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Database: UniProt
Entry: P05107
LinkDB: P05107
Original site: P05107 
ID   ITB2_HUMAN              Reviewed;         769 AA.
AC   P05107; B3KTS8; D3DSM1; Q16418; Q53HS5; Q9UD72;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-JUN-2021, entry version 255.
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, MFI7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-354.
RX   PubMed=3028646; DOI=10.1016/0092-8674(87)90246-7;
RA   Kishimoto T.K., O'Connor K., Lee A., Roberts T.M., Springer T.A.;
RT   "Cloning of the beta subunit of the leukocyte adhesion proteins: homology
RT   to an extracellular matrix receptor defines a novel supergene family.";
RL   Cell 48:681-690(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-354.
RX   PubMed=1683838; DOI=10.1016/0014-5793(91)81351-8;
RA   Weitzman J.B., Wells C.E., Wright A.H., Clark P.A., Law S.K.A.;
RT   "The gene organisation of the human beta 2 integrin subunit (CD18).";
RL   FEBS Lett. 294:97-103(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-354.
RC   TISSUE=Synovial cell;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-354.
RC   TISSUE=Adipose tissue;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-354.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-354.
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-769, PARTIAL PROTEIN SEQUENCE,
RP   PYROGLUTAMATE FORMATION AT GLN-23, AND VARIANT HIS-354.
RC   TISSUE=Spleen;
RX   PubMed=2954816; DOI=10.1002/j.1460-2075.1987.tb04838.x;
RA   Law S.K.A., Gagnon J., Hildreth J.E., Wells C.E., Willis A.C., Wong A.J.;
RT   "The primary structure of the beta-subunit of the cell surface adhesion
RT   glycoproteins LFA-1, CR3 and p150,95 and its relationship to the
RT   fibronectin receptor.";
RL   EMBO J. 6:915-919(1987).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 124-199, AND VARIANT LAD1 LEU-178.
RC   TISSUE=Lymphoblast;
RX   PubMed=7509236; DOI=10.1002/humu.1380020606;
RA   Ohashi Y., Yambe T., Tsuchiya S., Kikuchi H., Konno T.;
RT   "Familial genetic defect in a case of leukocyte adhesion deficiency.";
RL   Hum. Mutat. 2:458-467(1993).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 347-355, VARIANTS LAD1 SER-351 AND TRP-586,
RP   AND VARIANT HIS-354.
RX   PubMed=1346613;
RA   Nelson C., Rabb H., Arnaout M.A.;
RT   "Genetic cause of leukocyte adhesion molecule deficiency. Abnormal splicing
RT   and a missense mutation in a conserved region of CD18 impair cell surface
RT   expression of beta 2 integrins.";
RL   J. Biol. Chem. 267:3351-3357(1992).
RN   [11]
RP   INTERACTION WITH COPS5.
RX   PubMed=10766246; DOI=10.1038/35007098;
RA   Bianchi E., Denti S., Granata A., Bossi G., Geginat J., Villa A., Rogge L.,
RA   Pardi R.;
RT   "Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to
RT   modulate AP-1 activity.";
RL   Nature 404:617-621(2000).
RN   [12]
RP   PHOSPHORYLATION AT SER-745; SER-756; THR-758 AND THR-760.
RX   PubMed=11700305; DOI=10.1074/jbc.m106856200;
RA   Fagerholm S., Morrice N., Gahmberg C.G., Cohen P.;
RT   "Phosphorylation of the cytoplasmic domain of the integrin CD18 chain by
RT   protein kinase C isoforms in leukocytes.";
RL   J. Biol. Chem. 277:1728-1738(2002).
RN   [13]
RP   FUNCTION.
RX   PubMed=11812992; DOI=10.1038/ni755;
RA   Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.;
RT   "JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in
RT   transendothelial migration of leukocytes.";
RL   Nat. Immunol. 3:151-158(2002).
RN   [14]
RP   INTERACTION WITH RANBP9.
RX   PubMed=14722085; DOI=10.1074/jbc.m313515200;
RA   Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S.,
RA   Fabbri M., Pardi R., Bianchi E.;
RT   "RanBPM is a phosphoprotein that associates with the plasma membrane and
RT   interacts with the integrin LFA-1.";
RL   J. Biol. Chem. 279:13027-13034(2004).
RN   [15]
RP   FUNCTION.
RX   PubMed=15356110; DOI=10.4049/jimmunol.173.6.3653;
RA   Barber D.F., Faure M., Long E.O.;
RT   "LFA-1 contributes an early signal for NK cell cytotoxicity.";
RL   J. Immunol. 173:3653-3659(2004).
RN   [16]
RP   PHOSPHORYLATION AT THR-758, AND MUTAGENESIS OF THR-758.
