ITB2_MOUSE
ID ITB2_MOUSE Reviewed; 771 AA.
AC P11835; Q64482;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Integrin beta-2;
DE AltName: Full=Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta;
DE AltName: Full=Complement receptor C3 subunit beta;
DE AltName: CD_antigen=CD18;
DE Flags: Precursor;
GN Name=Itgb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX PubMed=2569711; DOI=10.1093/nar/17.13.5397;
RA Wilson R.W., O'Brien W.E., Beaudet A.L.;
RT "Nucleotide sequence of the cDNA from the mouse leukocyte adhesion protein
RT CD18.";
RL Nucleic Acids Res. 17:5397-5397(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1969385; DOI=10.1007/bf00211555;
RA Zeger D.L., Osman N., Hennings M., McKenzie I.F., Sears D.W., Hogarth P.M.;
RT "Mouse macrophage beta subunit (CD11b) cDNA for the CR3 complement
RT receptor/Mac-1 antigen.";
RL Immunogenetics 31:191-197(1990).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=1671669; DOI=10.1007/bf00211699;
RA Kofler R.;
RT "Mouse macrophage beta subunit (CD11b) cDNA for the CR3 complement
RT receptor/Mac-1 antigen.";
RL Immunogenetics 33:77-77(1991).
RN [4]
RP FUNCTION DURING LUNG INJURY.
RX PubMed=18587400; DOI=10.1038/ni.1628;
RA Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.;
RT "Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in
RT sepsis-induced lung inflammation by activating beta2 integrins.";
RL Nat. Immunol. 9:880-886(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH FGR.
RX PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
RA Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
RA Berton G.;
RT "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
RT migration.";
RL FEBS Lett. 584:15-21(2010).
CC -!- FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3
CC and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted
CC form of ubiquitin-like protein ISG15; the interaction is mediated by
CC ITGAL (By similarity). Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are
CC receptors for the iC3b fragment of the third complement component and
CC for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in
CC fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2
CC peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a
CC receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and
CC VCAM1. Contributes to natural killer cell cytotoxicity (By similarity).
CC Involved in leukocyte adhesion and transmigration of leukocytes
CC including T-cells and neutrophils (By similarity). Triggers neutrophil
CC transmigration during lung injury through PTK2B/PYK2-mediated
CC activation (PubMed:18587400). Integrin ITGAL/ITGB2 in association with
CC ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages
CC (By similarity). In association with alpha subunit ITGAM/CD11b,
CC required for CD177-PRTN3-mediated activation of TNF primed neutrophils
CC (By similarity). Integrin ITGAM/ITGB2 plays a critical role in mast
CC cell development and in immune complex-mediated glomerulonephritis.
CC Mice expressing a null mutation of the ITGAM subunit gene demonstrate
CC increase in neutrophil accumulation, in response to a impaired
CC degranulation and phagocytosis, events that apparently accelerate
CC apoptosis in neutrophils. These mice develop obesity.
CC {ECO:0000250|UniProtKB:P05107, ECO:0000269|PubMed:18587400,
CC ECO:0000269|PubMed:19903482}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The ITGB2 beta
CC subunit associates with the ITGAL, ITGAM, ITGAX or ITGAD alpha
CC subunits. Found in a complex with CD177 and ITGAM/CD11b (By
CC similarity). Interacts with FGR (PubMed:19903482). Interacts with COPS5
CC and RANBP9 (By similarity). Interacts with FLNA (via filamin repeats 4,
CC 9, 12, 17, 19, 21, and 23) (By similarity). Interacts with THBD (By
CC similarity). {ECO:0000250|UniProtKB:P05107,
CC ECO:0000269|PubMed:19903482}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05107};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05107}.
CC Membrane raft {ECO:0000250|UniProtKB:P05107}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:P05107}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; X14951; CAA33077.1; -; mRNA.
DR EMBL; M31039; AAA39325.1; -; mRNA.
DR PIR; A45839; A45839.
DR PIR; S04847; S04847.
DR RefSeq; NP_032430.2; NM_008404.4.
DR AlphaFoldDB; P11835; -.
DR SMR; P11835; -.
DR BioGRID; 200828; 65.
DR ComplexPortal; CPX-3126; Integrin alphaD-beta2 complex.
DR ComplexPortal; CPX-3128; Integrin alphaL-beta2 complex.
DR ComplexPortal; CPX-3129; Integrin alphaM-beta2 complex.
DR ComplexPortal; CPX-3134; Integrin alphaX-beta2 complex.
DR CORUM; P11835; -.
DR DIP; DIP-37428N; -.
DR IntAct; P11835; 8.
DR MINT; P11835; -.
DR STRING; 10090.ENSMUSP00000000299; -.
DR GlyConnect; 2404; 5 N-Linked glycans (2 sites).
DR GlyGen; P11835; 6 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; P11835; -.
DR PhosphoSitePlus; P11835; -.
DR SwissPalm; P11835; -.
DR CPTAC; non-CPTAC-4042; -.
DR EPD; P11835; -.
DR MaxQB; P11835; -.
DR PaxDb; P11835; -.
DR PeptideAtlas; P11835; -.
DR PRIDE; P11835; -.
DR ProteomicsDB; 269348; -.
DR DNASU; 16414; -.
DR GeneID; 16414; -.
DR KEGG; mmu:16414; -.
DR CTD; 3689; -.
DR MGI; MGI:96611; Itgb2.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; P11835; -.
DR OrthoDB; 473040at2759; -.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 16414; 6 hits in 73 CRISPR screens.
