891-904(2000).
RN [9]
RP IDENTIFICATION IN A SAC COMPLEX WITH PATJ AND SDT.
RX PubMed=11740560; DOI=10.1038/414638a;
RA Bachmann A., Schneider M., Theilenberg E., Grawe F., Knust E.;
RT "Drosophila Stardust is a partner of Crumbs in the control of epithelial
RT cell polarity.";
RL Nature 414:638-643(2001).
RN [10]
RP FUNCTION, AND INTERACTION WITH THE PAR-6 COMPLEX.
RX PubMed=12900452; DOI=10.1242/dev.00648;
RA Nam S.-C., Choi K.-W.;
RT "Interaction of Par-6 and Crumbs complexes is essential for photoreceptor
RT morphogenesis in Drosophila.";
RL Development 130:4363-4372(2003).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [12]
RP FUNCTION, INTERACTION WITH THE CGX COMPLEX, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25065591; DOI=10.1038/onc.2014.202;
RA Yeom E., Hong S.T., Choi K.W.;
RT "Crumbs interacts with Xpd for nuclear division control in Drosophila.";
RL Oncogene 34:2777-2789(2015).
RN [13]
RP FUNCTION, INTERACTION WITH APN, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=30645584; DOI=10.1371/journal.pgen.1007852;
RA Skouloudaki K., Papadopoulos D.K., Tomancak P., Knust E.;
RT "The apical protein Apnoia interacts with Crumbs to regulate tracheal
RT growth and inflation.";
RL PLoS Genet. 15:E1007852-E1007852(2019).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32579558; DOI=10.1371/journal.pgen.1008890;
RA Zelhof A.C., Mahato S., Liang X., Rylee J., Bergh E., Feder L.E.,
RA Larsen M.E., Britt S.G., Friedrich M.;
RT "The brachyceran de novo gene PIP82, a phosphorylation target of aPKC, is
RT essential for proper formation and maintenance of the rhabdomeric
RT photoreceptor apical domain in Drosophila.";
RL PLoS Genet. 16:e1008890-e1008890(2020).
CC -!- FUNCTION: Plays a central role in cell polarity establishment, and
CC contributes to the organization of zonula adherens, epithelial
CC morphogenesis, and tissue growth (PubMed:2344615, PubMed:12900452,
CC PubMed:10102271, PubMed:11740560). Participates in the assembly,
CC positioning and maintenance of adherens junctions via its interaction
CC with the SAC complex (PubMed:11740560, PubMed:12900452,
CC PubMed:10102271, PubMed:11076972). Controls the coalescence of the
CC spots of zonula adherens (ZA) into an adhesive ring around the cells
CC (PubMed:11740560). It may act as a signal (PubMed:2344615). Involved in
CC morphogenesis of the photoreceptor rhabdomere, for positioning and
CC growth of rhabdomere and AJ during the crucial period of photoreceptor
CC extension along the proximodistal axis of the retina (PubMed:12900452).
CC In cooperation with aPKC, required for the formation and maintenance of
CC the rhabdomeric and stalk apical cortical membrane domains
CC (PubMed:32579558). Recruits aPKC to the apical stalk membrane where it
CC phosphorylates and displaces rhabdomere specifying proteins such as
CC PIP82, to restrict their localization and thus activity to the
CC rhabdomeric apical domain (PubMed:32579558). Component of the crb-
CC galla-Xpd (CGX) complex which is essential for proper mitotic
CC chromosome segregation in early embryos (PubMed:25065591). The CGX
CC complex is also required for cell proliferation in developing wing
CC disks (PubMed:25065591). In the CGX complex, acts with galla-1 or
CC galla-2 to recruit Xpd and thus form the functional complex. Together
CC with apn, plays a key role in trachea development at larval stages
CC (PubMed:30645584). {ECO:0000269|PubMed:10102271,
CC ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:11740560,
CC ECO:0000269|PubMed:12900452, ECO:0000269|PubMed:2344615,
CC ECO:0000269|PubMed:25065591, ECO:0000269|PubMed:30645584,
CC ECO:0000269|PubMed:32579558}.
