ITBN_DROME
ID ITBN_DROME Reviewed; 799 AA.
AC Q27591; A9UN88; Q9VIG7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Integrin beta-nu;
DE Flags: Precursor;
GN Name=Itgbn {ECO:0000312|FlyBase:FBgn0010395};
GN Synonyms=beta-nu, betaInt-nu, Itgbetanu {ECO:0000312|FlyBase:FBgn0010395};
GN ORFNames=CG1762 {ECO:0000312|FlyBase:FBgn0010395};
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Midgut endoderm;
RX PubMed=8076521; DOI=10.1242/dev.118.3.845;
RA Yee G.H., Hynes R.O.;
RT "A novel, tissue-specific integrin subunit, beta nu, expressed in the
RT midgut of Drosophila melanogaster.";
RL Development 118:845-858(1993).
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.
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].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH SCB, AND TISSUE SPECIFICITY.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18925939; DOI=10.1186/1749-8104-3-26;
RA Tsai P.I., Kao H.H., Grabbe C., Lee Y.T., Ghose A., Lai T.T., Peng K.P.,
RA Van Vactor D., Palmer R.H., Chen R.H., Yeh S.R., Chien C.T.;
RT "Fak56 functions downstream of integrin alphaPS3betanu and suppresses MAPK
RT activation in neuromuscular junction growth.";
RL Neural Dev. 3:26-26(2008).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21592968; DOI=10.1074/jbc.m110.204503;
RA Nagaosa K., Okada R., Nonaka S., Takeuchi K., Fujita Y., Miyasaka T.,
RA Manaka J., Ando I., Nakanishi Y.;
RT "Integrin betanu-mediated phagocytosis of apoptotic cells in Drosophila
RT embryos.";
RL J. Biol. Chem. 286:25770-25777(2011).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22547074; DOI=10.1074/jbc.m111.333807;
RA Shiratsuchi A., Mori T., Sakurai K., Nagaosa K., Sekimizu K., Lee B.L.,
RA Nakanishi Y.;
RT "Independent recognition of Staphylococcus aureus by two receptors for
RT phagocytosis in Drosophila.";
RL J. Biol. Chem. 287:21663-21672(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23054837; DOI=10.1073/pnas.1206416109;
RA Tsai P.I., Wang M., Kao H.H., Cheng Y.J., Lin Y.J., Chen R.H., Chien C.T.;
RT "Activity-dependent retrograde laminin A signaling regulates synapse growth
RT at Drosophila neuromuscular junctions.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17699-17704(2012).
RN [10]
RP FUNCTION, INTERACTION WITH SCB, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23426364; DOI=10.1074/jbc.m113.451427;
RA Nonaka S., Nagaosa K., Mori T., Shiratsuchi A., Nakanishi Y.;
RT "Integrin alphaPS3/betanu-mediated phagocytosis of apoptotic cells and
RT bacteria in Drosophila.";
RL J. Biol. Chem. 288:10374-10380(2013).
CC -!- FUNCTION: Contributes to endodermal integrity and adhesion between the
CC midgut epithelium and the surrounding visceral muscle. Essential for
CC migration of the primordial midgut cells and for maintaining, but not
CC establishing, cell polarity in the midgut epithelium. Can only
CC partially compensate for the loss of beta-PS integrin during primordial
CC midgut cell migration. The two beta subunits mediate midgut migration
CC by distinct mechanisms: beta-PS requires rhea/Talin and beta-nu does
CC not. Integrin alpha-PS3/beta-nu is required for effective phagocytosis
CC of apoptotic cells during embryonic development and for the phagocytic
CC elimination of S.aureus by mediating the binding of S.aureus
CC peptidoglycan to larval hemocytes, which probably activates a signaling
CC pathway involving Rac1 and Rac2. Not required for the production of
CC antimicrobial peptides during S.aureus. Upon activation by LanA,
CC integrin alpha-PS3/beta-nu activates Fak in presynapsis to suppress
CC neuromuscular junction (NMJ) growth during larval development and
CC during low crawling activity, but not during higher-crawling
CC conditions. Mediates, together with LanA, glutamate receptor-modulated
CC NMJ growth. {ECO:0000269|PubMed:15469969, ECO:0000269|PubMed:18925939,
CC ECO:0000269|PubMed:21592968, ECO:0000269|PubMed:22547074,
CC ECO:0000269|PubMed:23054837, ECO:0000269|PubMed:23426364}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with
CC scb/alpha-PS3. {ECO:0000269|PubMed:15469969,
CC ECO:0000269|PubMed:23426364}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expression is confined to the developing midgut
CC endoderm and its precursors during embryogenesis. In the larvae,
CC expression is concentrated in the midgut imaginal disks. Expressed in
CC embryonic and larval hemocytes (at protein level).
