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Integrin beta-PS (Position-specific antigen beta subunit) (Protein myospheroid) (Protein olfactory C)

 ITBX_DROME              Reviewed;         846 AA.
P11584; Q8MYX9; Q9W3L2;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
20-JUN-2003, sequence version 3.
27-SEP-2017, entry version 191.
RecName: Full=Integrin beta-PS;
AltName: Full=Position-specific antigen beta subunit;
AltName: Full=Protein myospheroid;
AltName: Full=Protein olfactory C;
Flags: Precursor;
Name=mys; Synonyms=l(1)mys, olfC; ORFNames=CG1560;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3128792; DOI=10.1073/pnas.85.8.2633;
Mackrell A.J., Blumberg B., Haynes S.R., Fessler J.H.;
"The lethal myospheroid gene of Drosophila encodes a membrane protein
homologous to vertebrate integrin beta subunits.";
Proc. Natl. Acad. Sci. U.S.A. 85:2633-2637(1988).
[2]
NUCLEOTIDE SEQUENCE, FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
ASP-807; PHE-811; PHE-814; GLU-817; TYR-831 AND TYR-843.
TISSUE=Embryo, and Imaginal disk;
PubMed=8119134;
Grinblat Y., Zusman S., Yee G., Hynes R.O., Kafatos F.C.;
"Functions of the cytoplasmic domain of the beta PS integrin subunit
during Drosophila development.";
Development 120:91-102(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
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.A., 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.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., 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.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
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., Woodage T., 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.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., 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.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION.
PubMed=7924982;
Fogerty F.J., Fessler L.I., Bunch T.A., Yaron Y., Parker C.G.,
Nelson R.E., Brower D.L., Gullberg D., Fessler J.H.;
"Tiggrin, a novel Drosophila extracellular matrix protein that
functions as a ligand for Drosophila alpha PS2 beta PS integrins.";
Development 120:1747-1758(1994).
[7]
FUNCTION.
PubMed=7972082; DOI=10.1073/pnas.91.24.11447;
Gotwals P.J., Fessler L.I., Wehrli M., Hynes R.O.;
"Drosophila PS1 integrin is a laminin receptor and differs in ligand
specificity from PS2.";
Proc. Natl. Acad. Sci. U.S.A. 91:11447-11451(1994).
[8]
FUNCTION.
PubMed=9660786; DOI=10.1074/jbc.273.29.18235;
Graner M.W., Bunch T.A., Baumgartner S., Kerschen A., Brower D.L.;
"Splice variants of the Drosophila PS2 integrins differentially
interact with RGD-containing fragments of the extracellular proteins
tiggrin, ten-m, and D-laminin 2.";
J. Biol. Chem. 273:18235-18241(1998).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10821184; DOI=10.1007/s004380051194;
Ayyub C., Rodrigues V., Hasan G., Siddiqi O.;
"Genetic analysis of olfC demonstrates a role for the position-
specific integrins in the olfactory system of Drosophila
melanogaster.";
Mol. Gen. Genet. 263:498-504(2000).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15469969; DOI=10.1242/dev.01427;
Devenport D., Brown N.H.;
"Morphogenesis in the absence of integrins: mutation of both
Drosophila beta subunits prevents midgut migration.";
Development 131:5405-5415(2004).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-403; ASN-557 AND ASN-718,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Oregon-R; TISSUE=Head;
PubMed=17893096; DOI=10.1093/glycob/cwm097;
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
Panin V.;
"Identification of N-glycosylated proteins from the central nervous
system of Drosophila melanogaster.";
Glycobiology 17:1388-1403(2007).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19035354; DOI=10.1002/dvdy.21802;
Dinkins M.B., Fratto V.M., Lemosy E.K.;
"Integrin alpha chains exhibit distinct temporal and spatial
localization patterns in epithelial cells of the Drosophila ovary.";
Dev. Dyn. 237:3927-3939(2008).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-266; ASN-403; ASN-557 AND
ASN-718, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=27191715; DOI=10.1371/journal.pgen.1006043;
Lee J.Y., Chen J.Y., Shaw J.L., Chang K.T.;
"Maintenance of stem cell niche integrity by a novel activator of
integrin signaling.";
PLoS Genet. 12:E1006043-E1006043(2016).