CC -!- SUBUNIT: Component of the SAC complex, a complex composed of crb, Patj
CC and sdt (PubMed:11740560, PubMed:10102271, PubMed:11076972). May
CC interact with the par-6 complex, which is composed of par-6, baz and
CC aPKC, via its interaction with Patj (PubMed:12900452, PubMed:10102271,
CC PubMed:11076972). Interacts with other proteins with Patj and sdt via
CC its short cytoplasmic tail (PubMed:11740560). Component of the CGX
CC complex composed of crb, galla (galla-1 or galla-2) and Xpd
CC (PubMed:25065591). Able to interact independently (via intracellular
CC domain) with galla-1, galla-2 and Xpd (PubMed:25065591). Interacts with
CC apn (PubMed:30645584). {ECO:0000269|PubMed:10102271,
CC ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:11740560,
CC ECO:0000269|PubMed:12900452, ECO:0000269|PubMed:25065591,
CC ECO:0000269|PubMed:30645584}.
CC -!- INTERACTION:
CC P10040; A1Z9X0: aPKC; NbExp=3; IntAct=EBI-672928, EBI-160861;
CC P10040; Q07436: ex; NbExp=2; IntAct=EBI-672928, EBI-192660;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:2344615,
CC ECO:0000269|PubMed:30645584, ECO:0000269|PubMed:32579558}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:11076972,
CC ECO:0000269|PubMed:2344615}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:25065591}. Note=Specifically localized to the
CC apical membrane (PubMed:11076972, PubMed:2344615, PubMed:32579558).
CC Expressed in a mesh punctate pattern that overlaps with metaphase
CC spindle microtubules (PubMed:25065591). In tracheal cells, colocalizes
CC with apn in the subapical region, a small region of the apical membrane
CC apical to the adherens junctions (PubMed:30645584). In photoreceptor
CC cells, enriched in the apical stalk membrane with some residual
CC expression in the rhabdomere membrane (PubMed:32579558).
CC {ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:2344615,
CC ECO:0000269|PubMed:25065591, ECO:0000269|PubMed:30645584,
CC ECO:0000269|PubMed:32579558}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P10040-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P10040-2; Sequence=VSP_031870;
CC -!- DEVELOPMENTAL STAGE: Expressed in the larval trachea (at protein
CC level). {ECO:0000269|PubMed:30645584}.
CC -!- PTM: Phosphorylated in the cytoplasmic domain. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Flies show severe disruptions in the organization
CC of ectodermally derived epithelia and leading in some cases to cell
CC death in these tissues (PubMed:2344615). RNAi-mediated knockdown in the
CC whole body or tracheae results in depletion of its binding partner sdt,
CC twisted tracheal tubes, lack of gas filling and reduced apical surfaces
CC of tracheal tube cells with death occurring at larval stage 2 or 3
CC (PubMed:30645584). RNAi-mediated knockdown in germline cells results in
CC severe chromosomal and spindle microtubule defects such as chromosome
CC bridges, bent chromosomes, monopolar spindles and fusion with one or
CC more neighboring spindles (PubMed:25065591).
CC {ECO:0000269|PubMed:2344615, ECO:0000269|PubMed:25065591,
CC ECO:0000269|PubMed:30645584}.
CC -!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM49878.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M33753; AAA28428.1; -; mRNA.
DR EMBL; AE014297; AAF56276.1; -; Genomic_DNA.
DR EMBL; AE014297; ABI31202.1; -; Genomic_DNA.
DR EMBL; AY118509; AAM49878.1; ALT_INIT; mRNA.
DR EMBL; X05144; CAA28793.1; -; mRNA.
DR PIR; A35672; A35672.
DR PIR; B26637; B26637.
DR RefSeq; NP_001036751.1; NM_001043286.2. [P10040-2]
DR RefSeq; NP_524480.2; NM_079756.3. [P10040-1]
DR PDB; 4WSI; X-ray; 2.95 A; X/Y=2110-2146.