RX   PubMed=16301335; DOI=10.1083/jcb.200504016;
RA   Fagerholm S.C., Hilden T.J., Nurmi S.M., Gahmberg C.G.;
RT   "Specific integrin alpha and beta chain phosphorylations regulate LFA-1
RT   activation through affinity-dependent and -independent mechanisms.";
RL   J. Cell Biol. 171:705-715(2005).
RN   [17]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [18]
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   [19]
RP   INTERACTION WITH FLNA.
RX   PubMed=19828450; DOI=10.1074/jbc.m109.060954;
RA   Ithychanda S.S., Hsu D., Li H., Yan L., Liu D.D., Liu D., Das M.,
RA   Plow E.F., Qin J.;
RT   "Identification and characterization of multiple similar ligand-binding
RT   repeats in filamin: implication on filamin-mediated receptor clustering and
RT   cross-talk.";
RL   J. Biol. Chem. 284:35113-35121(2009).
RN   [20]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-212.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [21]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50; ASN-116 AND ASN-212.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [22]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGAM, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=21193407; DOI=10.1074/jbc.m110.171256;
RA   Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A., Luft F.,
RA   Kettritz R.;
RT   "Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-ANCA
RT   neutrophil activation.";
RL   J. Biol. Chem. 286:7070-7081(2011).
RN   [23]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23775590; DOI=10.1007/s10495-013-0873-z;
RA   Kristof E., Zahuczky G., Katona K., Doro Z., Nagy E., Fesues L.;
RT   "Novel role of ICAM3 and LFA-1 in the clearance of apoptotic neutrophils by
RT   human macrophages.";
RL   Apoptosis 18:1235-1251(2013).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [25]
RP   INTERACTION WITH THBD.
RX   PubMed=27055590; DOI=10.1016/j.bbrc.2016.04.007;
RA   Kawamoto E., Okamoto T., Takagi Y., Honda G., Suzuki K., Imai H.,
RA   Shimaoka M.;
RT   "LFA-1 and Mac-1 integrins bind to the serine/threonine-rich domain of
RT   thrombomodulin.";
RL   Biochem. Biophys. Res. Commun. 473:1005-1012(2016).
RN   [26]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGAM, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=28807980; DOI=10.1182/blood-2017-03-768507;
RA   Bai M., Grieshaber-Bouyer R., Wang J., Schmider A.B., Wilson Z.S., Zeng L.,
RA   Halyabar O., Godin M.D., Nguyen H.N., Levescot A., Cunin P., Lefort C.T.,
RA   Soberman R.J., Nigrovic P.A.;
RT   "CD177 modulates human neutrophil migration through activation-mediated
RT   integrin and chemoreceptor regulation.";
RL   Blood 130:2092-2100(2017).
RN   [27]
RP   FUNCTION.
RX   PubMed=29100055; DOI=10.1016/j.molcel.2017.10.003;
RA   Swaim C.D., Scott A.F., Canadeo L.A., Huibregtse J.M.;
RT   "Extracellular ISG15 signals cytokine secretion through the LFA-1 integrin
RT   receptor.";
RL   Mol. Cell 68:581-590(2017).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 23-699 IN COMPLEX WITH ITGAX,
RP   GLYCOSYLATION AT ASN-116, DISULFIDE BONDS, CALCIUM-BINDING SITES, AND
RP   SUBUNIT.
RX   PubMed=20033057; DOI=10.1038/emboj.2009.367;
RA   Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A.;
RT   "Structure of an integrin with an alphaI domain, complement receptor type
RT   4.";
RL   EMBO J. 29:666-679(2010).
RN   [29]
RP   VARIANTS LAD1 THR-196 AND CYS-593.
RX   PubMed=1968911; DOI=10.1172/jci114529;
RA   Arnaout M.A., Dana N., Gupta S.K., Tenen D.G., Fathallah D.M.;
RT   "Point mutations impairing cell surface expression of the common beta
RT   subunit (CD18) in a patient with leukocyte adhesion molecule (Leu-CAM)
RT   deficiency.";
RL   J. Clin. Invest. 85:977-981(1990).
RN   [30]
RP   VARIANTS LAD1 PRO-149 AND ARG-169.
RX   PubMed=1694220; DOI=10.1084/jem.172.1.335;
RA   Wardlaw A.J., Hibbs M.L., Stacker S.A., Springer T.A.;
RT   "Distinct mutations in two patients with leukocyte adhesion deficiency and
RT   their functional correlates.";
RL   J. Exp. Med. 172:335-345(1990).
RN   [31]
RP   VARIANT LAD1 ASN-128.
