ITBX_DROME
ID ITBX_DROME Reviewed; 846 AA.
AC P11584; Q8MYX9; Q9W3L2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Integrin beta-PS;
DE AltName: Full=Position-specific antigen beta subunit;
DE AltName: Full=Protein myospheroid;
DE AltName: Full=Protein olfactory C;
DE Flags: Precursor;
GN Name=mys; Synonyms=l(1)mys, olfC; ORFNames=CG1560;
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].
RX PubMed=3128792; DOI=10.1073/pnas.85.8.2633;
RA Mackrell A.J., Blumberg B., Haynes S.R., Fessler J.H.;
RT "The lethal myospheroid gene of Drosophila encodes a membrane protein
RT homologous to vertebrate integrin beta subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2633-2637(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE, FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-807; PHE-811; PHE-814; GLU-817; TYR-831 AND TYR-843.
RC TISSUE=Embryo, and Imaginal disk;
RX PubMed=8119134; DOI=10.1242/dev.120.1.91;
RA Grinblat Y., Zusman S., Yee G., Hynes R.O., Kafatos F.C.;
RT "Functions of the cytoplasmic domain of the beta PS integrin subunit during
RT Drosophila development.";
RL Development 120:91-102(1994).
RN [3]
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 [4]
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]
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 [6]
RP FUNCTION.
RX PubMed=7924982; DOI=10.1242/dev.120.7.1747;
RA Fogerty F.J., Fessler L.I., Bunch T.A., Yaron Y., Parker C.G., Nelson R.E.,
RA Brower D.L., Gullberg D., Fessler J.H.;
RT "Tiggrin, a novel Drosophila extracellular matrix protein that functions as
RT a ligand for Drosophila alpha PS2 beta PS integrins.";
RL Development 120:1747-1758(1994).
RN [7]
RP FUNCTION.
RX PubMed=7972082; DOI=10.1073/pnas.91.24.11447;
RA Gotwals P.J., Fessler L.I., Wehrli M., Hynes R.O.;
RT "Drosophila PS1 integrin is a laminin receptor and differs in ligand
RT specificity from PS2.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11447-11451(1994).
RN [8]
RP FUNCTION.
RX PubMed=9660786; DOI=10.1074/jbc.273.29.18235;
RA Graner M.W., Bunch T.A., Baumgartner S., Kerschen A., Brower D.L.;
RT "Splice variants of the Drosophila PS2 integrins differentially interact
RT with RGD-containing fragments of the extracellular proteins tiggrin, ten-m,
RT and D-laminin 2.";
RL J. Biol. Chem. 273:18235-18241(1998).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10821184; DOI=10.1007/s004380051194;
RA Ayyub C., Rodrigues V., Hasan G., Siddiqi O.;
RT "Genetic analysis of olfC demonstrates a role for the position-specific
RT integrins in the olfactory system of Drosophila melanogaster.";
RL Mol. Gen. Genet. 263:498-504(2000).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15469969; DOI=10.1242/dev.01427;
RA Devenport D., Brown N.H.;
RT "Morphogenesis in the absence of integrins: mutation of both Drosophila
RT beta subunits prevents midgut migration.";
RL Development 131:5405-5415(2004).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-403; ASN-557 AND ASN-718, AND
RP IDENTIFICATION BY 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, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19035354; DOI=10.1002/dvdy.21802;
RA Dinkins M.B., Fratto V.M., Lemosy E.K.;
RT "Integrin alpha chains exhibit distinct temporal and spatial localization
RT patterns in epithelial cells of the Drosophila ovary.";
RL Dev. Dyn. 237:3927-3939(2008).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-266; ASN-403; ASN-557 AND
RP ASN-718, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27191715; DOI=10.1371/journal.pgen.1006043;
RA Lee J.Y., Chen J.Y., Shaw J.L., Chang K.T.;
RT "Maintenance of stem cell niche integrity by a novel activator of integrin
RT signaling.";
RL PLoS Genet. 12:E1006043-E1006043(2016).
