EYS_DROME
ID EYS_DROME Reviewed; 2176 AA.
AC A0A1F4; Q06PM7; Q400N0; Q6IHY1; Q8MRJ7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein eyes shut;
DE AltName: Full=Protein spacemaker;
GN Name=eys {ECO:0000312|EMBL:ABJ09588.1, ECO:0000312|FlyBase:FBgn0031414};
GN Synonyms=spam {ECO:0000312|EMBL:ABH07112.1}; ORFNames=CG33955;
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] {ECO:0000305, ECO:0000312|EMBL:ABJ09588.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF GLU-521.
RX PubMed=17011488; DOI=10.1016/j.devcel.2006.08.012;
RA Husain N., Pellikka M., Hong H., Klimentova T., Choe K.-M., Clandinin T.R.,
RA Tepass U.;
RT "The agrin/perlecan-related protein eyes shut is essential for epithelial
RT lumen formation in the Drosophila retina.";
RL Dev. Cell 11:483-493(2006).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABH07112.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-2176, FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17036004; DOI=10.1038/nature05128;
RA Zelhof A.C., Hardy R.W., Becker A., Zuker C.S.;
RT "Transforming the architecture of compound eyes.";
RL Nature 443:696-699(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [4] {ECO:0000305}
RP GENOME REANNOTATION.
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAM50220.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1660-2176.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50220.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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 [6] {ECO:0000305, ECO:0000312|EMBL:DAA03484.1}
RP IDENTIFICATION.
RX PubMed=14709175; DOI=10.1186/gb-2003-5-1-r3;
RA Hild M., Beckmann B., Haas S.A., Koch B., Solovyev V., Busold C.,
RA Fellenberg K., Boutros M., Vingron M., Sauer F., Hoheisel J.D., Paro R.;
RT "An integrated gene annotation and transcriptional profiling approach
RT towards the full gene content of the Drosophila genome.";
RL Genome Biol. 5:R3.1-R3.17(2003).
RN [7] {ECO:0000305}
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1471, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head {ECO:0000269|PubMed:17893096};
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).
CC -!- FUNCTION: Essential for the formation of matrix-filled interrhabdomeral
CC space: critical for the formation of epithelial lumina in the retina.
CC Acts together with prominin (prom) and the cell adhesion molecule
CC chaoptin (chp) to choreograph the partitioning of rhabdomeres into an
CC open system. {ECO:0000269|PubMed:17011488,
CC ECO:0000269|PubMed:17036004}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:17011488,
CC ECO:0000269|PubMed:17036004}. Note=Secreted by photoreceptor cells,
CC through the stalk membrane into the interrhabdomeral space (IRS).
CC Although secreted, lacks a canonical signal sequence and contains a
CC predicted transmembrane domain. The discrepancy may be explained by
CC protein cleavage after the transmembrane region.
CC -!- TISSUE SPECIFICITY: Expressed from the beginning of rhabdomere
CC biogenesis (48 hours after pupal formation), when it decorates the
CC entire photoreceptor apical surface. {ECO:0000269|PubMed:17036004}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic, larval, and adult
CC stages. {ECO:0000269|PubMed:17011488}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit a closed rhabdomere system,
CC rhabdomeres within each ommatidium are fused to each other.
CC {ECO:0000269|PubMed:17036004}.
CC -!- SIMILARITY: Belongs to the EYS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DAA03484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ991915; ABJ09588.1; -; mRNA.
DR EMBL; DQ780942; ABH07112.1; -; mRNA.
DR EMBL; AE014134; AAZ83988.3; -; Genomic_DNA.
DR EMBL; AY119566; AAM50220.1; -; mRNA.
DR EMBL; BK003285; DAA03484.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001027571.3; NM_001032399.3.
DR RefSeq; NP_001259924.2; NM_001272995.1.
DR AlphaFoldDB; A0A1F4; -.
DR BioGRID; 533487; 3.
DR STRING; 7227.FBpp0112919; -.
DR GlyGen; A0A1F4; 12 sites.
DR iPTMnet; A0A1F4; -.
DR PaxDb; A0A1F4; -.
DR PRIDE; A0A1F4; -.
DR EnsemblMetazoa; FBtr0344662; FBpp0311004; FBgn0031414.
DR EnsemblMetazoa; FBtr0344663; FBpp0311005; FBgn0031414.
DR GeneID; 3771890; -.
DR KEGG; dme:Dmel_CG33955; -.
DR CTD; 346007; -.
DR FlyBase; FBgn0031414; eys.
DR VEuPathDB; VectorBase:FBgn0031414; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR HOGENOM; CLU_002251_0_0_1; -.
DR InParanoid; A0A1F4; -.
DR OMA; CRDRNNG; -.
DR OrthoDB; 115967at2759; -.