RX   PubMed=1590804; DOI=10.1016/s0006-291x(05)80047-6;
RA   Matsuura S., Kishi F., Tsukahara M., Nunoi H., Matsuda I., Kobayashi K.,
RA   Kajii T.;
RT   "Leukocyte adhesion deficiency: identification of novel mutations in two
RT   Japanese patients with a severe form.";
RL   Biochem. Biophys. Res. Commun. 184:1460-1467(1992).
RN   [32]
RP   VARIANT LAD1 ARG-169.
RX   PubMed=1352501; DOI=10.1002/eji.1830220730;
RA   Corbi A., Vara A., Ursa A., Rodriguez M.C.G., Fontan G., Sanchez-Madrid F.;
RT   "Molecular basis for a severe case of leukocyte adhesion deficiency.";
RL   Eur. J. Immunol. 22:1877-1881(1992).
RN   [33]
RP   VARIANT LAD1 LEU-178.
RX   PubMed=1347532;
RA   Back L.L., Kwok W.W., Hickstein D.D.;
RT   "Identification of two molecular defects in a child with leukocyte
RT   adherence deficiency.";
RL   J. Biol. Chem. 267:5482-5487(1992).
RN   [34]
RP   VARIANT LAD1 SER-284.
RX   PubMed=7686755; DOI=10.1006/bbrc.1993.1712;
RA   Back L.A., Kerkering M., Baker D., Bauer T.R., Embree L.J., Hickstein D.D.;
RT   "A point mutation associated with leukocyte adhesion deficiency type 1 of
RT   moderate severity.";
RL   Biochem. Biophys. Res. Commun. 193:912-918(1993).
RN   [35]
RP   VARIANTS LAD1 PRO-138 AND ARG-273.
RX   PubMed=9884339; DOI=10.1172/jci3312;
RA   Hogg N., Stewart M.P., Scarth S.L., Newton R., Shaw J.M., Law S.K.A.,
RA   Klein N.;
RT   "A novel leukocyte adhesion deficiency caused by expressed but
RT   nonfunctional beta2 integrins Mac-1 and LFA-1.";
RL   J. Clin. Invest. 103:97-106(1999).
RN   [36]
RP   VARIANT LAD1 VAL-300.
RX   PubMed=20529581;
RA   Li L., Jin Y.Y., Cao R.M., Chen T.X.;
RT   "A novel point mutation in CD18 causing leukocyte adhesion deficiency in a
RT   Chinese patient.";
RL   Chin. Med. J. 123:1278-1282(2010).
RN   [37]
RP   VARIANTS LAD1 TYR-128; THR-239 AND ALA-716.
RX   PubMed=20549317; DOI=10.1007/s10875-010-9433-2;
RA   Parvaneh N., Mamishi S., Rezaei A., Rezaei N., Tamizifar B., Parvaneh L.,
RA   Sherkat R., Ghalehbaghi B., Kashef S., Chavoshzadeh Z., Isaeian A.,
RA   Ashrafi F., Aghamohammadi A.;
RT   "Characterization of 11 new cases of leukocyte adhesion deficiency type 1
RT   with seven novel mutations in the ITGB2 gene.";
RL   J. Clin. Immunol. 30:756-760(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 (PubMed:29100055). 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
CC       (PubMed:15356110). Involved in leukocyte adhesion and transmigration of
CC       leukocytes including T-cells and neutrophils (PubMed:11812992,
CC       PubMed:28807980). 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 (PubMed:23775590). In
CC       association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-
CC       mediated activation of TNF primed neutrophils (PubMed:21193407).
CC       {ECO:0000269|PubMed:11812992, ECO:0000269|PubMed:15356110,
CC       ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:21193407,
CC       ECO:0000269|PubMed:23775590, ECO:0000269|PubMed:28807980,
CC       ECO:0000269|PubMed:29100055}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:20033057).
CC       The ITGB2 beta subunit associates with the ITGAL, ITGAM, ITGAX or ITGAD
CC       alpha subunits. Found in a complex with CD177 and ITGAM/CD11b
CC       (PubMed:21193407, PubMed:28807980). Interacts with FGR (By similarity).
CC       Interacts with COPS5 and RANBP9 (PubMed:10766246, PubMed:14722085).
CC       Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23)
CC       (PubMed:19828450). Interacts with THBD (PubMed:27055590).
CC       {ECO:0000250|UniProtKB:P11835, ECO:0000269|PubMed:10766246,
CC       ECO:0000269|PubMed:14722085, ECO:0000269|PubMed:19828450,
CC       ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:21193407,
CC       ECO:0000269|PubMed:27055590, ECO:0000269|PubMed:28807980}.