CC -!- FUNCTION: Integrin alpha-PS1/beta-PS is a receptor for laminin
CC (PubMed:7972082). Integrin alpha-PS2/beta-PS is a receptor for Tig, wb
CC and Ten-m (PubMed:7924982, PubMed:7972082, PubMed:9660786). Contributes
CC to endodermal integrity and adhesion between the midgut epithelium and
CC the surrounding visceral muscle (PubMed:15469969). Essential for
CC migration of the primordial midgut cells and for maintaining, but not
CC establishing, cell polarity in the midgut epithelium (PubMed:15469969).
CC The two beta subunits mediate midgut migration by distinct mechanisms:
CC beta-PS requires rhea/talin and Itgbn does not (PubMed:15469969).
CC Required for rhea/talin correct cellular localization in the midgut
CC (PubMed:15469969). Required for many embryonic (dorsal closure and
CC somatic muscle attachments) and postembryonic developmental processes
CC (attachment between cell layers of imaginal disks, organization of
CC ommatidial arrays and flight muscle development) (PubMed:8119134,
CC PubMed:7924982, PubMed:7972082, PubMed:10821184). Involved in the
CC function and/or development of the olfactory system (PubMed:10821184).
CC In the testes, essential for shv-dependent maintenance of somatic hub
CC cells and their localization to the apical tip (PubMed:27191715). Plays
CC a role in timely border cell migration during oogenesis
CC (PubMed:19035354). {ECO:0000269|PubMed:10821184,
CC ECO:0000269|PubMed:15469969, ECO:0000269|PubMed:19035354,
CC ECO:0000269|PubMed:27191715, ECO:0000269|PubMed:7924982,
CC ECO:0000269|PubMed:7972082, ECO:0000269|PubMed:8119134,
CC ECO:0000269|PubMed:9660786}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-PS associates
CC with either alpha-PS1, alpha-PS2, alpha-PS3, alpha-PS4 or alpha-PS5.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19035354}. Lateral cell membrane
CC {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19035354}. Basal cell membrane
CC {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19035354}. Note=In ovary, localizes to the apical,
CC lateral and basal membranes of follicle cells through oogenesis stage
CC 10A. Apical membrane expression peaks at oogenesis stages 9 and 10A in
CC columnar follicle cells overlying the oocyte but decreases in the most
CC posterior follicle cells. Thereafter, it is down-regulated.
CC Localization to lateral and basal membranes persists during dorsal
CC appendage morphogenesis.
CC -!- TISSUE SPECIFICITY: In ovaries, strongly expressed in follicle cells
CC (PubMed:19035354). In oocytes, expressed in the forming dorsal
CC appendages (at protein level) (PubMed:19035354). Expressed in the
CC embryonic dorsal cuticle, the larval eye and the wing imaginal disk
CC (PubMed:8119134). In testes, detected at the interface between somatic
CC hub cells and cyst stem cells (PubMed:27191715).
CC {ECO:0000269|PubMed:19035354, ECO:0000269|PubMed:27191715,
CC ECO:0000269|PubMed:8119134}.
CC -!- DISRUPTION PHENOTYPE: In zygotic mutant embryos, midgut forms primary
CC constrictions but fails to elongate and the visceral muscle does not
CC flatten but remains attached to the midgut epithelium. Embryos lacking
CC maternal and zygotic mys show a delay in midgut migration. Mutant
CC larvae present an olfactory phenotype, showing reduced response to
CC isoamyl acetate but normal response to ethyl acetate.
CC {ECO:0000269|PubMed:10821184, ECO:0000269|PubMed:15469969}.
CC -!- MISCELLANEOUS: The absence of the beta-PS subunit results in detachment
CC and rounding up of the muscles, thus the gene encoding beta-PS is
CC called myospheroid.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; J03251; AAA28714.1; -; mRNA.
