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Integrin beta-nu

 ITBN_DROME              Reviewed;         799 AA.
Q27591; A9UN88; Q9VIG7;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
23-MAY-2018, entry version 157.
RecName: Full=Integrin beta-nu;
Flags: Precursor;
Name=Itgbn {ECO:0000312|FlyBase:FBgn0010395};
Synonyms=beta-nu, betaInt-nu,
Itgbetanu {ECO:0000312|FlyBase:FBgn0010395};
ORFNames=CG1762 {ECO:0000312|FlyBase:FBgn0010395};
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Midgut endoderm;
PubMed=8076521;
Yee G.H., Hynes R.O.;
"A novel, tissue-specific integrin subunit, beta nu, expressed in the
midgut of Drosophila melanogaster.";
Development 118:845-858(1993).
[2]
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H.,
Yu C., Celniker S.E.;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, INTERACTION WITH SCB, AND TISSUE SPECIFICITY.
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).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18925939; DOI=10.1186/1749-8104-3-26;
Tsai P.I., Kao H.H., Grabbe C., Lee Y.T., Ghose A., Lai T.T.,
Peng K.P., Van Vactor D., Palmer R.H., Chen R.H., Yeh S.R.,
Chien C.T.;
"Fak56 functions downstream of integrin alphaPS3betanu and suppresses
MAPK activation in neuromuscular junction growth.";
Neural Dev. 3:26-26(2008).
[7]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=21592968; DOI=10.1074/jbc.M110.204503;
Nagaosa K., Okada R., Nonaka S., Takeuchi K., Fujita Y., Miyasaka T.,
Manaka J., Ando I., Nakanishi Y.;
"Integrin betanu-mediated phagocytosis of apoptotic cells in
Drosophila embryos.";
J. Biol. Chem. 286:25770-25777(2011).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22547074; DOI=10.1074/jbc.M111.333807;
Shiratsuchi A., Mori T., Sakurai K., Nagaosa K., Sekimizu K.,
Lee B.L., Nakanishi Y.;
"Independent recognition of Staphylococcus aureus by two receptors for
phagocytosis in Drosophila.";
J. Biol. Chem. 287:21663-21672(2012).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23054837; DOI=10.1073/pnas.1206416109;
Tsai P.I., Wang M., Kao H.H., Cheng Y.J., Lin Y.J., Chen R.H.,
Chien C.T.;
"Activity-dependent retrograde laminin A signaling regulates synapse
growth at Drosophila neuromuscular junctions.";
Proc. Natl. Acad. Sci. U.S.A. 109:17699-17704(2012).
[10]
FUNCTION, INTERACTION WITH SCB, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=23426364; DOI=10.1074/jbc.M113.451427;
Nonaka S., Nagaosa K., Mori T., Shiratsuchi A., Nakanishi Y.;
"Integrin alphaPS3/betanu-mediated phagocytosis of apoptotic cells and
bacteria in Drosophila.";
J. Biol. Chem. 288:10374-10380(2013).
-!- FUNCTION: Contributes to endodermal integrity and adhesion between
the midgut epithelium and the surrounding visceral muscle.
Essential for migration of the primordial midgut cells and for
maintaining, but not establishing, cell polarity in the midgut
epithelium. Can only partially compensate for the loss of beta-PS
integrin during primordial midgut cell migration. The two beta
subunits mediate midgut migration by distinct mechanisms: beta-PS
requires rhea/Talin and beta-nu does not. Integrin alpha-PS3/beta-
nu is required for effective phagocytosis of apoptotic cells
during embryonic development and for the phagocytic elimination of
S.aureus by mediating the binding of S.aureus peptidoglycan to
larval hemocytes, which probably activates a signaling pathway
involving Rac1 and Rac2. Not required for the production of
antimicrobial peptides during S.aureus. Upon activation by LanA,
integrin alpha-PS3/beta-nu activates Fak in presynapsis to
suppress neuromuscular junction (NMJ) growth during larval
development and during low crawling activity, but not during
higher-crawling conditions. Mediates, together with LanA,
glutamate receptor-modulated NMJ growth.