CC   -!- INTERACTION:
CC       P05107; P00519: ABL1; NbExp=4; IntAct=EBI-300173, EBI-375543;
CC       P05107; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-300173, EBI-10173507;
CC       P05107; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-300173, EBI-4290634;
CC       P05107; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-300173, EBI-3867333;
CC       P05107; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-300173, EBI-6425864;
CC       P05107; P20702: ITGAX; NbExp=3; IntAct=EBI-300173, EBI-2568308;
CC       P05107; Q14145: KEAP1; NbExp=3; IntAct=EBI-300173, EBI-751001;
CC       P05107; Q15323: KRT31; NbExp=3; IntAct=EBI-300173, EBI-948001;
CC       P05107; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-300173, EBI-10171774;
CC       P05107; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-300173, EBI-2820517;
CC       P05107; Q9GZW8: MS4A7; NbExp=3; IntAct=EBI-300173, EBI-721391;
CC       P05107; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-300173, EBI-3923617;
CC       P05107; Q7Z3S9: NOTCH2NLA; NbExp=7; IntAct=EBI-300173, EBI-945833;
CC       P05107; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-300173, EBI-22310682;
CC       P05107; P35241: RDX; NbExp=2; IntAct=EBI-300173, EBI-2514878;
CC       P05107; Q9UN30-2: SCML1; NbExp=3; IntAct=EBI-300173, EBI-12137487;
CC       P05107; Q15582: TGFBI; NbExp=2; IntAct=EBI-300173, EBI-10236573;
CC       P05107; Q9Y4G6: TLN2; NbExp=5; IntAct=EBI-300173, EBI-1220811;
CC       P05107; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-300173, EBI-13351685;
CC       P05107; O75841: UPK1B; NbExp=3; IntAct=EBI-300173, EBI-12237619;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21193407,
CC       ECO:0000269|PubMed:28807980}; Single-pass type I membrane protein
CC       {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:21193407}; Single-pass
CC       type I membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Leukocytes (PubMed:23775590). Expressed in
CC       neutrophils (at protein level) (PubMed:21193407, PubMed:28807980).
CC       {ECO:0000269|PubMed:21193407, ECO:0000269|PubMed:23775590,
CC       ECO:0000269|PubMed:28807980}.
CC   -!- PTM: Both Ser-745 and Ser-756 become phosphorylated when T-cells are
CC       exposed to phorbol esters (PubMed:11700305). Phosphorylation on Thr-758
CC       (but not on Ser-756) allows interaction with 14-3-3 proteins
CC       (PubMed:11700305, PubMed:16301335). {ECO:0000269|PubMed:11700305,
CC       ECO:0000269|PubMed:16301335}.
CC   -!- DISEASE: Leukocyte adhesion deficiency 1 (LAD1) [MIM:116920]: LAD1
CC       patients have recurrent bacterial infections and their leukocytes are
CC       deficient in a wide range of adhesion-dependent functions.
CC       {ECO:0000269|PubMed:1346613, ECO:0000269|PubMed:1347532,
CC       ECO:0000269|PubMed:1352501, ECO:0000269|PubMed:1590804,
CC       ECO:0000269|PubMed:1694220, ECO:0000269|PubMed:1968911,
CC       ECO:0000269|PubMed:20529581, ECO:0000269|PubMed:20549317,
CC       ECO:0000269|PubMed:7509236, ECO:0000269|PubMed:7686755,
CC       ECO:0000269|PubMed:9884339}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD96225.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=ITGB2base; Note=ITGB2 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/ITGB2base/";
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DR   EMBL; M15395; AAA59490.1; -; mRNA.
DR   EMBL; X64072; CAA45427.1; -; Genomic_DNA.
DR   EMBL; X64073; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64074; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64075; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64076; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64077; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64078; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64079; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64080; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64081; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64082; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X64083; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X63924; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X63925; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; X63926; CAA45427.1; JOINED; Genomic_DNA.
DR   EMBL; AK095992; BAG53190.1; -; mRNA.
DR   EMBL; AK222505; BAD96225.1; ALT_INIT; mRNA.
DR   EMBL; AL163300; CAB90553.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09381.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09382.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09385.1; -; Genomic_DNA.
DR   EMBL; BC005861; AAH05861.1; -; mRNA.
DR   EMBL; Y00057; CAA68266.1; -; mRNA.
DR   EMBL; S81234; AAB21404.1; -; mRNA.
DR   CCDS; CCDS13716.1; -.
DR   PIR; A25967; IJHULM.
DR   RefSeq; NP_000202.3; NM_000211.4.
DR   RefSeq; NP_001120963.2; NM_001127491.2.
DR   RefSeq; NP_001290167.1; NM_001303238.1.
DR   PDB; 1JX3; Model; -; A=126-364.
DR   PDB; 1L3Y; NMR; -; A=535-574.
DR   PDB; 1YUK; X-ray; 1.80 A; A=23-125, B=365-482.
DR   PDB; 2JF1; X-ray; 2.20 A; T=735-769.