-!- FUNCTION: Integrin alpha-PS1/beta-PS is a receptor for laminin
(PubMed:7972082). Integrin alpha-PS2/beta-PS is a receptor for
Tig, wb and Ten-m (PubMed:7924982, PubMed:7972082,
PubMed:9660786). Contributes to endodermal integrity and adhesion
between the midgut epithelium and the surrounding visceral muscle
(PubMed:15469969). Essential for migration of the primordial
midgut cells and for maintaining, but not establishing, cell
polarity in the midgut epithelium (PubMed:15469969). The two beta
subunits mediate midgut migration by distinct mechanisms: beta-PS
requires rhea/talin and Itgbn does not (PubMed:15469969). Required
for rhea/talin correct cellular localization in the midgut
(PubMed:15469969). Required for many embryonic (dorsal closure and
somatic muscle attachments) and postembryonic developmental
processes (attachment between cell layers of imaginal disks,
organization of ommatidial arrays and flight muscle development)
(PubMed:8119134, PubMed:7924982, PubMed:7972082, PubMed:10821184).
Involved in the function and/or development of the olfactory
system (PubMed:10821184). In the testes, essential for shv-
dependent maintenance of somatic hub cells and their localization
to the apical tip (PubMed:27191715). Plays a role in timely border
cell migration during oogenesis (PubMed:19035354).
{ECO:0000269|PubMed:10821184, ECO:0000269|PubMed:15469969,
ECO:0000269|PubMed:19035354, ECO:0000269|PubMed:27191715,
ECO:0000269|PubMed:7924982, ECO:0000269|PubMed:7972082,
ECO:0000269|PubMed:8119134, ECO:0000269|PubMed:9660786}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-PS
associates with either alpha-PS1, alpha-PS2, alpha-PS3, alpha-PS4
or alpha-PS5.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Lateral cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Basal cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Note=In ovary, localizes to the
apical, lateral and basal membranes of follicle cells through
oogenesis stage 10A. Apical membrane expression peaks at oogenesis
stages 9 and 10A in columnar follicle cells overlying the oocyte
but decreases in the most posterior follicle cells. Thereafter, it
is down-regulated. Localization to lateral and basal membranes
persists during dorsal appendage morphogenesis.
-!- TISSUE SPECIFICITY: In ovaries, strongly expressed in follicle
cells (PubMed:19035354). In oocytes, expressed in the forming
dorsal appendages (at protein level) (PubMed:19035354). Expressed
in the embryonic dorsal cuticle, the larval eye and the wing
imaginal disk (PubMed:8119134). In testes, detected at the
interface between somatic hub cells and cyst stem cells
(PubMed:27191715). {ECO:0000269|PubMed:19035354,
ECO:0000269|PubMed:27191715, ECO:0000269|PubMed:8119134}.
-!- DISRUPTION PHENOTYPE: In zygotic mutant embryos, midgut forms
primary constrictions but fails to elongate and the visceral
muscle does not flatten but remains attached to the midgut
epithelium. Embryos lacking maternal and zygotic mys show a delay
in midgut migration. Mutant larvae present an olfactory phenotype,
showing reduced response to isoamyl acetate but normal response to
ethyl acetate. {ECO:0000269|PubMed:10821184,
ECO:0000269|PubMed:15469969}.
-!- MISCELLANEOUS: The absence of the beta-PS subunit results in
detachment and rounding up of the muscles, thus the gene encoding
beta-PS is called myospheroid.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
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EMBL; J03251; AAA28714.1; -; mRNA.
EMBL; AE014298; AAF46313.2; -; Genomic_DNA.
EMBL; AY113499; AAM29504.1; -; mRNA.
PIR; A30889; A30889.
RefSeq; NP_001284998.1; NM_001298069.1.
RefSeq; NP_001284999.1; NM_001298070.1.
RefSeq; NP_524793.2; NM_080054.3.
UniGene; Dm.1814; -.
ProteinModelPortal; P11584; -.
SMR; P11584; -.
BioGrid; 69357; 44.
IntAct; P11584; 3.
STRING; 7227.FBpp0071061; -.
PaxDb; P11584; -.
PRIDE; P11584; -.
EnsemblMetazoa; FBtr0071105; FBpp0071061; FBgn0004657.
EnsemblMetazoa; FBtr0340136; FBpp0309122; FBgn0004657.
EnsemblMetazoa; FBtr0340137; FBpp0309123; FBgn0004657.
GeneID; 44885; -.
KEGG; dme:Dmel_CG1560; -.
CTD; 44885; -.
FlyBase; FBgn0004657; mys.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
InParanoid; P11584; -.
KO; K05719; -.
OMA; FFDEDDC; -.
OrthoDB; EOG091G029W; -.
PhylomeDB; P11584; -.
Reactome; R-DME-1566948; Elastic fibre formation.