CC {ECO:0000269|PubMed:15469969, ECO:0000269|PubMed:21592968,
CC ECO:0000269|PubMed:22547074, ECO:0000269|PubMed:8076521}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Highest
CC expression occurs during 12-15 hours of embryonic development (at
CC protein level). {ECO:0000269|PubMed:21592968,
CC ECO:0000269|PubMed:23426364, ECO:0000269|PubMed:8076521}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutant flies are viable and fertile.
CC Mutant embryos show reduced level of phagocytosis, but normal level of
CC hemocytes or apoptosis. At NMJ, mutant larvae show normal patterns of
CC synaptic proteins but increased branch length, bouton number and
CC quantal content in basal synaptic transmission recording.
CC {ECO:0000269|PubMed:18925939, ECO:0000269|PubMed:21592968,
CC ECO:0000269|PubMed:23054837, ECO:0000269|PubMed:23426364}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; L13305; AAC37169.1; -; mRNA.
DR EMBL; AE014134; AAF53952.1; -; Genomic_DNA.
DR EMBL; BT031252; ABY20493.1; -; mRNA.
DR RefSeq; NP_001303333.1; NM_001316404.1.
DR RefSeq; NP_523608.2; NM_078884.3.
DR AlphaFoldDB; Q27591; -.
DR SMR; Q27591; -.
DR BioGRID; 61326; 5.
DR IntAct; Q27591; 2.
DR STRING; 7227.FBpp0080990; -.
DR GlyGen; Q27591; 5 sites.
DR PaxDb; Q27591; -.
DR DNASU; 35368; -.
DR EnsemblMetazoa; FBtr0081461; FBpp0080990; FBgn0010395.
DR EnsemblMetazoa; FBtr0346711; FBpp0312322; FBgn0010395.
DR GeneID; 35368; -.
DR KEGG; dme:Dmel_CG1762; -.
DR CTD; 35368; -.
DR FlyBase; FBgn0010395; Itgbn.
DR VEuPathDB; VectorBase:FBgn0010395; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_011772_1_0_1; -.
DR InParanoid; Q27591; -.
DR OMA; NHGDCDC; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; Q27591; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
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-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 35368; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35368; -.
DR PRO; PR:Q27591; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0010395; Expressed in adult midgut (Drosophila) and 18 other tissues.
DR ExpressionAtlas; Q27591; baseline and differential.
DR Genevisible; Q27591; DM.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0008305; C:integrin complex; IDA:FlyBase.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS: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:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
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; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 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; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Glycoprotein; Integrin; Membrane; Phagocytosis; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..799
FT /note="Integrin beta-nu"
FT /id="PRO_0000016357"
FT TOPO_DOM 27..725
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 136..372
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 680
FT /note="E -> G (in Ref. 1; AAC37169)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="V -> A (in Ref. 1; AAC37169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 90842 MW; 351869D523F07DEB CRC64;
MTSLGGRAFL WIYLVFLIAE ISHSDADSID DQCRHADSCE RCLSAHLECA WCTDKEYQVG
YRCLSRRQLL NYNCSETDIY ENQPVLDVLQ DKPLKDYETS DQAVQVTPQR AYLKLVKGNT
QRMKLSYRTA RNNPLDLYVL MDLTWTMRDD KKTLEELGAQ LSQTLKNLTG NYRLGFGSFA
DKPTLPMILP QHRENPCAAE RATCEPTYGY RHQLSLTDDI PAFTSAVANS KITGNLDNLE
GGLDALMQVI VCTKEIGWKE QARKVVILVT DGFMHLAGDG LLAGIIQRND KQCHLNKAGE
YTGSLNYDYP SLEEIYRELL RRKINVIFAV TEEVVSSYWE LSALMKEISY VDILSADSSN
ILELIKKSYE SLIKRTQFAD NSPDFIDMAY YTDCGGQFPS LQKRNYCNNV TLGKQIDFYV
DVTLKKYPDN QVYTHKIRVE ETSLSEFMDL DVELQRPCPC QETPDPENEE GRFLCDYKGY
LYCGMCECDE GWTGTYCNCP TDATNVTSNE ALLQKCRQPF SDKSTSELVC SNHGDCDCGT
CLCDPGYTGP FCECRECLDC DEKLADCFCG QCVCKYGWSG SKCNCDGDTD ACVGPTGEIC
SERGTCQCEE CQCEEPYLGK FCEIDPEKDN KLCLFYEPCV TCLIEQKQGM GVCENLTEIC
SSLDRQETYP YNFVHELDPE QDQCLVRLVN KHGIQCDSFF VYQVIDHSNF LTIQAVDCEP
PDYVALVGYI SAFTLLIGLL IIFIILWYIR AKDAREYAKF EEDQKNSVRQ ENPIYRDPVG
RYEVPKALSV KYDENPFAS
