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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   10-APR-2019, entry version 239.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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:
RT   homology to an extracellular matrix receptor defines a novel supergene
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA   Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA   Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA   Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA   Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA   Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA   Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA   Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA   Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA   Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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;
RA   Law S.K.A., Gagnon J., Hildreth J.E., Wells C.E., Willis A.C.,
RA   Wong A.J.;
RT   "The primary structure of the beta-subunit of the cell surface
RT   adhesion glycoproteins LFA-1, CR3 and p150,95 and its relationship to
RT   the 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
RP   TRP-586, AND VARIANT HIS-354.
RX   PubMed=1346613;
RA   Nelson C., Rabb H., Arnaout M.A.;
RT   "Genetic cause of leukocyte adhesion molecule deficiency. Abnormal
RT   splicing and a missense mutation in a conserved region of CD18 impair
RT   cell surface 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.,
RA   Rogge L., Pardi R.;
RT   "Integrin LFA-1 interacts with the transcriptional co-activator JAB1
RT   to 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
RT   by 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
RT   and 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-
RT   1 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.,
RA   Moore R.J., 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
RT   transmigration in sepsis-induced lung inflammation by activating beta2
RT   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-
RT   binding repeats in filamin: implication on filamin-mediated receptor
RT   clustering and 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
RT   multiple 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-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [22]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGAM,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=21193407; DOI=10.1074/jbc.M110.171256;
RA   Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A.,
RA   Luft F., Kettritz R.;
RT   "Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-
RT   ANCA 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
RT   neutrophils by 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.,
RA   Ayoub D., 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,
RP   SUBCELLULAR 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.,
RA   Zeng L., Halyabar O., Godin M.D., Nguyen H.N., Levescot A., Cunin P.,
RA   Lefort C.T., Soberman R.J., Nigrovic P.A.;
RT   "CD177 modulates human neutrophil migration through activation-
RT   mediated integrin and chemoreceptor regulation.";
RL   Blood 130:2092-2100(2017).
RN   [27]
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
RT   type 4.";
RL   EMBO J. 29:666-679(2010).
RN   [28]
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   [29]
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
RT   and their functional correlates.";
RL   J. Exp. Med. 172:335-345(1990).
RN   [30]
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.,
RA   Kobayashi K., Kajii T.;
RT   "Leukocyte adhesion deficiency: identification of novel mutations in
RT   two Japanese patients with a severe form.";
RL   Biochem. Biophys. Res. Commun. 184:1460-1467(1992).
RN   [31]
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.,
RA   Sanchez-Madrid F.;
RT   "Molecular basis for a severe case of leukocyte adhesion deficiency.";
RL   Eur. J. Immunol. 22:1877-1881(1992).
RN   [32]
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   [33]
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.,
RA   Hickstein D.D.;
RT   "A point mutation associated with leukocyte adhesion deficiency type 1
RT   of moderate severity.";
RL   Biochem. Biophys. Res. Commun. 193:912-918(1993).
RN   [34]
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   [35]
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
RT   in a Chinese patient.";
RL   Chin. Med. J. 123:1278-1282(2010).
RN   [36]
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.,
RA   Parvaneh L., Sherkat R., Ghalehbaghi B., Kashef S., Chavoshzadeh Z.,
RA   Isaeian A., Ashrafi F., Aghamohammadi A.;
RT   "Characterization of 11 new cases of leukocyte adhesion deficiency
RT   type 1 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,
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 (PubMed:15356110). Involved in leukocyte adhesion and
CC       transmigration of leukocytes including T-cells and neutrophils
CC       (PubMed:11812992, PubMed:28807980). Triggers neutrophil
CC       transmigration during lung injury through PTK2B/PYK2-mediated
CC       activation (PubMed:18587400). Integrin ITGAL/ITGB2 in association
CC       with ICAM3, contributes to apoptotic neutrophil phagocytosis by
CC       macrophages (PubMed:23775590). In association with alpha subunit
CC       ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF
CC       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   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit
CC       (PubMed:20033057). ITGB2 associates with either ITGAL, ITGAM,
CC       ITGAX or ITGAD. Found in a complex with CD177 and ITGAM/CD11b
CC       (PubMed:21193407, PubMed:28807980). Interacts with FGR (By
CC       similarity). Interacts with COPS5 and RANBP9 (PubMed:10766246,
CC       PubMed:14722085). Interacts with FLNA (via filamin repeats 4, 9,
CC       12, 17, 19, 21, and 23) (PubMed:19828450). Interacts with THBD
CC       (PubMed:27055590). {ECO:0000250|UniProtKB:P11835,
CC       ECO:0000269|PubMed:10766246, ECO:0000269|PubMed:14722085,
CC       ECO:0000269|PubMed:19828450, ECO:0000269|PubMed:20033057,
CC       ECO:0000269|PubMed:21193407, ECO:0000269|PubMed:27055590,
CC       ECO:0000269|PubMed:28807980}.