{ECO:0000269|PubMed:15469969, ECO:0000269|PubMed:18925939,
ECO:0000269|PubMed:21592968, ECO:0000269|PubMed:22547074,
ECO:0000269|PubMed:23054837, ECO:0000269|PubMed:23426364}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts
with scb/alpha-PS3. {ECO:0000269|PubMed:15469969,
ECO:0000269|PubMed:23426364}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Expression is confined to the developing
midgut endoderm and its precursors during embryogenesis. In the
larvae, expression is concentrated in the midgut imaginal disks.
Expressed in embryonic and larval hemocytes (at protein level).
{ECO:0000269|PubMed:15469969, ECO:0000269|PubMed:21592968,
ECO:0000269|PubMed:22547074, ECO:0000269|PubMed:8076521}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development. Highest
expression occurs during 12-15 hours of embryonic development (at
protein level). {ECO:0000269|PubMed:21592968,
ECO:0000269|PubMed:23426364, ECO:0000269|PubMed:8076521}.
-!- DISRUPTION PHENOTYPE: Homozygous mutant flies are viable and
fertile. Mutant embryos show reduced level of phagocytosis, but
normal level of hemocytes or apoptosis. At NMJ, mutant larvae show
normal patterns of synaptic proteins but increased branch length,
bouton number and quantal content in basal synaptic transmission
recording. {ECO:0000269|PubMed:18925939,
ECO:0000269|PubMed:21592968, ECO:0000269|PubMed:23054837,
ECO:0000269|PubMed:23426364}.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L13305; AAC37169.1; -; mRNA.
EMBL; AE014134; AAF53952.1; -; Genomic_DNA.
EMBL; BT031252; ABY20493.1; -; mRNA.
RefSeq; NP_001303333.1; NM_001316404.1.
RefSeq; NP_523608.2; NM_078884.3.
UniGene; Dm.19859; -.
ProteinModelPortal; Q27591; -.
SMR; Q27591; -.
BioGrid; 61326; 4.
IntAct; Q27591; 2.
STRING; 7227.FBpp0080990; -.
PaxDb; Q27591; -.
PRIDE; Q27591; -.
EnsemblMetazoa; FBtr0081461; FBpp0080990; FBgn0010395.
EnsemblMetazoa; FBtr0346711; FBpp0312322; FBgn0010395.
GeneID; 35368; -.
KEGG; dme:Dmel_CG1762; -.
CTD; 35368; -.
FlyBase; FBgn0010395; Itgbn.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
GeneTree; ENSGT00760000119064; -.
InParanoid; Q27591; -.
KO; K05719; -.
OMA; MDLTWTM; -.
OrthoDB; EOG091G029W; -.
PhylomeDB; Q27591; -.
GenomeRNAi; 35368; -.
PRO; PR:Q27591; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0010395; -.
ExpressionAtlas; Q27591; baseline and differential.
Genevisible; Q27591; DM.
GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
GO; GO:0008305; C:integrin complex; IDA:FlyBase.
GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
GO; GO:0043277; P:apoptotic cell clearance; IMP:FlyBase.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:FlyBase.
GO; GO:0007160; P:cell-matrix adhesion; TAS:FlyBase.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:FlyBase.
GO; GO:0045886; P:negative regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10082; PTHR10082; 1.
Pfam; PF07974; EGF_2; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
PROSITE; PS00022; EGF_1; 4.
PROSITE; PS01186; EGF_2; 4.
PROSITE; PS00243; INTEGRIN_BETA; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
Cell adhesion; Complete proteome; Glycoprotein; Integrin; Membrane;
Phagocytosis; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 799 Integrin beta-nu.
/FTId=PRO_0000016357.
TOPO_DOM 27 725 Extracellular. {ECO:0000255}.
TRANSMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 799 Cytoplasmic. {ECO:0000255}.
DOMAIN 136 372 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 505 505 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 655 655 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 680 680 E -> G (in Ref. 1; AAC37169).
{ECO:0000305}.
CONFLICT 701 701 V -> A (in Ref. 1; AAC37169).
{ECO:0000305}.
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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