GIL_DROME
ID GIL_DROME Reviewed; 444 AA.
AC Q00805; Q8MQZ2; Q9VV64;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein giant-lens;
DE AltName: Full=Protein argos;
DE AltName: Full=Protein strawberry;
DE Flags: Precursor;
GN Name=aos; Synonyms=gil, sty; ORFNames=CG4531;
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], AND FUNCTION.
RC STRAIN=Oregon-R;
RX PubMed=1628618; DOI=10.1002/j.1460-2075.1992.tb05318.x;
RA Kretzschmar D., Brunner A., Wiersdorff V., Pflugfelder G.O., Heisenberg M.,
RA Schneuwly S.;
RT "Giant lens, a gene involved in cell determination and axon guidance in the
RT visual system of Drosophila melanogaster.";
RL EMBO J. 11:2531-2539(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=1606617; DOI=10.1016/0092-8674(92)90615-j;
RA Freeman M., Klambt C., Goodman C.S., Rubin G.M.;
RT "The argos gene encodes a diffusible factor that regulates cell fate
RT decisions in the Drosophila eye.";
RL Cell 69:963-975(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1286772; DOI=10.1111/j.1432-0436.1992.tb00494.x;
RA Okano H., Hayashi S., Tanimura T., Sawamoto K., Yoshikawa S., Watanabe J.,
RA Iwasaki M., Hirose S., Mikoshiba K., Montell C.;
RT "Regulation of Drosophila neural development by a putative secreted
RT protein.";
RL Differentiation 52:1-11(1992).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP FUNCTION.
RX PubMed=10200472; DOI=10.1038/sj.cdd.4400342;
RA Sawamoto K., Taguchi A., Hirota Y., Yamada C., Jin M.-H., Okano H.;
RT "Argos induces programmed cell death in the developing Drosophila eye by
RT inhibition of the Ras pathway.";
RL Cell Death Differ. 5:262-270(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH SPI.
RX PubMed=15329724; DOI=10.1038/nature02840;
RA Klein D.E., Nappi V.M., Reeves G.T., Shvartsman S.Y., Lemmon M.A.;
RT "Argos inhibits epidermal growth factor receptor signalling by ligand
RT sequestration.";
RL Nature 430:1040-1044(2004).
RN [9]
RP FUNCTION.
RX PubMed=15879554; DOI=10.1101/gad.1298105;
RA Wildonger J., Sosinsky A., Honig B., Mann R.S.;
RT "Lozenge directly activates argos and klumpfuss to regulate programmed cell
RT death.";
RL Genes Dev. 19:1034-1039(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 113-165 AND 285-444 ALONE AND IN
RP COMPLEX WITH SPITZ, REPEATS, AND DISULFIDE BONDS.
RX PubMed=18500331; DOI=10.1038/nature06978;
RA Klein D.E., Stayrook S.E., Shi F., Narayan K., Lemmon M.A.;
RT "Structural basis for EGFR ligand sequestration by Argos.";
RL Nature 453:1271-1275(2008).
CC -!- FUNCTION: Regulates cell determination; development of ommatidia and
CC optic lobe. Is a signaling molecule involved in the process of axon
CC pathfinding in the eye. Part of the Ras pathway regulating programmed
CC cell death in pupal eyes; activated by lozenge (lz). Antagonist for the
CC Egfr receptor (gurken). Inhibits Egfr signaling without interacting
CC directly with the receptor, but instead by sequestering the Egfr-
CC activating ligand spitz (spi). {ECO:0000269|PubMed:10200472,
CC ECO:0000269|PubMed:1286772, ECO:0000269|PubMed:15329724,
CC ECO:0000269|PubMed:15879554, ECO:0000269|PubMed:1606617,
CC ECO:0000269|PubMed:1628618}.
CC -!- SUBUNIT: Interacts with spi. {ECO:0000269|PubMed:15329724,
CC ECO:0000269|PubMed:18500331}.
CC -!- INTERACTION:
CC Q00805; Q00805: aos; NbExp=3; IntAct=EBI-596393, EBI-596393;
CC Q00805; Q01083: spi; NbExp=2; IntAct=EBI-596393, EBI-91342;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1606617}.
CC -!- TISSUE SPECIFICITY: During embryogenesis, expression is in a segmental
CC pattern in the ectoderm and in the nervous system. In the eye imaginal
CC disks, expression in photoreceptor cells begins a few rows posterior to
CC the morphogenetic furrow. Also expressed in the wing disk. In the
CC adult, expression is seen in the retina and lamina.
CC {ECO:0000269|PubMed:1286772}.
CC -!- DOMAIN: The three two-fingered repeats tightly encircle spi, providing
CC the basis for it's sequestration. The first repeat harbors a 120 AA
CC insert specific to drosophilidae.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit transformation of the eye mystery
CC cells, which are usually non-neuronal, into extra photoreceptors, and
CC supernumerary cone cells and pigment cells are also recruited. Mutants
CC also exhibit abnormal head involution, a change in a number of sensilla
CC in the antennomaxillary complex and abnormal morphogenesis of the
CC maxillary palp and wings in later stages. {ECO:0000269|PubMed:1606617}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM52736.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; X65161; CAA46279.1; -; mRNA.
DR EMBL; M91381; AAA28379.1; -; mRNA.
DR EMBL; S55367; AAB25390.1; -; mRNA.