CC   -!- INTERACTION:
CC       P00519:ABL1; NbExp=4; IntAct=EBI-300173, EBI-375543;
CC       P20702:ITGAX; NbExp=3; IntAct=EBI-300173, EBI-2568308;
CC       Q7Z3S9:NOTCH2NLA; NbExp=8; IntAct=EBI-300173, EBI-945833;
CC       P35241:RDX; NbExp=2; IntAct=EBI-300173, EBI-2514878;
CC       Q9Y4G6:TLN2; NbExp=5; IntAct=EBI-300173, EBI-1220811;
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};
CC       Single-pass 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
CC       are exposed to phorbol esters (PubMed:11700305). Phosphorylation
CC       on Thr-758 (but not on Ser-756) allows interaction with 14-3-3
CC       proteins (PubMed:11700305, PubMed:16301335).
CC       {ECO:0000269|PubMed:11700305, ECO:0000269|PubMed:16301335}.
CC   -!- DISEASE: Leukocyte adhesion deficiency 1 (LAD1) [MIM:116920]: LAD1
CC       patients have recurrent bacterial infections and their leukocytes
CC       are 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
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {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/";
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   UniGene; Hs.375957; -.
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   ProteinModelPortal; P05107; -.
DR   SMR; P05107; -.
DR   BioGrid; 109895; 36.
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; 27.
DR   MINT; P05107; -.
DR   STRING; 9606.ENSP00000380948; -.
DR   BindingDB; P05107; -.
DR   ChEMBL; CHEMBL3631; -.
DR   DrugBank; DB00641; Simvastatin.
DR   GuidetoPHARMACOLOGY; 2456; -.
DR   GlyConnect; 1415; -.
DR   iPTMnet; P05107; -.
DR   PhosphoSitePlus; P05107; -.
DR   BioMuta; ITGB2; -.
DR   DMDM; 124056465; -.
DR   EPD; P05107; -.
DR   jPOST; P05107; -.
DR   MaxQB; P05107; -.
DR   PaxDb; P05107; -.
DR   PeptideAtlas; P05107; -.
DR   PRIDE; P05107; -.
DR   ProteomicsDB; 51793; -.
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   EuPathDB; HostDB:ENSG00000160255.16; -.
DR   GeneCards; ITGB2; -.
DR   HGNC; HGNC:6155; ITGB2.
DR   HPA; HPA008877; -.
DR   HPA; HPA016894; -.
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   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P05107; -.
DR   KO; K06464; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P05107; -.
DR   TreeFam; TF105392; -.
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   ChiTaRS; ITGB2; human.
DR   EvolutionaryTrace; P05107; -.
DR   GeneWiki; CD18; -.
DR   GenomeRNAi; 3689; -.
DR   PMAP-CutDB; P05107; -.
DR   PRO; PR:P05107; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   Bgee; ENSG00000160255; Expressed in 187 organ(s), highest expression level in blood.
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; NAS:ARUK-UCL.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0046982; F:protein heterodimerization activity; NAS:ARUK-UCL.
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; TAS:ProtInc.
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:1903980; P:positive regulation of microglial cell activation; NAS:ARUK-UCL.
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   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; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   Glycoprotein; Integrin; Membrane; Metal-binding; Phagocytosis;
KW   Phosphoprotein; Pyrrolidone carboxylic acid; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22
FT   CHAIN        23    769       Integrin beta-2.
FT                                /FTId=PRO_0000016341.
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   METAL       141    141       Calcium.
