ITB2_HUMAN
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 03-AUG-2022, entry version 259.
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; DOI=10.1016/s0021-9258(19)50738-4;
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; DOI=10.1016/s0021-9258(18)42791-3;
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; 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; 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 AlphaFoldDB; P05107; -.
DR BMRB; P05107; -.
DR SMR; P05107; -.
DR BioGRID; 109895; 61.
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; 12 sites, 7 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
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; 2057 antibodies from 50 providers.
DR DNASU; 3689; -.
DR Ensembl; ENST00000302347.10; ENSP00000303242.6; ENSG00000160255.18.
DR Ensembl; ENST00000355153.8; ENSP00000347279.4; ENSG00000160255.18.
DR Ensembl; ENST00000397850.6; ENSP00000380948.2; ENSG00000160255.18.
DR Ensembl; ENST00000397852.5; ENSP00000380950.1; ENSG00000160255.18.
DR Ensembl; ENST00000397857.5; ENSP00000380955.1; ENSG00000160255.18.
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 (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; -.
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; 15 hits in 1068 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 163 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: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:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
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:0001774; P:microglial cell activation; NAS:ARUK-UCL.
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:1990266; P:neutrophil migration; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
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: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:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR DisProt; DP01848; -.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015439; Integrin_bsu-2.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF15; PTHR10082:SF15; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 1: Evidence at protein level;
KW 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 BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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