DR PDB; 4YL8; X-ray; 1.50 A; B=2110-2146.
DR PDBsum; 4WSI; -.
DR PDBsum; 4YL8; -.
DR AlphaFoldDB; P10040; -.
DR SMR; P10040; -.
DR BioGRID; 67824; 59.
DR DIP; DIP-40915N; -.
DR IntAct; P10040; 9.
DR MINT; P10040; -.
DR STRING; 7227.FBpp0293268; -.
DR TCDB; 9.B.87.1.11; the selenoprotein p receptor (selp-receptor) family.
DR GlyGen; P10040; 35 sites.
DR iPTMnet; P10040; -.
DR PaxDb; P10040; -.
DR PRIDE; P10040; -.
DR EnsemblMetazoa; FBtr0084603; FBpp0083987; FBgn0259685. [P10040-1]
DR EnsemblMetazoa; FBtr0111008; FBpp0110307; FBgn0259685. [P10040-2]
DR GeneID; 42896; -.
DR KEGG; dme:Dmel_CG6383; -.
DR CTD; 42896; -.
DR FlyBase; FBgn0259685; crb.
DR VEuPathDB; VectorBase:FBgn0259685; -.
DR HOGENOM; CLU_000827_0_0_1; -.
DR InParanoid; P10040; -.
DR OMA; NCELNLN; -.
DR PhylomeDB; P10040; -.
DR SignaLink; P10040; -.
DR BioGRID-ORCS; 42896; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42896; -.
DR PRO; PR:P10040; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0259685; Expressed in wing disc and 27 other tissues.
DR ExpressionAtlas; P10040; baseline and differential.
DR Genevisible; P10040; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0035003; C:subapical complex; TAS:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0005080; F:protein kinase C binding; IPI:FlyBase.
DR GO; GO:0030507; F:spectrin binding; TAS:FlyBase.
DR GO; GO:0034332; P:adherens junction organization; IMP:FlyBase.
DR GO; GO:0046665; P:amnioserosa maintenance; IMP:FlyBase.
DR GO; GO:0003383; P:apical constriction; IMP:FlyBase.
DR GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR GO; GO:0106036; P:assembly of apicomedial cortex actomyosin; IMP:FlyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0061336; P:cell morphogenesis involved in Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IMP:FlyBase.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:FlyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:FlyBase.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IMP:FlyBase.
DR GO; GO:0035002; P:liquid clearance, open tracheal system; IGI:FlyBase.
DR GO; GO:0035090; P:maintenance of apical/basal cell polarity; IMP:FlyBase.
DR GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0061024; P:membrane organization; IMP:FlyBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:FlyBase.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IGI:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0098813; P:nuclear chromosome segregation; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR GO; GO:0045570; P:regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0033157; P:regulation of intracellular protein transport; IMP:FlyBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0061541; P:rhabdomere morphogenesis; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0060438; P:trachea development; IGI:UniProtKB.
DR GO; GO:0035239; P:tube morphogenesis; IMP:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0045186; P:zonula adherens assembly; IMP:FlyBase.
DR GO; GO:0045218; P:zonula adherens maintenance; IMP:FlyBase.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 17.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00181; EGF; 28.
DR SMART; SM00179; EGF_CA; 23.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; SSF49899; 4.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 16.
DR PROSITE; PS00022; EGF_1; 25.
DR PROSITE; PS01186; EGF_2; 17.
DR PROSITE; PS50026; EGF_3; 27.