FT   METAL       142    142       Calcium.
FT   METAL       347    347       Calcium.
FT   MOD_RES      23     23       Pyrrolidone carboxylic acid.
FT                                {ECO:0000305|PubMed:2954816}.
FT   MOD_RES     745    745       Phosphoserine; by PKC.
FT                                {ECO:0000269|PubMed:11700305}.
FT   MOD_RES     756    756       Phosphoserine.
FT                                {ECO:0000269|PubMed:11700305}.
FT   MOD_RES     758    758       Phosphothreonine; by PKC; in vitro.
FT                                {ECO:0000269|PubMed:11700305,
FT                                ECO:0000269|PubMed:16301335}.
FT   MOD_RES     759    759       Phosphothreonine. {ECO:0000255}.
FT   MOD_RES     760    760       Phosphothreonine; by PKC/PRKCA; in vitro.
FT                                {ECO:0000269|PubMed:11700305}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:19349973}.
FT   CARBOHYD    116    116       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:20033057}.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:19349973}.
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:0000269|PubMed:20033057}.
FT   DISULFID     33    447       {ECO:0000269|PubMed:20033057}.
FT   DISULFID     36     62       {ECO:0000269|PubMed:20033057}.
FT   DISULFID     46     73       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    191    198       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    246    286       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    386    400       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    420    445       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    449    467       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    459    470       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    472    481       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    483    514       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    497    512       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    506    517       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    519    534       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    536    559       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    541    557       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    549    562       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    564    573       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    575    598       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    582    596       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    590    601       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    603    612       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    615    618       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    622    662       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    628    647       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    631    643       {ECO:0000269|PubMed:20033057}.
FT   DISULFID    670    695       {ECO:0000269|PubMed:20033057}.
FT   VARIANT     128    128       D -> N (in LAD1; dbSNP:rs137852615).
FT                                {ECO:0000269|PubMed:1590804}.
FT                                /FTId=VAR_003984.
FT   VARIANT     128    128       D -> Y (in LAD1; dbSNP:rs137852615).
FT                                {ECO:0000269|PubMed:20549317}.
FT                                /FTId=VAR_065661.
FT   VARIANT     138    138       S -> P (in LAD1; dbSNP:rs137852617).
FT                                {ECO:0000269|PubMed:9884339}.
FT                                /FTId=VAR_013402.
FT   VARIANT     149    149       L -> P (in LAD1; dbSNP:rs137852611).
FT                                {ECO:0000269|PubMed:1694220}.
FT                                /FTId=VAR_003985.
FT   VARIANT     169    169       G -> R (in LAD1; dbSNP:rs137852612).
FT                                {ECO:0000269|PubMed:1352501,
FT                                ECO:0000269|PubMed:1694220}.
FT                                /FTId=VAR_003986.
FT   VARIANT     178    178       P -> L (in LAD1; dbSNP:rs137852614).
FT                                {ECO:0000269|PubMed:1347532,
FT                                ECO:0000269|PubMed:7509236}.
FT                                /FTId=VAR_003987.
FT   VARIANT     196    196       K -> T (in LAD1; dbSNP:rs137852610).
FT                                {ECO:0000269|PubMed:1968911}.
FT                                /FTId=VAR_003988.
FT   VARIANT     239    239       A -> T (in LAD1; dbSNP:rs179363873).
FT                                {ECO:0000269|PubMed:20549317}.
FT                                /FTId=VAR_065662.
FT   VARIANT     273    273       G -> R (in LAD1; dbSNP:rs137852618).
FT                                {ECO:0000269|PubMed:9884339}.
FT                                /FTId=VAR_013403.
FT   VARIANT     284    284       G -> S (in LAD1; dbSNP:rs137852616).
FT                                {ECO:0000269|PubMed:7686755}.
FT                                /FTId=VAR_003989.
FT   VARIANT     300    300       D -> V (in LAD1; dbSNP:rs179363874).
FT                                {ECO:0000269|PubMed:20529581}.
FT                                /FTId=VAR_065663.
FT   VARIANT     351    351       N -> S (in LAD1; dbSNP:rs137852613).
FT                                {ECO:0000269|PubMed:1346613}.