DR   PDB; 2P26; X-ray; 1.75 A; A=23-535.
DR   PDB; 2P28; X-ray; 2.20 A; A=23-122, B=362-574.
DR   PDB; 2V7D; X-ray; 2.50 A; P/Q/R/S=755-764.
DR   PDB; 3K6S; X-ray; 3.50 A; B/D/F/H=23-699.
DR   PDB; 3K71; X-ray; 3.95 A; B/D/F/H=23-699.
DR   PDB; 3K72; X-ray; 3.70 A; B/D=23-699.
DR   PDB; 4NEH; X-ray; 2.75 A; B=23-695.
DR   PDB; 4NEN; X-ray; 2.90 A; B=23-696.
DR   PDB; 5E6R; X-ray; 2.90 A; B=23-482.
DR   PDB; 5E6S; X-ray; 2.15 A; B/D/F=23-482.
DR   PDB; 5E6U; X-ray; 2.50 A; B=23-482.
DR   PDB; 5E6V; X-ray; 1.80 A; A=24-482.
DR   PDB; 5E6W; X-ray; 2.20 A; A=23-118, A=362-574.
DR   PDB; 5E6X; X-ray; 1.75 A; A=23-535.
DR   PDB; 5ES4; X-ray; 3.30 A; B/D/F/H=23-696.
DR   PDB; 5XR1; NMR; -; A=752-763.
DR   PDB; 5ZAZ; NMR; -; A=689-739.
DR   PDBsum; 1JX3; -.
DR   PDBsum; 1L3Y; -.
DR   PDBsum; 1YUK; -.
DR   PDBsum; 2JF1; -.
DR   PDBsum; 2P26; -.
DR   PDBsum; 2P28; -.
DR   PDBsum; 2V7D; -.
DR   PDBsum; 3K6S; -.
DR   PDBsum; 3K71; -.
DR   PDBsum; 3K72; -.
DR   PDBsum; 4NEH; -.
DR   PDBsum; 4NEN; -.
DR   PDBsum; 5E6R; -.
DR   PDBsum; 5E6S; -.
DR   PDBsum; 5E6U; -.
DR   PDBsum; 5E6V; -.
DR   PDBsum; 5E6W; -.
DR   PDBsum; 5E6X; -.
DR   PDBsum; 5ES4; -.
DR   PDBsum; 5XR1; -.
DR   PDBsum; 5ZAZ; -.
DR   BMRB; P05107; -.
DR   SMR; P05107; -.
DR   BioGRID; 109895; 50.
DR   ComplexPortal; CPX-1825; Integrin alphaL-beta2 complex.
DR   ComplexPortal; CPX-1826; Integrin alphaM-beta2 complex.
DR   ComplexPortal; CPX-1827; Integrin alphaX-beta2 complex.
DR   ComplexPortal; CPX-1828; Integrin alphaD-beta2 complex.
DR   CORUM; P05107; -.
DR   DIP; DIP-478N; -.
DR   ELM; P05107; -.
DR   IntAct; P05107; 36.
DR   MINT; P05107; -.
DR   STRING; 9606.ENSP00000380948; -.
DR   BindingDB; P05107; -.
DR   ChEMBL; CHEMBL3631; -.
DR   DrugCentral; P05107; -.
DR   GuidetoPHARMACOLOGY; 2456; -.
DR   GlyConnect; 1415; 7 N-Linked glycans (3 sites).
DR   GlyGen; P05107; 11 sites.
DR   iPTMnet; P05107; -.
DR   PhosphoSitePlus; P05107; -.
DR   BioMuta; ITGB2; -.
DR   DMDM; 124056465; -.
DR   EPD; P05107; -.
DR   jPOST; P05107; -.
DR   MassIVE; P05107; -.
DR   MaxQB; P05107; -.
DR   PaxDb; P05107; -.
DR   PeptideAtlas; P05107; -.
DR   PRIDE; P05107; -.
DR   ProteomicsDB; 51793; -.
DR   ABCD; P05107; 55 sequenced antibodies.
DR   Antibodypedia; 1501; 2021 antibodies.
DR   DNASU; 3689; -.
DR   Ensembl; ENST00000302347; ENSP00000303242; ENSG00000160255.
DR   Ensembl; ENST00000355153; ENSP00000347279; ENSG00000160255.
DR   Ensembl; ENST00000397850; ENSP00000380948; ENSG00000160255.
DR   Ensembl; ENST00000397852; ENSP00000380950; ENSG00000160255.
DR   Ensembl; ENST00000397857; ENSP00000380955; ENSG00000160255.
DR   GeneID; 3689; -.
DR   KEGG; hsa:3689; -.
DR   UCSC; uc002zgd.4; human.