DR EMBL; AE014298; AAF46313.2; -; Genomic_DNA.
DR EMBL; AY113499; AAM29504.1; -; mRNA.
DR PIR; A30889; A30889.
DR RefSeq; NP_001284998.1; NM_001298069.1.
DR RefSeq; NP_001284999.1; NM_001298070.1.
DR RefSeq; NP_524793.2; NM_080054.3.
DR AlphaFoldDB; P11584; -.
DR SMR; P11584; -.
DR BioGRID; 69357; 50.
DR IntAct; P11584; 1.
DR STRING; 7227.FBpp0071061; -.
DR GlyGen; P11584; 9 sites.
DR iPTMnet; P11584; -.
DR PaxDb; P11584; -.
DR PRIDE; P11584; -.
DR DNASU; 44885; -.
DR EnsemblMetazoa; FBtr0071105; FBpp0071061; FBgn0004657.
DR EnsemblMetazoa; FBtr0340136; FBpp0309122; FBgn0004657.
DR EnsemblMetazoa; FBtr0340137; FBpp0309123; FBgn0004657.
DR GeneID; 44885; -.
DR KEGG; dme:Dmel_CG1560; -.
DR CTD; 44885; -.
DR FlyBase; FBgn0004657; mys.
DR VEuPathDB; VectorBase:FBgn0004657; -.
DR eggNOG; KOG1226; Eukaryota.
DR HOGENOM; CLU_011772_1_1_1; -.
DR InParanoid; P11584; -.
DR OMA; NCVCGAC; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P11584; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-DME-1566977; Fibronectin matrix formation.
DR Reactome; R-DME-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-DME-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-DME-210991; Basigin interactions.
DR Reactome; R-DME-2129379; Molecules associated with elastic fibres.
DR Reactome; R-DME-216083; Integrin cell surface interactions.
DR Reactome; R-DME-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-DME-3000157; Laminin interactions.
DR Reactome; R-DME-3000170; Syndecan interactions.
DR Reactome; R-DME-3000178; ECM proteoglycans.
DR Reactome; R-DME-354192; Integrin signaling.
DR Reactome; R-DME-446107; Type I hemidesmosome assembly.
DR Reactome; R-DME-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR Reactome; R-DME-9634597; GPER1 signaling.
DR SignaLink; P11584; -.
DR BioGRID-ORCS; 44885; 0 hits in 3 CRISPR screens.
DR ChiTaRS; mys; fly.
DR GenomeRNAi; 44885; -.
DR PRO; PR:P11584; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004657; Expressed in thoracico-abdominal ganglion (Drosophila) and 38 other tissues.
DR ExpressionAtlas; P11584; baseline and differential.
DR Genevisible; P11584; DM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
DR GO; GO:0043034; C:costamere; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0008305; C:integrin complex; IDA:FlyBase.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005927; C:muscle tendon junction; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IMP:FlyBase.
DR GO; GO:0042734; C:presynaptic membrane; IMP:FlyBase.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
DR GO; GO:0016340; P:calcium-dependent cell-matrix adhesion; ISS:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0021551; P:central nervous system morphogenesis; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0035001; P:dorsal trunk growth, open tracheal system; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IEA:UniProtKB-KW.
DR GO; GO:0007377; P:germ-band extension; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IGI:FlyBase.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0007508; P:larval heart development; IMP:FlyBase.
DR GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IMP:FlyBase.
DR GO; GO:0007494; P:midgut development; TAS:FlyBase.
DR GO; GO:0016203; P:muscle attachment; IMP:FlyBase.
DR GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0003344; P:pericardium morphogenesis; IMP:FlyBase.
DR GO; GO:0090129; P:positive regulation of synapse maturation; IMP:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IMP:FlyBase.
DR GO; GO:0007431; P:salivary gland development; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:FlyBase.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IGI:FlyBase.