Reactome; R-DME-1566977; Fibronectin matrix formation.
Reactome; R-DME-202733; Cell surface interactions at the vascular wall.
Reactome; R-DME-210991; Basigin interactions.
Reactome; R-DME-2129379; Molecules associated with elastic fibres.
Reactome; R-DME-216083; Integrin cell surface interactions.
Reactome; R-DME-3000170; Syndecan interactions.
Reactome; R-DME-445144; Signal transduction by L1.
Reactome; R-DME-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
Reactome; R-DME-6798695; Neutrophil degranulation.
ChiTaRS; mys; fly.
GenomeRNAi; 44885; -.
PRO; PR:P11584; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0004657; -.
ExpressionAtlas; P11584; differential.
Genevisible; P11584; DM.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
GO; GO:0043034; C:costamere; IDA:FlyBase.
GO; GO:0030425; C:dendrite; IDA:FlyBase.
GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
GO; GO:0008305; C:integrin complex; IDA:FlyBase.
GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
GO; GO:0005927; C:muscle tendon junction; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; TAS:FlyBase.
GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
GO; GO:0004872; F:receptor activity; TAS:FlyBase.
GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
GO; GO:0007475; P:apposition of dorsal and ventral imaginal disc-derived wing surfaces; NAS:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
GO; GO:0016340; P:calcium-dependent cell-matrix adhesion; ISS:FlyBase.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
GO; GO:0016477; P:cell migration; TAS:FlyBase.
GO; GO:0007160; P:cell-matrix adhesion; TAS:FlyBase.
GO; GO:0031589; P:cell-substrate adhesion; IMP:FlyBase.
GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
GO; GO:0021551; P:central nervous system morphogenesis; IMP:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
GO; GO:0035001; P:dorsal trunk growth, open tracheal system; IMP:FlyBase.
GO; GO:0007427; P:epithelial cell migration, open tracheal system; TAS:FlyBase.
GO; GO:0007629; P:flight behavior; IEA:UniProtKB-KW.
GO; GO:0007377; P:germ-band extension; IMP:FlyBase.
GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
GO; GO:0035099; P:hemocyte migration; IGI:FlyBase.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0007508; P:larval heart development; IMP:FlyBase.
GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IMP:FlyBase.
GO; GO:0007494; P:midgut development; TAS:FlyBase.
GO; GO:0016203; P:muscle attachment; IMP:FlyBase.
GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0003344; P:pericardium morphogenesis; IMP:FlyBase.
GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
GO; GO:0051492; P:regulation of stress fiber assembly; IMP:FlyBase.
GO; GO:0007431; P:salivary gland development; IMP:FlyBase.
GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:FlyBase.
GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IGI:FlyBase.
GO; GO:0007426; P:tracheal outgrowth, open tracheal system; TAS:FlyBase.
GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom.
InterPro; IPR002035; VWF_A.
PANTHER; PTHR10082; PTHR10082; 1.
Pfam; PF07974; EGF_2; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS00243; INTEGRIN_BETA; 3.
1: Evidence at protein level;
Behavior; Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Disulfide bond; Flight; Glycoprotein; Integrin;
Membrane; Olfaction; Phosphoprotein; Receptor; Reference proteome;
Repeat; Sensory transduction; Signal; Transmembrane;
Transmembrane helix; Vision.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 846 Integrin beta-PS.
/FTId=PRO_0000016356.
TOPO_DOM 24 776 Extracellular. {ECO:0000255}.
TRANSMEM 777 799 Helical. {ECO:0000255}.
TOPO_DOM 800 846 Cytoplasmic. {ECO:0000255}.
DOMAIN 186 419 VWFA.
REPEAT 507 560 I.
REPEAT 561 605 II.
REPEAT 606 646 III.
REPEAT 647 687 IV.
REGION 507 687 Cysteine-rich tandem repeats.
COMPBIAS 115 143 Ser-rich.
MOD_RES 831 831 Phosphotyrosine. {ECO:0000250}.
MOD_RES 843 843 Phosphotyrosine. {ECO:0000250}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096,
ECO:0000269|PubMed:19349973}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096,
ECO:0000269|PubMed:19349973}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 644 644 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 718 718 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096,
ECO:0000269|PubMed:19349973}.
DISULFID 46 55 {ECO:0000250}.
DISULFID 249 252 {ECO:0000250}.
DISULFID 300 341 {ECO:0000250}.
DISULFID 441 453 {ECO:0000250}.
DISULFID 473 741 {ECO:0000250}.
DISULFID 503 507 {ECO:0000250}.