DR EMBL; AE014296; AAF49458.2; -; Genomic_DNA.
DR EMBL; AY122224; AAM52736.1; ALT_SEQ; mRNA.
DR PIR; S22699; S22699.
DR RefSeq; NP_524107.2; NM_079383.3.
DR PDB; 3C9A; X-ray; 1.60 A; A/B=113-165, A/B=285-444.
DR PDB; 3CGU; X-ray; 2.51 A; A/B=113-165, A/B=285-444.
DR PDBsum; 3C9A; -.
DR PDBsum; 3CGU; -.
DR AlphaFoldDB; Q00805; -.
DR SMR; Q00805; -.
DR BioGRID; 65137; 59.
DR DIP; DIP-60630N; -.
DR IntAct; Q00805; 1.
DR STRING; 7227.FBpp0075166; -.
DR GlyGen; Q00805; 1 site.
DR PaxDb; Q00805; -.
DR EnsemblMetazoa; FBtr0075408; FBpp0075166; FBgn0004569.
DR GeneID; 39833; -.
DR KEGG; dme:Dmel_CG4531; -.
DR CTD; 100188340; -.
DR FlyBase; FBgn0004569; aos.
DR VEuPathDB; VectorBase:FBgn0004569; -.
DR eggNOG; ENOG502RZNS; Eukaryota.
DR HOGENOM; CLU_050120_0_0_1; -.
DR InParanoid; Q00805; -.
DR OMA; TEQVVHC; -.
DR OrthoDB; 1279794at2759; -.
DR PhylomeDB; Q00805; -.
DR SignaLink; Q00805; -.
DR BioGRID-ORCS; 39833; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; Q00805; -.
DR GenomeRNAi; 39833; -.
DR PRO; PR:Q00805; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004569; Expressed in anlage in statu nascendi and 74 other tissues.
DR Genevisible; Q00805; DM.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048019; F:receptor antagonist activity; IDA:FlyBase.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0001654; P:eye development; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0035215; P:genital disc development; IMP:FlyBase.
DR GO; GO:0007482; P:haltere development; IGI:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IDA:FlyBase.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:FlyBase.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IGI:FlyBase.
DR GO; GO:0060233; P:oenocyte delamination; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR InterPro; IPR021633; Argos.
DR Pfam; PF11581; Argos; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Disulfide bond; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Sensory transduction; Signal; Vision.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..444
FT /note="Protein giant-lens"
FT /id="PRO_0000021331"
FT REPEAT 123..165
FT /note="Two-fingered domain 1 part 1"
FT /evidence="ECO:0000269|PubMed:18500331"
FT REPEAT 285..307
FT /note="Two-fingered domain 1 part 2"
FT /evidence="ECO:0000269|PubMed:18500331"
FT REPEAT 316..370
FT /note="Two-fingered domain 2"
FT /evidence="ECO:0000269|PubMed:18500331"
FT REPEAT 378..444
FT /note="Two-fingered domain 3"
FT /evidence="ECO:0000269|PubMed:18500331"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..162
FT /evidence="ECO:0000269|PubMed:18500331"
FT DISULFID 147..285
FT /evidence="ECO:0000269|PubMed:18500331"
FT DISULFID 164..307
FT /evidence="ECO:0000269|PubMed:18500331"
FT DISULFID 316..341
FT /evidence="ECO:0000269|PubMed:18500331"
FT DISULFID 343..370
FT /evidence="ECO:0000269|PubMed:18500331"
FT DISULFID 378..405
FT /evidence="ECO:0000269|PubMed:18500331"
FT DISULFID 384..413
FT /evidence="ECO:0000269|PubMed:18500331"
FT DISULFID 407..440
FT /evidence="ECO:0000269|PubMed:18500331"
FT CONFLICT 282
FT /note="I -> V (in Ref. 6; AAM52736)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="T -> K (in Ref. 1; CAA46279, 2; AAA28379 and 3;
FT AAB25390)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="G -> D (in Ref. 1; CAA46279, 2; AAA28379 and 3;
FT AAB25390)"
FT /evidence="ECO:0000305"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:3C9A"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:3C9A"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3CGU"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:3C9A"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 347..356
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 383..393
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:3C9A"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:3C9A"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:3CGU"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:3C9A"
SQ SEQUENCE 444 AA; 49924 MW; 10F7D17D4ACDBC00 CRC64;
MPTTLMLLPC MLLLLLTAAA VAVGGTRLPL EVFEITPTTS TADKHKSLQY TVVYDAKDIS
GAAAATGVAS STVKPATEQL TVVSISSTAA AEKDLAESRR HARQMLQKQQ QHRSIIGGKH
GDRDVRILYQ VGDSEEDLPV CAPNAVCSKI DLYETPWIER QCRCPESNRM PNNVIIHHHS
HSSGSVDSLK YRNYYEREKM MQHKRMLLGE FQDKKFESLH MKKLMQKLGA VYEDDLDHLD
QSPDYNDALP YAEVQDNEFP RGSAHMRHSG HRGSKEPATT FIGGCPSSLG VEDGHTIADK
TRHYKMCQPV HKLPVCTHFR DYTWTLTTAA ELNVTEQIVH CRCPRNSVTY LTKREPIGNG
SPGYRYLFAC SPLTRLRCQR KQPCKLFTVR KRQEFLDEVN INSLCQCPKG HRCPSHHTQS
GVIAGESFLE DNIQTYSGYC MAND