DR GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 1: Evidence at protein level;
KW Behavior; Cell adhesion; Cell membrane; Developmental protein;
KW Disulfide bond; Flight; Glycoprotein; Integrin; Membrane; Olfaction;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Sensory transduction;
KW Signal; Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..846
FT /note="Integrin beta-PS"
FT /id="PRO_0000016356"
FT TOPO_DOM 24..776
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..846
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 186..419
FT /note="VWFA"
FT REPEAT 507..560
FT /note="I"
FT REPEAT 561..605
FT /note="II"
FT REPEAT 606..646
FT /note="III"
FT REPEAT 647..687
FT /note="IV"
FT REGION 507..687
FT /note="Cysteine-rich tandem repeats"
FT MOD_RES 831
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 843
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19349973"
FT DISULFID 46..55
FT /evidence="ECO:0000250"
FT DISULFID 249..252
FT /evidence="ECO:0000250"
FT DISULFID 300..341
FT /evidence="ECO:0000250"
FT DISULFID 441..453
FT /evidence="ECO:0000250"
FT DISULFID 473..741
FT /evidence="ECO:0000250"
FT DISULFID 503..507
FT /evidence="ECO:0000250"
FT DISULFID 522..533
FT /evidence="ECO:0000250"
FT DISULFID 530..571
FT /evidence="ECO:0000250"
FT DISULFID 535..544
FT /evidence="ECO:0000250"
FT DISULFID 546..561
FT /evidence="ECO:0000250"
FT DISULFID 584..599
FT /evidence="ECO:0000250"
FT DISULFID 601..606
FT /evidence="ECO:0000250"
FT DISULFID 622..627
FT /evidence="ECO:0000250"
FT DISULFID 624..656
FT /evidence="ECO:0000250"
FT DISULFID 629..638
FT /evidence="ECO:0000250"
FT DISULFID 640..647
FT /evidence="ECO:0000250"
FT DISULFID 662..667
FT /evidence="ECO:0000250"
FT DISULFID 664..715
FT /evidence="ECO:0000250"
FT DISULFID 669..682
FT /evidence="ECO:0000250"
FT DISULFID 685..688
FT /evidence="ECO:0000250"
FT DISULFID 692..701
FT /evidence="ECO:0000250"
FT DISULFID 698..771
FT /evidence="ECO:0000250"
FT DISULFID 719..749
FT /evidence="ECO:0000250"
FT MUTAGEN 807
FT /note="D->A: Rescues dorsal closure defect, muscle
FT attachment defect, disorganized ommatidial array and loss
FT of cell layer attachment in mutants; when associated with
FT A-817."
FT /evidence="ECO:0000269|PubMed:8119134"
FT MUTAGEN 811
FT /note="F->A: Rescues muscle attachment defect and loss of
FT cell layer attachment in mutants; when associated with A-
FT 814."
FT /evidence="ECO:0000269|PubMed:8119134"
FT MUTAGEN 814
FT /note="F->A: Rescues muscle attachment defect and loss of
FT cell layer attachment in mutants; when associated with A-
FT 811."
FT /evidence="ECO:0000269|PubMed:8119134"
FT MUTAGEN 817
FT /note="E->A: Rescues dorsal closure defect, muscle
FT attachment defects, disorganized ommatidial array and loss
FT of cell layer attachment in mutants; when associated with
FT A-807."
FT /evidence="ECO:0000269|PubMed:8119134"
FT MUTAGEN 831
FT /note="Y->A: No effect on lethality; when associated with
FT A-843."
FT /evidence="ECO:0000269|PubMed:8119134"
FT MUTAGEN 843
FT /note="Y->A: No effect on lethality; when associated with
FT A-831."
FT /evidence="ECO:0000269|PubMed:8119134"
FT CONFLICT 18
FT /note="I -> M (in Ref. 1; AAA28714)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="G -> A (in Ref. 1; AAA28714)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="D -> N (in Ref. 1; AAA28714)"
FT /evidence="ECO:0000305"
SQ 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