DR PRO; PR:P11835; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P11835; protein.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0034687; C:integrin alphaL-beta2 complex; ISO:MGI.
DR GO; GO:0034688; C:integrin alphaM-beta2 complex; IMP:ARUK-UCL.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IMP:ARUK-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0001851; F:complement component C3b binding; IGI:ARUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0030369; F:ICAM-3 receptor activity; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0045123; P:cellular extravasation; IMP:MGI.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; ISO:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISO:MGI.
DR GO; GO:0030101; P:natural killer cell activation; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR GO; GO:1990266; P:neutrophil migration; ISO:MGI.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:ARUK-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IMP:UniProtKB.
DR GO; GO:0043315; P:positive regulation of neutrophil degranulation; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:0043113; P:receptor clustering; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015439; Integrin_bsu-2.
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; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF15; PTHR10082:SF15; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 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; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 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; 3.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Integrin; Membrane; Metal-binding; Phagocytosis; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT CHAIN 24..771
FT /note="Integrin beta-2"
FT /id="PRO_0000016342"
FT TOPO_DOM 24..702
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..725
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 726..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 125..364
FT /note="VWFA"
FT REPEAT 450..497
FT /note="I"
FT REPEAT 498..541
FT /note="II"
FT REPEAT 542..582
FT /note="III"
FT REPEAT 583..618
FT /note="IV"
FT REGION 450..618
FT /note="Cysteine-rich tandem repeats"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 760
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 762
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..44
FT /evidence="ECO:0000250"
FT DISULFID 34..448
FT /evidence="ECO:0000250"
FT DISULFID 37..63
FT /evidence="ECO:0000250"
FT DISULFID 47..74
FT /evidence="ECO:0000250"
FT DISULFID 192..199
FT /evidence="ECO:0000250"
FT DISULFID 247..287
FT /evidence="ECO:0000250"
FT DISULFID 387..401
FT /evidence="ECO:0000250"
FT DISULFID 421..446
FT /evidence="ECO:0000250"
FT DISULFID 450..468
FT /evidence="ECO:0000250"
FT DISULFID 460..471
FT /evidence="ECO:0000250"
FT DISULFID 473..482
FT /evidence="ECO:0000250"
FT DISULFID 484..515
FT /evidence="ECO:0000250"
FT DISULFID 498..513
FT /evidence="ECO:0000250"
FT DISULFID 507..518
FT /evidence="ECO:0000250"
FT DISULFID 520..535
FT /evidence="ECO:0000250"
FT DISULFID 537..560
FT /evidence="ECO:0000250"
FT DISULFID 542..558
FT /evidence="ECO:0000250"
FT DISULFID 550..563
FT /evidence="ECO:0000250"
FT DISULFID 565..574
FT /evidence="ECO:0000250"
FT DISULFID 576..599
FT /evidence="ECO:0000250"
FT DISULFID 583..597
FT /evidence="ECO:0000250"
FT DISULFID 591..602
FT /evidence="ECO:0000250"
FT DISULFID 604..613
FT /evidence="ECO:0000250"
FT DISULFID 616..619
FT /evidence="ECO:0000250"
FT DISULFID 623..664
FT /evidence="ECO:0000250"
FT DISULFID 630..649
FT /evidence="ECO:0000250"
FT DISULFID 633..645
FT /evidence="ECO:0000250"
FT DISULFID 672..697
FT /evidence="ECO:0000250"
FT CONFLICT 4..6
FT /note="LRP -> PH (in Ref. 1; CAA33077)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="Q -> H (in Ref. 2; AAA39325)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="R -> K (in Ref. 2; AAA39325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 771 AA; 85026 MW; 6FA51DA93AB40D8A CRC64;
MLGLRPSLLL ALAGLFFLGS AVSQECTKYK VSSCRDCIQS GPGCSWCQKL NFTGPGEPDS
LRCDTRAQLL LKGCPADDIM DPRSIANPEF DQRGQRKQLS PQKVTLYLRP GQAAAFNVTF
RRAKGYPIDL YYLMDLSYSM LDDLNNVKKL GGDLLQALNE ITESGRIGFG SFVDKTVLPF
VNTHPEKLRN PCPNKEKACQ PPFAFRHVLK LTDNSNQFQT EVGKQLISGN LDAPEGGLDA
IMQVAACPEE IGWRNVTRLL VFATDDGFHF AGDGKLGAIL TPNDGRCHLE DNMYKRSNEF
DYPSVGQLAH KLSESNIQPI FAVTKKMVKT YEKLTEIIPK SAVGELSDDS SNVVQLIKNA
YYKLSSRVFL DHSTLPDTLK VTYDSFCSNG ASSIGKSRGD CDGVQINNPV TFQVKVMASE
CIQEQSFVIR ALGFTDTVTV QVRPQCECQC RDQSREQSLC GGKGVMECGI CRCESGYIGK
NCECQTQGRS SQELERNCRK DNSSIVCSGL GDCICGQCVC HTSDVPNKEI FGQYCECDNV
NCERYNSQVC GGSDRGSCNC GKCSCKPGYE GSACQCQRST TGCLNARLVE CSGRGHCQCN
RCICDEGYQP PMCEDCPSCG SHCRDNHTSC AECLKFDKGP FEKNCSVQCA GMTLQTIPLK
KKPCKERDSE GCWITYTLQQ KDGRNIYNIH VEDSLECVKG PNVAAIVGGT VVGVVLIGVL
LLVIWKALTH LTDLREYRRF EKEKLKSQWN NDNPLFKSAT TTVMNPKFAE S