DR PhylomeDB; A0A1F4; -.
DR BioGRID-ORCS; 3771890; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 3771890; -.
DR PRO; PR:A0A1F4; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031414; Expressed in brain and 9 other tissues.
DR ExpressionAtlas; A0A1F4; baseline and differential.
DR Genevisible; A0A1F4; DM.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0031012; C:extracellular matrix; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097730; C:non-motile cilium; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:UniProtKB.
DR GO; GO:0010378; P:temperature compensation of the circadian clock; IMP:FlyBase.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00179; EGF_CA; 10.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; SSF49899; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 13.
DR PROSITE; PS01187; EGF_CA; 4.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Transmembrane; Transmembrane helix.
FT CHAIN 1..2176
FT /note="Protein eyes shut"
FT /id="PRO_0000339236"
FT TOPO_DOM 1..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..2176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 144..180
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 182..218
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 220..256
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 258..298
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 300..336
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 338..374
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 376..413
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1018..1054
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1059..1266
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1309..1346
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1353..1549
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1545..1581
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1583..1621
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1692..1879
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1875..1912
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1913..1946
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1952..2166
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 429..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2080..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2084..2101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 1665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1861
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2035
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2099
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 148..158
FT /evidence="ECO:0000255"
FT DISULFID 153..168
FT /evidence="ECO:0000255"
FT DISULFID 170..179
FT /evidence="ECO:0000255"
FT DISULFID 186..197
FT /evidence="ECO:0000255"
FT DISULFID 191..206
FT /evidence="ECO:0000255"
FT DISULFID 208..217
FT /evidence="ECO:0000255"
FT DISULFID 224..235
FT /evidence="ECO:0000255"
FT DISULFID 229..244
FT /evidence="ECO:0000255"
FT DISULFID 246..255
FT /evidence="ECO:0000255"
FT DISULFID 262..276
FT /evidence="ECO:0000255"
FT DISULFID 270..286
FT /evidence="ECO:0000255"
FT DISULFID 288..297
FT /evidence="ECO:0000255"
FT DISULFID 304..315
FT /evidence="ECO:0000255"
FT DISULFID 309..324
FT /evidence="ECO:0000255"
FT DISULFID 326..335
FT /evidence="ECO:0000255"
FT DISULFID 342..353
FT /evidence="ECO:0000255"
FT DISULFID 347..362
FT /evidence="ECO:0000255"
FT DISULFID 364..373
FT /evidence="ECO:0000255"
FT DISULFID 380..392
FT /evidence="ECO:0000255"
FT DISULFID 386..401
FT /evidence="ECO:0000255"
FT DISULFID 403..412
FT /evidence="ECO:0000255"
FT DISULFID 1022..1033
FT /evidence="ECO:0000255"
FT DISULFID 1027..1042
FT /evidence="ECO:0000255"
FT DISULFID 1044..1053
FT /evidence="ECO:0000255"
FT DISULFID 1313..1324
FT /evidence="ECO:0000255"
FT DISULFID 1318..1334
FT /evidence="ECO:0000255"
FT DISULFID 1336..1345
FT /evidence="ECO:0000255"
FT DISULFID 1549..1560
FT /evidence="ECO:0000255"
FT DISULFID 1554..1569
FT /evidence="ECO:0000255"
FT DISULFID 1571..1580
FT /evidence="ECO:0000255"
FT DISULFID 1587..1600
FT /evidence="ECO:0000255"
FT DISULFID 1594..1609
FT /evidence="ECO:0000255"
FT DISULFID 1611..1620
FT /evidence="ECO:0000255"
FT DISULFID 1879..1890
FT /evidence="ECO:0000255"
FT DISULFID 1884..1900
FT /evidence="ECO:0000255"
FT DISULFID 1902..1911
FT /evidence="ECO:0000255"
FT DISULFID 1917..1928
FT /evidence="ECO:0000255"
FT DISULFID 1922..1934
FT /evidence="ECO:0000255"
FT DISULFID 1936..1945
FT /evidence="ECO:0000255"
FT MUTAGEN 521
FT /note="E->K: In eys(734); fails to form an interrhabdomeral
FT space."