DR   CTD; 3689; -.
DR   DisGeNET; 3689; -.
DR   GeneCards; ITGB2; -.
DR   HGNC; HGNC:6155; ITGB2.
DR   HPA; ENSG00000160255; Tissue enhanced (blood, bone marrow, lymphoid tissue).
DR   MalaCards; ITGB2; -.
DR   MIM; 116920; phenotype.
DR   MIM; 600065; gene.
DR   neXtProt; NX_P05107; -.
DR   Orphanet; 99842; Leukocyte adhesion deficiency type I.
DR   PharmGKB; PA29955; -.
DR   VEuPathDB; HostDB:ENSG00000160255.16; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   HOGENOM; CLU_011772_2_1_1; -.
DR   InParanoid; P05107; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P05107; -.
DR   TreeFam; TF105392; -.
DR   PathwayCommons; P05107; -.
DR   Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; P05107; -.
DR   SIGNOR; P05107; -.
DR   BioGRID-ORCS; 3689; 11 hits in 988 CRISPR screens.
DR   ChiTaRS; ITGB2; human.
DR   EvolutionaryTrace; P05107; -.
DR   GeneWiki; CD18; -.
DR   GenomeRNAi; 3689; -.
DR   Pharos; P05107; Tclin.
DR   PRO; PR:P05107; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P05107; protein.
DR   Bgee; ENSG00000160255; Expressed in granulocyte and 204 other tissues.
DR   ExpressionAtlas; P05107; baseline and differential.
DR   Genevisible; P05107; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; NAS:ARUK-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR   GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0034687; C:integrin alphaL-beta2 complex; IDA:UniProtKB.
DR   GO; GO:0034688; C:integrin alphaM-beta2 complex; ISS:ARUK-UCL.
DR   GO; GO:0034689; C:integrin alphaX-beta2 complex; TAS:ARUK-UCL.
DR   GO; GO:0008305; C:integrin complex; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR   GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IMP:UniProtKB.
DR   GO; GO:0001851; F:complement component C3b binding; ISS:ARUK-UCL.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
DR   GO; GO:0030369; F:ICAM-3 receptor activity; IMP:UniProtKB.
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; IPI:UniProtKB.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
DR   GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
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; ISS:BHF-UCL.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; NAS:ARUK-UCL.
DR   GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0045123; P:cellular extravasation; IEA:Ensembl.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR   GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0001774; P:microglial cell activation; NAS:ARUK-UCL.
DR   GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
DR   GO; GO:0045963; P:negative regulation of dopamine metabolic process; NAS:ARUK-UCL.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:1990266; P:neutrophil migration; IMP:UniProtKB.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISS:UniProtKB.
DR   GO; GO:1901216; P:positive regulation of neuron death; NAS:ARUK-UCL.
DR   GO; GO:0043315; P:positive regulation of neutrophil degranulation; IGI:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; NAS:ARUK-UCL.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; NAS:ARUK-UCL.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IGI:UniProtKB.
DR   GO; GO:0043113; P:receptor clustering; IMP:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
DR   GO; GO:0008360; P:regulation of cell shape; NAS:UniProtKB.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
DR   DisProt; DP01848; -.
DR   Gene3D; 1.20.5.630; -; 1.
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; IPR037076; Integrin_bsu_cyt_dom_sf.
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   3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing;
KW   Disease variant; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW   Metal-binding; Phagocytosis; Phosphoprotein; Pyrrolidone carboxylic acid;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT   CHAIN           23..769
FT                   /note="Integrin beta-2"
FT                   /id="PRO_0000016341"
FT   TOPO_DOM        23..700
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        701..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        724..769
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          124..363
FT                   /note="VWFA"
FT   REPEAT          449..496
FT                   /note="I"
FT   REPEAT          497..540
FT                   /note="II"
FT   REPEAT          541..581
FT                   /note="III"
FT   REPEAT          582..617
FT                   /note="IV"
FT   REGION          449..617
FT                   /note="Cysteine-rich tandem repeats"
FT   MOTIF           397..399
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   METAL           138
FT                   /note="Calcium; via carbonyl oxygen"
FT   METAL           141
FT                   /note="Calcium"
FT   METAL           142
FT                   /note="Calcium"
FT   METAL           347
FT                   /note="Calcium"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:2954816"
FT   MOD_RES         745
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000269|PubMed:11700305"
FT   MOD_RES         756
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:11700305"
FT   MOD_RES         758
FT                   /note="Phosphothreonine; by PKC; in vitro"
FT                   /evidence="ECO:0000269|PubMed:11700305,
FT                   ECO:0000269|PubMed:16301335"
FT   MOD_RES         759
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         760
FT                   /note="Phosphothreonine; by PKC/PRKCA; in vitro"