FT                                /FTId=VAR_003990.
FT   VARIANT     354    354       Q -> H (in dbSNP:rs235330).
FT                                {ECO:0000269|PubMed:1346613,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:1683838,
FT                                ECO:0000269|PubMed:2954816,
FT                                ECO:0000269|PubMed:3028646,
FT                                ECO:0000269|Ref.4, ECO:0000269|Ref.6}.
FT                                /FTId=VAR_030035.
FT   VARIANT     586    586       R -> W (in LAD1; dbSNP:rs5030672).
FT                                {ECO:0000269|PubMed:1346613}.
FT                                /FTId=VAR_003991.
FT   VARIANT     593    593       R -> C (in LAD1; dbSNP:rs137852609).
FT                                {ECO:0000269|PubMed:1968911}.
FT                                /FTId=VAR_003992.
FT   VARIANT     716    716       G -> A (in LAD1; dbSNP:rs179363872).
FT                                {ECO:0000269|PubMed:20549317}.
FT                                /FTId=VAR_065664.
FT   MUTAGEN     758    758       T->A: Abolishes phosphorylation. Reduces
FT                                COS cell adhesion to ICAM1.
FT                                {ECO:0000269|PubMed:16301335}.
FT   CONFLICT    199    199       Q -> P (in Ref. 8; CAA68266).
FT                                {ECO:0000305}.
FT   CONFLICT    279    279       L -> P (in Ref. 4; BAD96225).
FT                                {ECO:0000305}.
FT   CONFLICT    526    526       G -> C (in Ref. 3; BAG53190).
FT                                {ECO:0000305}.
FT   CONFLICT    630    630       E -> K (in Ref. 3; BAG53190).
FT                                {ECO:0000305}.
FT   HELIX        33     37       {ECO:0000244|PDB:2P26}.
FT   STRAND       44     46       {ECO:0000244|PDB:2P26}.
FT   HELIX        49     51       {ECO:0000244|PDB:2P28}.
FT   STRAND       54     56       {ECO:0000244|PDB:5E6R}.
FT   HELIX        58     61       {ECO:0000244|PDB:2P26}.
FT   HELIX        65     70       {ECO:0000244|PDB:2P26}.
FT   HELIX        75     77       {ECO:0000244|PDB:2P26}.
FT   STRAND       84     88       {ECO:0000244|PDB:2P26}.
FT   STRAND       91     94       {ECO:0000244|PDB:2P26}.
FT   STRAND       96     99       {ECO:0000244|PDB:2P26}.
FT   STRAND      101    107       {ECO:0000244|PDB:2P26}.
FT   STRAND      113    119       {ECO:0000244|PDB:2P26}.
FT   STRAND      121    123       {ECO:0000244|PDB:2P26}.
FT   STRAND      127    134       {ECO:0000244|PDB:5E6S}.
FT   HELIX       137    139       {ECO:0000244|PDB:5E6S}.
FT   HELIX       140    146       {ECO:0000244|PDB:5E6S}.
FT   HELIX       150    160       {ECO:0000244|PDB:5E6S}.
FT   STRAND      161    163       {ECO:0000244|PDB:5E6S}.
FT   STRAND      165    171       {ECO:0000244|PDB:5E6S}.
FT   TURN        177    179       {ECO:0000244|PDB:5E6S}.
FT   HELIX       184    188       {ECO:0000244|PDB:5E6S}.
FT   STRAND      196    198       {ECO:0000244|PDB:4NEH}.
FT   STRAND      203    212       {ECO:0000244|PDB:5E6S}.
FT   HELIX       214    222       {ECO:0000244|PDB:5E6S}.
FT   STRAND      230    234       {ECO:0000244|PDB:5E6S}.
FT   HELIX       236    245       {ECO:0000244|PDB:5E6S}.
FT   HELIX       247    250       {ECO:0000244|PDB:5E6S}.
FT   STRAND      254    265       {ECO:0000244|PDB:5E6S}.
FT   HELIX       272    276       {ECO:0000244|PDB:5E6S}.
FT   STRAND      289    292       {ECO:0000244|PDB:4NEH}.
FT   HELIX       294    297       {ECO:0000244|PDB:5E6S}.