DR PROSITE; PS01187; EGF_CA; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Cell membrane; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Mitosis; Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..88
FT CHAIN 89..2146
FT /note="Protein crumbs"
FT /id="PRO_0000007499"
FT TOPO_DOM 89..2082
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2083..2109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2110..2146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 265..301
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 304..341
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 346..384
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 386..423
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 425..461
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 462..498
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 543..579
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 609..644
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 646..683
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 685..721
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 723..759
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 761..798
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 800..836
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 838..900
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 902..938
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 940..976
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 978..1019
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1021..1203
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1205..1241
FT /note="EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1248..1483
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1479..1515
FT /note="EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1555..1757
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1758..1792
FT /note="EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1794..1830
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1832..1868
FT /note="EGF-like 22; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1871..1909
FT /note="EGF-like 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1912..1948
FT /note="EGF-like 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1950..1987
FT /note="EGF-like 25; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1989..2027
FT /note="EGF-like 26; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2028..2068
FT /note="EGF-like 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 1112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1891
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2027
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2033
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 269..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 274..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 291..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 308..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 313..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 331..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 350..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 355..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 374..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 390..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 395..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 412..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 429..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 434..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 451..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 466..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 471..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 488..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 547..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 554..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 569..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 611..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 616..632
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 634..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 650..662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 657..671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 673..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 689..700
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 694..709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 711..720
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 727..738
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 732..747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 749..758
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 765..776
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 770..785
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 787..797
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 804..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 809..824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 826..835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 842..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 847..888
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 890..899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 906..917
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 911..926