FT                   /evidence="ECO:0000269|PubMed:11700305"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:19349973"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:20033057"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        642
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        25..43
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        33..447
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        36..62
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        46..73
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        191..198
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        246..286
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        386..400
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        420..445
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        449..467
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        459..470
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        472..481
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        483..514
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        497..512
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        506..517
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        519..534
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        536..559
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        541..557
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        549..562
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        564..573
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        575..598
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        582..596
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        590..601
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        603..612
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        615..618
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        622..662
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        628..647
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        631..643
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   DISULFID        670..695
FT                   /evidence="ECO:0000269|PubMed:20033057"
FT   VARIANT         128
FT                   /note="D -> N (in LAD1; dbSNP:rs137852615)"
FT                   /evidence="ECO:0000269|PubMed:1590804"
FT                   /id="VAR_003984"
FT   VARIANT         128
FT                   /note="D -> Y (in LAD1; dbSNP:rs137852615)"
FT                   /evidence="ECO:0000269|PubMed:20549317"
FT                   /id="VAR_065661"
FT   VARIANT         138
FT                   /note="S -> P (in LAD1; dbSNP:rs137852617)"
FT                   /evidence="ECO:0000269|PubMed:9884339"
FT                   /id="VAR_013402"
FT   VARIANT         149
FT                   /note="L -> P (in LAD1; dbSNP:rs137852611)"
FT                   /evidence="ECO:0000269|PubMed:1694220"
FT                   /id="VAR_003985"
FT   VARIANT         169
FT                   /note="G -> R (in LAD1; dbSNP:rs137852612)"
FT                   /evidence="ECO:0000269|PubMed:1352501,
FT                   ECO:0000269|PubMed:1694220"
FT                   /id="VAR_003986"
FT   VARIANT         178
FT                   /note="P -> L (in LAD1; dbSNP:rs137852614)"
FT                   /evidence="ECO:0000269|PubMed:1347532,
FT                   ECO:0000269|PubMed:7509236"
FT                   /id="VAR_003987"
FT   VARIANT         196
FT                   /note="K -> T (in LAD1; dbSNP:rs137852610)"
FT                   /evidence="ECO:0000269|PubMed:1968911"
FT                   /id="VAR_003988"
FT   VARIANT         239
FT                   /note="A -> T (in LAD1; dbSNP:rs179363873)"
FT                   /evidence="ECO:0000269|PubMed:20549317"
FT                   /id="VAR_065662"
FT   VARIANT         273
FT                   /note="G -> R (in LAD1; dbSNP:rs137852618)"
FT                   /evidence="ECO:0000269|PubMed:9884339"
FT                   /id="VAR_013403"
FT   VARIANT         284
FT                   /note="G -> S (in LAD1; dbSNP:rs137852616)"
FT                   /evidence="ECO:0000269|PubMed:7686755"
FT                   /id="VAR_003989"
FT   VARIANT         300
FT                   /note="D -> V (in LAD1; dbSNP:rs179363874)"
FT                   /evidence="ECO:0000269|PubMed:20529581"
FT                   /id="VAR_065663"
FT   VARIANT         351
FT                   /note="N -> S (in LAD1; dbSNP:rs137852613)"
FT                   /evidence="ECO:0000269|PubMed:1346613"
FT                   /id="VAR_003990"
FT   VARIANT         354
FT                   /note="Q -> H (in dbSNP:rs235330)"
FT                   /evidence="ECO:0000269|PubMed:1346613,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:1683838, ECO:0000269|PubMed:2954816,
FT                   ECO:0000269|PubMed:3028646, ECO:0000269|Ref.4,
FT                   ECO:0000269|Ref.6"
FT                   /id="VAR_030035"
FT   VARIANT         586
FT                   /note="R -> W (in LAD1; dbSNP:rs5030672)"
FT                   /evidence="ECO:0000269|PubMed:1346613"
FT                   /id="VAR_003991"
FT   VARIANT         593
FT                   /note="R -> C (in LAD1; dbSNP:rs137852609)"
FT                   /evidence="ECO:0000269|PubMed:1968911"
FT                   /id="VAR_003992"
FT   VARIANT         716
FT                   /note="G -> A (in LAD1; dbSNP:rs179363872)"
FT                   /evidence="ECO:0000269|PubMed:20549317"
FT                   /id="VAR_065664"
FT   MUTAGEN         758
FT                   /note="T->A: Abolishes phosphorylation. Reduces COS cell
FT                   adhesion to ICAM1."