FT   HELIX       304    313       {ECO:0000244|PDB:5E6S}.
FT   STRAND      316    322       {ECO:0000244|PDB:5E6S}.
FT   HELIX       324    326       {ECO:0000244|PDB:5E6S}.
FT   HELIX       327    331       {ECO:0000244|PDB:5E6S}.
FT   HELIX       333    336       {ECO:0000244|PDB:5E6S}.
FT   STRAND      337    339       {ECO:0000244|PDB:5E6S}.
FT   STRAND      341    344       {ECO:0000244|PDB:5E6S}.
FT   HELIX       352    364       {ECO:0000244|PDB:5E6S}.
FT   STRAND      365    371       {ECO:0000244|PDB:2P26}.
FT   STRAND      378    385       {ECO:0000244|PDB:2P26}.
FT   STRAND      387    389       {ECO:0000244|PDB:2P26}.
FT   STRAND      391    402       {ECO:0000244|PDB:2P26}.
FT   STRAND      409    419       {ECO:0000244|PDB:2P26}.
FT   STRAND      424    430       {ECO:0000244|PDB:2P26}.
FT   STRAND      437    443       {ECO:0000244|PDB:2P26}.
FT   STRAND      452    454       {ECO:0000244|PDB:3K6S}.
FT   HELIX       458    461       {ECO:0000244|PDB:2P26}.
FT   STRAND      462    466       {ECO:0000244|PDB:2P26}.
FT   STRAND      469    472       {ECO:0000244|PDB:2P26}.
FT   STRAND      476    478       {ECO:0000244|PDB:2P26}.
FT   STRAND      483    487       {ECO:0000244|PDB:4NEH}.
FT   HELIX       490    495       {ECO:0000244|PDB:2P26}.
FT   STRAND      498    500       {ECO:0000244|PDB:2P28}.
FT   HELIX       505    508       {ECO:0000244|PDB:2P26}.
FT   STRAND      509    513       {ECO:0000244|PDB:2P26}.
FT   STRAND      516    519       {ECO:0000244|PDB:2P26}.
FT   STRAND      528    531       {ECO:0000244|PDB:2P26}.
FT   STRAND      536    539       {ECO:0000244|PDB:2P28}.
FT   STRAND      544    550       {ECO:0000244|PDB:1L3Y}.
FT   TURN        552    554       {ECO:0000244|PDB:2P28}.
FT   STRAND      555    558       {ECO:0000244|PDB:2P28}.
FT   STRAND      561    564       {ECO:0000244|PDB:2P28}.
FT   STRAND      568    570       {ECO:0000244|PDB:2P28}.
FT   STRAND      575    577       {ECO:0000244|PDB:4NEH}.
FT   TURN        580    582       {ECO:0000244|PDB:4NEH}.
FT   TURN        590    592       {ECO:0000244|PDB:5ES4}.
FT   STRAND      593    597       {ECO:0000244|PDB:4NEH}.
FT   STRAND      600    603       {ECO:0000244|PDB:4NEH}.
FT   TURN        609    611       {ECO:0000244|PDB:4NEH}.
FT   STRAND      616    618       {ECO:0000244|PDB:4NEN}.
FT   HELIX       622    624       {ECO:0000244|PDB:4NEH}.
FT   HELIX       626    634       {ECO:0000244|PDB:4NEH}.
FT   HELIX       637    639       {ECO:0000244|PDB:4NEH}.
FT   TURN        640    642       {ECO:0000244|PDB:4NEH}.
FT   HELIX       643    646       {ECO:0000244|PDB:4NEH}.
FT   STRAND      650    655       {ECO:0000244|PDB:4NEH}.
FT   STRAND      658    665       {ECO:0000244|PDB:4NEH}.
FT   STRAND      667    669       {ECO:0000244|PDB:5ES4}.
FT   STRAND      671    679       {ECO:0000244|PDB:4NEH}.
FT   TURN        680    683       {ECO:0000244|PDB:4NEH}.
FT   STRAND      684    689       {ECO:0000244|PDB:4NEH}.
FT   HELIX       702    734       {ECO:0000244|PDB:5ZAZ}.
FT   STRAND      754    762       {ECO:0000244|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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