DISULFID 522 533 {ECO:0000250}.
DISULFID 530 571 {ECO:0000250}.
DISULFID 535 544 {ECO:0000250}.
DISULFID 546 561 {ECO:0000250}.
DISULFID 584 599 {ECO:0000250}.
DISULFID 601 606 {ECO:0000250}.
DISULFID 622 627 {ECO:0000250}.
DISULFID 624 656 {ECO:0000250}.
DISULFID 629 638 {ECO:0000250}.
DISULFID 640 647 {ECO:0000250}.
DISULFID 662 667 {ECO:0000250}.
DISULFID 664 715 {ECO:0000250}.
DISULFID 669 682 {ECO:0000250}.
DISULFID 685 688 {ECO:0000250}.
DISULFID 692 701 {ECO:0000250}.
DISULFID 698 771 {ECO:0000250}.
DISULFID 719 749 {ECO:0000250}.
MUTAGEN 807 807 D->A: Rescues dorsal closure defect,
muscle attachment defect, disorganized
ommatidial array and loss of cell layer
attachment in mutants; when associated
with A-817. {ECO:0000269|PubMed:8119134}.
MUTAGEN 811 811 F->A: Rescues muscle attachment defect
and loss of cell layer attachment in
mutants; when associated with A-814.
{ECO:0000269|PubMed:8119134}.
MUTAGEN 814 814 F->A: Rescues muscle attachment defect
and loss of cell layer attachment in
mutants; when associated with A-811.
{ECO:0000269|PubMed:8119134}.
MUTAGEN 817 817 E->A: Rescues dorsal closure defect,
muscle attachment defects, disorganized
ommatidial array and loss of cell layer
attachment in mutants; when associated
with A-807. {ECO:0000269|PubMed:8119134}.
MUTAGEN 831 831 Y->A: No effect on lethality; when
associated with A-843.
{ECO:0000269|PubMed:8119134}.
MUTAGEN 843 843 Y->A: No effect on lethality; when
associated with A-831.
{ECO:0000269|PubMed:8119134}.
CONFLICT 18 18 I -> M (in Ref. 1; AAA28714).
{ECO:0000305}.
CONFLICT 24 24 G -> A (in Ref. 1; AAA28714).
{ECO:0000305}.
CONFLICT 27 27 D -> N (in Ref. 1; AAA28714).
{ECO:0000305}.
SEQUENCE 846 AA; 92656 MW; 3618C74FA1B99AFB CRC64;
MILERNRRCQ LALLMIAILA AIAGQTDAQK AAKLTAVSTC ASKEKCHTCI QTEGCAWCMQ
PDFKGQSRCY QNTSSLCPEE FAYSPITVEQ ILVNNKLTNQ YKAELAAGGG GSAMSGSSSS
SYSSSSSSSS FYSQSSSGSS SASGYEEYSA GEIVQIQPQS MRLALRVNEK HNIKISYSQA
EGYPVDLYYL MDLSKSMEDD KAKLSTLGDK LSETMKRITN NFHLGFGSFV DKVLMPYVST
IPKKLEHPCE NCKAPYGYQN HMPLNNNTES FSNEVKNATV SGNLDAPEGG FDAIMQAIAC
RSQIGWREQA RRLLVFSTDA GFHYAGDGKL GGVIAPNDGE CHLSPKGEYT HSTLQDYPSI
SQINQKVKDN AINIIFAVTA SQLSVYEKLV EHIQGSSAAK LDNDSSNVVE LVKEEYRKIS
SSVEMKDNAT GDVKITYFSS CLSNGPEVQT SKCDNLKEGQ QVSFTAQIQL LKCPEDPRDW
TQTIHISPVG INEVMQIQLT MLCSCPCENP GSIGYQVQAN SCSGHGTSMC GICNCDDSYF
GNKCECSATD LTSKFANDTS CRADSTSTTD CSGRGHCVCG ACECHKRPNP IEIISGKHCE
CDNFSCERNR NQLCSGPDHG TCECGRCKCK PGWTGSNCGC QESNDTCMPP GGGEICSGHG
TCECGVCKCT VNDQGRFSGR HCEKCPTCSG RCQELKDCVQ CQMYKTGELK NGDDCARNCT
QFVPVGVEKV EIDETKDEQM CKFFDEDDCK FMFKYSEQGE LHVYAQENKE CPAKVFMLGI
VMGVIAAIVL VGLAILLLWK LLTTIHDRRE FARFEKERMN AKWDTGENPI YKQATSTFKN
PMYAGK


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