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Database: UniProt
Entry: P32592
LinkDB: P32592
Original site: P32592 
ID   ITB2_BOVIN              Reviewed;         769 AA.
AC   P32592;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   10-APR-2019, entry version 158.
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; Synonyms=CD18;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1351021; DOI=10.1016/0378-1119(92)90586-E;
RA   Shuster D.E., Bosworth B.T., Kehrli M.E. Jr.;
RT   "Sequence of the bovine CD18-encoding cDNA: comparison with the human
RT   and murine glycoproteins.";
RL   Gene 114:267-271(1992).
RN   [2]
RP   VARIANT LAD GLY-128, AND DISEASE.
RX   PubMed=1384046; DOI=10.1073/pnas.89.19.9225;
RA   Shuster D.E., Kehrli M.E. Jr., Ackermann M.R., Gilbert R.O.;
RT   "Identification and prevalence of a genetic defect that causes
RT   leukocyte adhesion deficiency in Holstein cattle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:9225-9229(1992).
CC   -!- FUNCTION: Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2,
CC       ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are
CC       receptors for the iC3b fragment of the third complement component
CC       and for fibrinogen. Integrin alpha-X/beta-2 recognizes the
CC       sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2
CC       recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin
CC       alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-
CC       D/beta-2 is a receptor for ICAM3 and VCAM1. Contributes to natural
CC       killer cell cytotoxicity. Involved in leukocyte adhesion and
CC       transmigration of leukocytes including T-cells and neutrophils.
CC       Triggers neutrophil transmigration during lung injury through
CC       PTK2B/PYK2-mediated activation. Integrin alpha-L/beta-2 in
CC       association with ICAM3, contributes to apoptotic neutrophil
CC       phagocytosis by macrophages. {ECO:0000250|UniProtKB:P05107}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-2
CC       associates with either alpha-L, alpha-M, alpha-X or alpha-D.
CC       Interacts with COPS5 and RANBP9. Interacts with FGR. Interacts
CC       with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23).
CC       Interacts with THBD. {ECO:0000250|UniProtKB:P05107}.
CC   -!- INTERACTION:
CC       Q7BHI8:lktA (xeno); NbExp=3; IntAct=EBI-11509482, EBI-11580242;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- DISEASE: Note=Defects in ITGB2 are the cause of leukocyte adhesion
CC       deficiency (LAD). The mutation causing LAD (Gly-128) is prevalent
CC       among Holstein cattle throughout the world, placing this disorder
CC       among the most common genetic diseases known in animal
CC       agriculture. All cattle with the mutant allele are related to one
CC       bull, who through the use of artificial insemination sired many
CC       calves in the 1950s and 1960s. {ECO:0000269|PubMed:1384046}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; M81233; AAA30438.1; -; mRNA.
DR   PIR; JC1121; JC1121.
DR   RefSeq; NP_786975.1; NM_175781.1.
DR   RefSeq; XP_015329203.1; XM_015473717.1.
DR   UniGene; Bt.63143; -.
DR   ProteinModelPortal; P32592; -.
DR   SMR; P32592; -.
DR   IntAct; P32592; 1.
DR   STRING; 9913.ENSBTAP00000022687; -.
DR   PaxDb; P32592; -.
DR   PeptideAtlas; P32592; -.
DR   PRIDE; P32592; -.
DR   Ensembl; ENSBTAT00000076413; ENSBTAP00000069668; ENSBTAG00000017060.
DR   GeneID; 281877; -.
DR   KEGG; bta:281877; -.
DR   CTD; 3689; -.
DR   VGNC; VGNC:30327; ITGB2.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P32592; -.
DR   KO; K06464; -.
DR   OMA; KECQAPF; -.
DR   OrthoDB; 473040at2759; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-BTA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR   Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-BTA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-BTA-216083; Integrin cell surface interactions.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000017060; Expressed in 9 organ(s), highest expression level in spleen.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
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:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
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; 2.
DR   PROSITE; PS00243; INTEGRIN_BETA; 3.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Complete proteome; Disease mutation;
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     22       {ECO:0000250}.
FT   CHAIN        23    769       Integrin beta-2.
FT                                /FTId=PRO_0000016340.
FT   TOPO_DOM     23    700       Extracellular. {ECO:0000255}.
FT   TRANSMEM    701    723       Helical. {ECO:0000255}.
FT   TOPO_DOM    724    769       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      124    363       VWFA.
