GenomeNet

Database: UniProt
Entry: Q27591
LinkDB: Q27591
Original site: Q27591 
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   10-APR-2019, entry version 162.
DE   RecName: Full=Integrin beta-nu;
DE   Flags: Precursor;
GN   Name=Itgbn {ECO:0000312|FlyBase:FBgn0010395};
GN   Synonyms=beta-nu, betaInt-nu,
GN   Itgbetanu {ECO:0000312|FlyBase:FBgn0010395};
GN   ORFNames=CG1762 {ECO:0000312|FlyBase:FBgn0010395};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Midgut endoderm;
RX   PubMed=8076521;
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   Yu C., 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
RT   Drosophila 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.,
RA   Peng K.P., Van Vactor D., Palmer R.H., Chen R.H., Yeh S.R.,
RA   Chien C.T.;
RT   "Fak56 functions downstream of integrin alphaPS3betanu and suppresses
RT   MAPK 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
RT   Drosophila 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.,
RA   Lee B.L., 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.,
RA   Chien C.T.;
RT   "Activity-dependent retrograde laminin A signaling regulates synapse
RT   growth 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
CC       the midgut epithelium and the surrounding visceral muscle.
CC       Essential for migration of the primordial midgut cells and for
CC       maintaining, but not establishing, cell polarity in the midgut
CC       epithelium. Can only partially compensate for the loss of beta-PS
CC       integrin during primordial midgut cell migration. The two beta
CC       subunits mediate midgut migration by distinct mechanisms: beta-PS
CC       requires rhea/Talin and beta-nu does not. Integrin alpha-PS3/beta-
CC       nu is required for effective phagocytosis of apoptotic cells
CC       during embryonic development and for the phagocytic elimination of
CC       S.aureus by mediating the binding of S.aureus peptidoglycan to
CC       larval hemocytes, which probably activates a signaling pathway
CC       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
CC       suppress neuromuscular junction (NMJ) growth during larval
CC       development and during low crawling activity, but not during
CC       higher-crawling conditions. Mediates, together with LanA,
CC       glutamate receptor-modulated NMJ growth.
CC       {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
CC       with scb/alpha-PS3. {ECO:0000269|PubMed:15469969,
CC       ECO:0000269|PubMed:23426364}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expression is confined to the developing
CC       midgut endoderm and its precursors during embryogenesis. In the
CC       larvae, expression is concentrated in the midgut imaginal disks.
CC       Expressed in 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
CC       fertile. Mutant embryos show reduced level of phagocytosis, but
CC       normal level of hemocytes or apoptosis. At NMJ, mutant larvae show
CC       normal patterns of synaptic proteins but increased branch length,
CC       bouton number and quantal content in basal synaptic transmission
CC       recording. {ECO:0000269|PubMed:18925939,
CC       ECO:0000269|PubMed:21592968, ECO:0000269|PubMed:23054837,
CC       ECO:0000269|PubMed:23426364}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
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   UniGene; Dm.19859; -.
DR   ProteinModelPortal; Q27591; -.
DR   SMR; Q27591; -.
DR   BioGrid; 61326; 4.
DR   IntAct; Q27591; 2.
DR   STRING; 7227.FBpp0080990; -.
DR   PaxDb; Q27591; -.
DR   PRIDE; Q27591; -.
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   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   InParanoid; Q27591; -.
DR   KO; K05719; -.
DR   OMA; MDLTWTM; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; Q27591; -.
DR   Reactome; R-DME-3000170; Syndecan interactions.
DR   GenomeRNAi; 35368; -.
DR   PRO; PR:Q27591; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0010395; Expressed in 5 organ(s), highest expression level in larva.
DR   ExpressionAtlas; Q27591; baseline and differential.
DR   Genevisible; Q27591; DM.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
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 growth 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; Complete proteome; Glycoprotein; Integrin; Membrane;
KW   Phagocytosis; Receptor; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    799       Integrin beta-nu.
FT                                /FTId=PRO_0000016357.
FT   TOPO_DOM     27    725       Extracellular. {ECO:0000255}.
FT   TRANSMEM    726    746       Helical. {ECO:0000255}.
FT   TOPO_DOM    747    799       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      136    372       VWFA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   CARBOHYD     73     73       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    167    167       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    409    409       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    505    505       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    655    655       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    680    680       E -> G (in Ref. 1; AAC37169).
FT                                {ECO:0000305}.
FT   CONFLICT    701    701       V -> A (in Ref. 1; AAC37169).
FT                                {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
//
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