FT                   /evidence="ECO:0000269|PubMed:16301335"
FT   CONFLICT        199
FT                   /note="Q -> P (in Ref. 8; CAA68266)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279
FT                   /note="L -> P (in Ref. 4; BAD96225)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        526
FT                   /note="G -> C (in Ref. 3; BAG53190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        630
FT                   /note="E -> K (in Ref. 3; BAG53190)"
FT                   /evidence="ECO:0000305"
FT   HELIX           33..37
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:2P28"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:5E6R"
FT   HELIX           58..61
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   HELIX           65..70
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          101..107
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          127..134
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           140..146
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           150..160
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          165..171
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   TURN            177..179
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           184..188
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   STRAND          203..212
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           214..222
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           236..245
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           247..250
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          254..265
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           272..276
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          289..292
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   HELIX           294..297
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           304..313
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          316..322
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           324..326
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           327..331
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           333..336
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          341..344
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   HELIX           352..364
FT                   /evidence="ECO:0007829|PDB:5E6S"
FT   STRAND          365..371
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          378..385
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          391..402
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          409..419
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          424..430
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          437..443
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          452..454
FT                   /evidence="ECO:0007829|PDB:3K6S"
FT   HELIX           458..461
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          462..466
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          469..472
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          476..478
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          483..487
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   HELIX           490..495
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          498..500
FT                   /evidence="ECO:0007829|PDB:2P28"
FT   HELIX           505..508
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          509..513
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          516..519
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          528..531
FT                   /evidence="ECO:0007829|PDB:2P26"
FT   STRAND          536..539
FT                   /evidence="ECO:0007829|PDB:2P28"
FT   STRAND          544..550
FT                   /evidence="ECO:0007829|PDB:1L3Y"
FT   TURN            552..554
FT                   /evidence="ECO:0007829|PDB:2P28"
FT   STRAND          555..558
FT                   /evidence="ECO:0007829|PDB:2P28"
FT   STRAND          561..564
FT                   /evidence="ECO:0007829|PDB:2P28"
FT   STRAND          568..570
FT                   /evidence="ECO:0007829|PDB:2P28"
FT   STRAND          575..577
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   TURN            580..582
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   TURN            590..592
FT                   /evidence="ECO:0007829|PDB:5ES4"
FT   STRAND          593..597
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   STRAND          600..603
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   TURN            609..611
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   STRAND          616..618
FT                   /evidence="ECO:0007829|PDB:4NEN"
FT   HELIX           622..624
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   HELIX           626..634
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   HELIX           637..639
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   TURN            640..642
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   HELIX           643..646
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   STRAND          650..655
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   STRAND          658..665
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   STRAND          667..669
FT                   /evidence="ECO:0007829|PDB:5ES4"
FT   STRAND          671..679
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   TURN            680..683
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   STRAND          684..689
FT                   /evidence="ECO:0007829|PDB:4NEH"
FT   HELIX           702..734
FT                   /evidence="ECO:0007829|PDB:5ZAZ"
FT   STRAND          754..762
FT                   /evidence="ECO:0007829|PDB:2JF1"
SQ   SEQUENCE   769 AA;  84782 MW;  EB9F3C3DF338B4E1 CRC64;
     MLGLRPPLLA LVGLLSLGCV LSQECTKFKV SSCRECIESG PGCTWCQKLN FTGPGDPDSI
     RCDTRPQLLM RGCAADDIMD PTSLAETQED HNGGQKQLSP QKVTLYLRPG QAAAFNVTFR
     RAKGYPIDLY YLMDLSYSML DDLRNVKKLG GDLLRALNEI TESGRIGFGS FVDKTVLPFV
     NTHPDKLRNP CPNKEKECQP PFAFRHVLKL TNNSNQFQTE VGKQLISGNL DAPEGGLDAM
     MQVAACPEEI GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKRSNEFD
     YPSVGQLAHK LAENNIQPIF AVTSRMVKTY EKLTEIIPKS AVGELSEDSS NVVQLIKNAY
     NKLSSRVFLD HNALPDTLKV TYDSFCSNGV THRNQPRGDC DGVQINVPIT FQVKVTATEC
     IQEQSFVIRA LGFTDIVTVQ VLPQCECRCR DQSRDRSLCH GKGFLECGIC RCDTGYIGKN
     CECQTQGRSS QELEGSCRKD NNSIICSGLG DCVCGQCLCH TSDVPGKLIY GQYCECDTIN
     CERYNGQVCG GPGRGLCFCG KCRCHPGFEG SACQCERTTE GCLNPRRVEC SGRGRCRCNV
     CECHSGYQLP LCQECPGCPS PCGKYISCAE CLKFEKGPFG KNCSAACPGL QLSNNPVKGR
     TCKERDSEGC WVAYTLEQQD GMDRYLIYVD ESRECVAGPN IAAIVGGTVA GIVLIGILLL
     VIWKALIHLS DLREYRRFEK EKLKSQWNND NPLFKSATTT VMNPKFAES
//
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