FT   REPEAT      449    496       I.
FT   REPEAT      497    540       II.
FT   REPEAT      541    581       III.
FT   REPEAT      582    617       IV.
FT   REGION      449    617       Cysteine-rich tandem repeats.
FT   MOTIF       397    399       Cell attachment site. {ECO:0000255}.
FT   METAL       138    138       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       141    141       Calcium. {ECO:0000250}.
FT   METAL       142    142       Calcium. {ECO:0000250}.
FT   METAL       347    347       Calcium. {ECO:0000250}.
FT   MOD_RES      23     23       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     745    745       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     756    756       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     758    758       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     760    760       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    116    116       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    254    254       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    501    501       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    642    642       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     25     43       {ECO:0000250}.
FT   DISULFID     33    447       {ECO:0000250}.
FT   DISULFID     36     62       {ECO:0000250}.
FT   DISULFID     46     73       {ECO:0000250}.
FT   DISULFID    191    198       {ECO:0000250}.
FT   DISULFID    246    286       {ECO:0000250}.
FT   DISULFID    386    400       {ECO:0000250}.
FT   DISULFID    420    445       {ECO:0000250}.
FT   DISULFID    449    467       {ECO:0000250}.
FT   DISULFID    459    470       {ECO:0000250}.
FT   DISULFID    472    481       {ECO:0000250}.
FT   DISULFID    483    514       {ECO:0000250}.
FT   DISULFID    497    512       {ECO:0000250}.
FT   DISULFID    506    517       {ECO:0000250}.
FT   DISULFID    519    534       {ECO:0000250}.
FT   DISULFID    536    559       {ECO:0000250}.
FT   DISULFID    541    557       {ECO:0000250}.
FT   DISULFID    549    562       {ECO:0000250}.
FT   DISULFID    564    573       {ECO:0000250}.
FT   DISULFID    575    598       {ECO:0000250}.
FT   DISULFID    582    596       {ECO:0000250}.
FT   DISULFID    590    601       {ECO:0000250}.
FT   DISULFID    603    612       {ECO:0000250}.
FT   DISULFID    615    618       {ECO:0000250}.
FT   DISULFID    622    662       {ECO:0000250}.
FT   DISULFID    628    647       {ECO:0000250}.
FT   DISULFID    631    643       {ECO:0000250}.
FT   DISULFID    670    695       {ECO:0000250}.
FT   VARIANT     128    128       D -> G (in LAD).
FT                                {ECO:0000269|PubMed:1384046}.
SQ   SEQUENCE   769 AA;  84400 MW;  5903ADF4E8998CEA CRC64;
     MLRQRPQLLL LAGLLALQSV LSQECTNYKV STCRDCIESG PGCAWCQKLN FTGQGEPDSI
     RCDTRAELLS KGCPADDIME PKSLAETRDS QAGSRKQLSP QEVTLYLRPG QAVAFNVTFR
     RAKGYPIDLY YLMDLSYSMV DDLVNVKKLG GDLLRALNGI TESGRIGFGS FVDKTVLPFV
     NTHPEKLRNP CPNKEKECQP PFAFRHVLKL TDNSKQFETE VGKQLISGNL DAPEGGLDAM
     MQVAACPEEI GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKSSNEFD
     YPSVGQLAHK LAESNIQPIF AVTKKMVKTY EKLTEIIPKS AVGELSEDSR NVVELIKNAY
     NKLSSRVFLD HSTLPDTLKV TYDSFCSNGK SQVDQPRGDC DGVQINVPIT FQVKVTATEC
     IQQQSFTIRA LGFTDTVTVR VLPQCECQCR DASRDGSICG GRGSMECGVC RCDAGYIGKN
     CECQTQGRSS QELEGSCRKD NSSIICSGLG DCICGQCVCH TSDVPNKKIY GQFCECDNVN
     CERYDGQVCG GEKRGLCFCG TCRCDEQYEG SACQCLKSTQ GCLNLDGVEC SGRGRCRCNV
     CQCDPGYQPP LCSECPGCPV PCAGFAPCTE CLKFDKGPFA KNCSAACGQT KLLSSPVPGR
     KCKERDSEGC WMTYTLVQRD GRDRYDVHVD DMLECVKGPN IAAIVGGTVG GVVLVGILLL
     VIWKALTHLS DLREYHRFEK EKLKSQWNND NPLFKSATTT VMNPKFAES
//
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