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 928..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 944..955
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 950..964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 966..975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 982..993
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 987..1007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1009..1018
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1171..1203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1209..1220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1214..1229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1231..1240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1483..1494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1488..1503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1505..1514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1713..1757
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1760..1771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1765..1780
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1782..1791
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1798..1809
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1803..1818
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1820..1829
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1836..1847
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1841..1856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1858..1867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1875..1886
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1880..1900
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1916..1927
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1921..1936
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1938..1947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1954..1965
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1959..1974
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1976..1986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1993..2006
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2000..2015
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2017..2026
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2032..2044
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2038..2056
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2058..2067
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 526
FT /note="G -> ASDMEPLTPLELDILDATLCPSEKKKRYISPEWLKRKRCELKLS
FT (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_031870"
FT CONFLICT 1661..1673
FT /note="VDPTPAFSTDIDQ -> WWIRRQLFPRTSTK (in Ref. 5;
FT CAA28793)"
FT /evidence="ECO:0000305"
FT CONFLICT 1719
FT /note="V -> L (in Ref. 1; AAA28428)"
FT /evidence="ECO:0000305"
FT CONFLICT 1952
FT /note="N -> K (in Ref. 5; CAA28793)"
FT /evidence="ECO:0000305"
FT STRAND 2116..2119
FT /evidence="ECO:0007829|PDB:4YL8"
FT TURN 2121..2123
FT /evidence="ECO:0007829|PDB:4YL8"
FT HELIX 2131..2135
FT /evidence="ECO:0007829|PDB:4WSI"
SQ SEQUENCE 2146 AA; 233572 MW; 8E23B9E32B761115 CRC64;
MAKIANASLS QQQKQRQAET ATTTTTTVAA SVETATTTAR SRDRTKSAAQ ITSHLLKRAI
SVYSSPQWIP LFILIYLATD VASVAVPTKE AYFNGSTYLR LTTPMPIWDH SAISFRSCRG
GEILAQQYNK NSIVISVLND FLQISLAGPA VHGPNNRLDV KLPYQLLDNR WHTLQFKYEY
GNLYLHVDRA ASIFANSTYN SQFLTNQDIG YKDAILILGN SFSGCLLDGP GLQFVNNSTV
QNVVFGHCPL TPGPCSDHDL FTRLPDNFCL NDPCMGHGTC SSSPEGYECR CTARYSGKNC
QKDNGSPCAK NPCENGGSCL ENSRGDYQCF CDPNHSGQHC ETEVNIHPLC QTNPCLNNGA
CVVIGGSGAL TCECPKGYAG ARCEVDTDEC ASQPCQNNGS CIDRINGFSC DCSGTGYTGA
FCQTNVDECD KNPCLNGGRC FDTYGWYTCQ CLDGWGGEIC DRPMTCQTQQ CLNGGTCLDK
PIGFQCLCPP EYTGELCQIA PSCAQQCPID SECVGGKCVC KPGSSGYNCQ TSTGDGASAL
ALTPINCNAT NGKCLNGGTC SMNGTHCYCA VGYSGDRCEK AENCSPLNCQ EPMVCVQNQC
LCPENKVCNQ CATQPCQNGG ECVDLPNGDY ECKCTRGWTG RTCGNDVDEC TLHPKICGNG
ICKNEKGSYK CYCTPGFTGV HCDSDVDECL SFPCLNGATC HNKINAYECV CQPGYEGENC
EVDIDECGSN PCSNGSTCID RINNFTCNCI PGMTGRICDI DIDDCVGDPC LNGGQCIDQL
GGFRCDCSGT GYEGENCELN IDECLSNPCT NGAKCLDRVK DYFCDCHNGY KGKNCEQDIN
ECESNPCQYN GNCLERSNIT LYQMSRITDL PKVFSQPFSF ENASGYECVC VPGIIGKNCE
ININECDSNP CSKHGNCNDG IGTYTCECEP GFEGTHCEIN IDECDRYNPC QRGTCYDQID
DYDCDCDANY GGKNCSVLLK GCDQNPCLNG GACLPYLINE VTHLYNCTCE NGFQGDKCEK
TTTLSMVATS LISVTTEREE GYDINLQFRT TLPNGVLAFG TTGEKNEPVS YILELINGRL
NLHSSLLNKW EGVFIGSKLN DSNWHKVFVA INTSHLVLSA NDEQAIFPVG SYETANNSQP
SFPRTYLGGT IPNLKSYLRH LTHQPSAFVG CMQDIMVNGK WIFPDEQDAN ISYTKLENVQ
SGCPRTEQCK PNPCHSNGEC TDLWHTFACH CPRPFFGHTC QHNMTAATFG HENTTHSAVI
VETTDVARRA IRSILDISMF IRTREPTGQV FYLGTDPRKA PTKNIGDSYV AAKLHGGELL
VKMQFSGTPE AYTVGGQKLD NGYNHLIEVV RNQTLVQVKL NGTEYFRKTL STTGLLDAQV
LYLGGPAPTR ESLLGATTEP GIIPVPGAGI PIEDTTVPKE ADDSRDYFKG IIQDVKVSNG
SLNLIVEMYS LNVTDVQVNA KPLGAVTIDR ASVLPGEVSD DLCRKNPCLH NAECRNTWND
YTCKCPNGYK GKNCQEIEFC QHVTCPGQSL CQNLDDGYEC VTNTTFTGQE RSPLAFFYFQ
EQQSDDIVSE ASPKQTLKPV IDIAFRTRAG GTLLYIDNVD GFFEIGVNGG RVTITWKLSA
LHFGESARFE KENTDGEWSR IYLRAHNSKL EGGWKGWESM VDPTPAFSTD IDQAAFQSLI
ATSTQVYLGG MPESRQARGS TLSAQQGSQF KGCVGEARVG DLLLPYFSMA ELYSRTNVSV
QQKAQFRLNA TRPEEGCILC FQSDCKNDGF CQSPSDEYAC TCQPGFEGDD CGTDIDECLN
TECLNNGTCI NQVAAFFCQC QPGFEGQHCE QNIDECADQP CHNGGNCTDL IASYVCDCPE
DYMGPQCDVL KQMTCENEPC RNGSTCQNGF NASTGNNFTC TCVPGFEGPL CDIPFCEITP
CDNGGLCLTT GAVPMCKCSL GYTGRLCEQD INECESNPCQ NGGQCKDLVG RYECDCQGTG
FEGIRCENDI DECNMEGDYC GGLGRCFNKP GSFQCICQKP YCGAYCNFTD PCNATDLCSN
GGRCVESCGA KPDYYCECPE GFAGKNCTAP ITAKEDGPST TDIAIIVIPV VVVLLLIAGA
LLGTFLVMAR NKRATRGTYS PSAQEYCNPR LEMDNVLKPP PEERLI
