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Database: UniProt
Entry: P11835
LinkDB: P11835
Original site: P11835 
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   13-FEB-2019, entry version 184.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   protein 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.,
RA   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
RT   transmigration in sepsis-induced lung inflammation by activating beta2
RT   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
RT   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,
CC       ICAM3 and ICAM4. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are
CC       receptors for the iC3b fragment of the third complement component
CC       and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence
CC       G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes
CC       P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2
CC       is also a receptor for factor X. Integrin ITGAD/ITGB2 is a
CC       receptor for ICAM3 and VCAM1. Contributes to natural killer cell
CC       cytotoxicity (By similarity). Involved in leukocyte adhesion and
CC       transmigration of leukocytes including T-cells and neutrophils (By
CC       similarity). Triggers neutrophil transmigration during lung injury
CC       through PTK2B/PYK2-mediated activation (PubMed:18587400). Integrin
CC       ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic
CC       neutrophil phagocytosis by macrophages (By similarity). In
CC       association with alpha subunit ITGAM/CD11b, required for CD177-
CC       PRTN3-mediated activation of TNF primed neutrophils (By
CC       similarity). Alpha-M/beta-2 play a critical role in mast cell
CC       development and in immune complex-mediated glomerulonephritis.
CC       Mice expressing a null mutation of the alpha-M subunit gene
CC       demonstrate increase in neutrophil accumulation, in response to a
CC       impaired degranulation and phagocytosis, events that apparently
CC       accelerate 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. ITGB2
CC       associates with either ITGAL, ITGAM, ITGAX or ITGAD. Found in a
CC       complex with CD177 and ITGAM/CD11b (By similarity). Interacts with
CC       FGR (PubMed:19903482). Interacts with COPS5 and RANBP9 (By
CC       similarity). Interacts with FLNA (via filamin repeats 4, 9, 12,
CC       17, 19, 21, and 23) (By similarity).
CC       {ECO:0000250|UniProtKB:P05107, ECO:0000269|PubMed:19903482}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P05107}. Membrane raft
CC       {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P05107}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
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   UniGene; Mm.1137; -.
DR   ProteinModelPortal; P11835; -.
DR   SMR; P11835; -.
DR   BioGrid; 200828; 2.
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; 9.
DR   MINT; P11835; -.
DR   STRING; 10090.ENSMUSP00000000299; -.
DR   iPTMnet; P11835; -.
DR   PhosphoSitePlus; P11835; -.
DR   SwissPalm; P11835; -.
DR   EPD; P11835; -.
DR   MaxQB; P11835; -.
DR   PaxDb; P11835; -.
DR   PeptideAtlas; P11835; -.
DR   PRIDE; P11835; -.
DR   GeneID; 16414; -.
DR   KEGG; mmu:16414; -.
DR   CTD; 3689; -.
DR   MGI; MGI:96611; Itgb2.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P11835; -.
DR   KO; K06464; -.
DR   OrthoDB; 473040at2759; -.
DR   PRO; PR:P11835; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0009986; C:cell surface; 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:0008305; C:integrin complex; IBA:GO_Central.
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:0046982; F:protein heterodimerization activity; ISO:MGI.
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: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; Complete proteome;
KW   Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding;
KW   Phagocytosis; Phosphoprotein; Pyrrolidone carboxylic acid; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23
FT   CHAIN        24    771       Integrin beta-2.
FT                                /FTId=PRO_0000016342.
FT   TOPO_DOM     24    702       Extracellular. {ECO:0000255}.
FT   TRANSMEM    703    725       Helical. {ECO:0000255}.
FT   TOPO_DOM    726    771       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      125    364       VWFA.
FT   REPEAT      450    497       I.
FT   REPEAT      498    541       II.
FT   REPEAT      542    582       III.
FT   REPEAT      583    618       IV.
FT   REGION      450    618       Cysteine-rich tandem repeats.
FT   METAL       139    139       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       142    142       Calcium. {ECO:0000250}.
FT   METAL       143    143       Calcium. {ECO:0000250}.
FT   METAL       348    348       Calcium. {ECO:0000250}.
FT   MOD_RES      24     24       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     747    747       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     758    758       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     760    760       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     762    762       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   CARBOHYD     51     51       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    117    117       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    255    255       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    502    502       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    626    626       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    644    644       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     26     44       {ECO:0000250}.
FT   DISULFID     34    448       {ECO:0000250}.
FT   DISULFID     37     63       {ECO:0000250}.
FT   DISULFID     47     74       {ECO:0000250}.
FT   DISULFID    192    199       {ECO:0000250}.
FT   DISULFID    247    287       {ECO:0000250}.
FT   DISULFID    387    401       {ECO:0000250}.
FT   DISULFID    421    446       {ECO:0000250}.
FT   DISULFID    450    468       {ECO:0000250}.
FT   DISULFID    460    471       {ECO:0000250}.
FT   DISULFID    473    482       {ECO:0000250}.
FT   DISULFID    484    515       {ECO:0000250}.
FT   DISULFID    498    513       {ECO:0000250}.
FT   DISULFID    507    518       {ECO:0000250}.
FT   DISULFID    520    535       {ECO:0000250}.
FT   DISULFID    537    560       {ECO:0000250}.
FT   DISULFID    542    558       {ECO:0000250}.
FT   DISULFID    550    563       {ECO:0000250}.
FT   DISULFID    565    574       {ECO:0000250}.
FT   DISULFID    576    599       {ECO:0000250}.
FT   DISULFID    583    597       {ECO:0000250}.
FT   DISULFID    591    602       {ECO:0000250}.
FT   DISULFID    604    613       {ECO:0000250}.
FT   DISULFID    616    619       {ECO:0000250}.
FT   DISULFID    623    664       {ECO:0000250}.
FT   DISULFID    630    649       {ECO:0000250}.
FT   DISULFID    633    645       {ECO:0000250}.
FT   DISULFID    672    697       {ECO:0000250}.
FT   CONFLICT      4      6       LRP -> PH (in Ref. 1; CAA33077).
FT                                {ECO:0000305}.
FT   CONFLICT    449    449       Q -> H (in Ref. 2; AAA39325).
FT                                {ECO:0000305}.
FT   CONFLICT    667    667       R -> K (in Ref. 2; AAA39325).
FT                                {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
//
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