FT /evidence="ECO:0000269|PubMed:17011488"
SQ SEQUENCE 2176 AA; 234104 MW; 7C21E204FCF3E311 CRC64;
MSNVHQFDTQ TMAESPQIRR DMGRLCATWP SKDSEDGAGT ALRAATPLTA NGATTTGLSV
TLAPKDMQRN HLLKMPTATI EKPTITATIA SSSSTSTSTT RKSVTATRSL KLNPNILLPT
LRILARGLLL PALILAILVG SSQAGFACLS NPCVFGVCID GLNSSYSCYC IDGYTGIQCQ
TNWDECWSSP CQNGGTCVDG VAYYNCTCPE GFSGSNCEEN VDECMSNPCQ NGGLCRDRTN
GYICTCQPGY LGSHCELDVA VCETGTGARC QHGGECIEGP GLEFTCDCPA GWHGRICQEE
INECASSPCQ NGGVCVDKLA AYACACPMGY TGINCEEEIL ICADNPCQNN ALCLMEEGVP
TCYCVPDYHG EKCEFQYDEC QLGPRCMNGG VCIDGVDTFS CSCPPLLTGM LCECLMVGEE
SLDCNYTAPA TQSPPRRTTT TSTMAPPTVR PVTPPETTVS PSRASEEVEI IVVTTSAPAE
VVTSVLSPSS SSSSSEEGVS VEIKTPTVAP PESGSHSISV EQTTAVPAQP EPESEQEPES
KPHPESESAS ESETETEEEI IPGTTARPPT SRSSSSSEES PSIFTTLPPL PGKPQTSASS
ESSGEVVTSE EYTTVPHFEV SGSKSESGSE EVTTVRPTAA PSITISVDIT SSGSSSSSSE
SVEVFTTPAP VFVQRVTTIE TSISIDYVTP TPLPETTTPR VVPVPRPTFA PEPPLDVVET
TASTHHLWTE VPTTAAPFFT EYPAEVLITT HRTSAGRFTT VQPPAGVTTT SPTEDSSVEL
PTPHTPQIVV TILDSNEVIP SLITTTGSPT THHHHHHHPH HEAEGTTLQP LEEDEHHHHH
HHDEFTTPQP VEITTGHPLQ TEDLIGVQEP AVVTTESPFA PAETTVVPVV VPATIAPLGT
AAPPATPAPV PPATTTPPPS PPSLATETPT LPPTLPPVTL PPVTQPPPTI PPTPPSTQSA
QTLPPPTSAI NVYTTPDGPP TASQTKPSVT ESSEEVEGTN TVSTGGRGSG GVPEEKAGDV
DCIKLGCYNG GTCVTTSEGS RCVCRFDRQG PLCELPIIIR NAAFSGDSYV SHRIYKDIGG
HESLDAVLPM HIQLKVRTRA TNGLIMLAAA QGTKGGHYMA LFLQKGLMQF QFSCGLQTML
LSELETPVNT GHEITIRAEL DFSRNYTHCN ASLLVNDTLA MSGDQPTWLK LLPPRLHTPE
AILNTWLHLG GAPQAPIGLI IELPPAQSGS GFTGCLHTLR INGQAREIFG DALDGFGITE
CGSLACLSSP CRNGAACIKI ETNDLDENGE KAEKWKCKCP TGYMGPTCEI SVCEDNPCQY
GGTCVQFPGS GYLCLCPLGK HGHYCEHNLE VALPSFSGSV NGLSSFVAYT VPIPLEYSLE
LSFKILPQTM SQISLLAFFG QSGYHDEKSD HLAVSFIQGY IMLTWNLGAG PRRIFTQKPI
DFRLDAPRVP YEIKVGRIGR QAWLSVDGKF NITGRSPGSG SRMDVLPILY LGGHEIANFN
TLPHDLPLHS GFQGCIYDVQ LKAGQVTVPL QETRGVRGRG VGQCGTRECH RHACQHDGAC
LQHGATFTCI CQEGWYGPLC AQPTNPCDSF NNKCYEDATC VPLVNGYECD CPVGRTGKNC
EEVIRSLSDV SLTGRRSYLA VRWPYLYDGG DKLGAKRSQM VSYRNFTKKL MPPKPITTPS
SHFVMKLLNE VEKQRSFSPV PLMGSKSFEE HHRVQFFFIE FQLRPLSERG LLLYFGTLNN
NQDKKIGFVS LSLQGGVVEF RISGPSNHVT VVRSVRMLAI GEWHKIKMAQ RGRWLTLWVE
GSASSALAPS AEVLVEPDSL LYIGGLKDVS KLPHNAISGF PIPFRGCVRG LVVSGTRIVL
NETNIVESRN IRDCDGTACG GDSCESGGHC WLDEKLQPHC ICPEYAKGDR CEYSETCKLI
PCKNNGRCLR SGRCSCPNGW GGFYCEIAMS KPTTPSFRGN SYLILPPPRI PMKDKRRGPS
LYVRPREAIQ VSLNFSTIEP DGLLLWSEHE RSKFLGLGLE AGHLKLASNL LGSTNDTVRA
PASGFIADGA WHWTSVLLDR SRLELQLDGE VIFTERLPEG GRSLGSTTPR STLAGRRKNS
SKEPTISYED VFYLGGFPNS DSVSRRTKGR FFDPFKGCLQ DIQFGAEPTA IISDFSTYQG
ENIGSCDLHG DEPLTV
