ICAM1_HUMAN
ID ICAM1_HUMAN Reviewed; 532 AA.
AC P05362; B2R6M3; Q5NKV7; Q96B50;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 250.
DE RecName: Full=Intercellular adhesion molecule 1;
DE Short=ICAM-1;
DE AltName: Full=Major group rhinovirus receptor;
DE AltName: CD_antigen=CD54;
DE Flags: Precursor;
GN Name=ICAM1;
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 GLU-469.
RX PubMed=3340213; DOI=10.1038/331624a0;
RA Simmons D., Makgoba M.W., Seed B.;
RT "ICAM, an adhesion ligand of LFA-1, is homologous to the neural cell
RT adhesion molecule NCAM.";
RL Nature 331:624-627(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-469.
RX PubMed=3349522; DOI=10.1016/0092-8674(88)90434-5;
RA Staunton D.E., Marlin S.D., Stratowa C., Dustin M.L., Springer T.A.;
RT "Primary structure of ICAM-1 demonstrates interaction between members of
RT the immunoglobulin and integrin supergene families.";
RL Cell 52:925-933(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2544880; DOI=10.1073/pnas.86.13.4907;
RA Tomassini J.E., Graham D., Dewitt C.M., Lineberger D.W., Rodkey J.A.,
RA Colonno R.J.;
RT "cDNA cloning reveals that the major group rhinovirus receptor on HeLa
RT cells is intercellular adhesion molecule 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4907-4911(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-469.
RX PubMed=1680919;
RA Voraberger G.F., Schaefer R., Stratowa C.;
RT "Cloning of the human gene for intercellular adhesion molecule 1 and
RT analysis of its 5'-regulatory region. Induction by cytokines and phorbol
RT ester.";
RL J. Immunol. 147:2777-2786(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT KILIFI MET-56, AND VARIANTS
RP ARG-241; LEU-352; GLN-397 AND TRP-478.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=1983003; DOI=10.1016/s0171-2985(11)80585-1;
RA Stade B.G., Messer G., Riethmueller G., Johnson J.P.;
RT "Structural characteristics of the 5' region of the human ICAM-1 gene.";
RL Immunobiology 182:79-87(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-532, AND VARIANT GLU-469.
RC TISSUE=Blood;
RX PubMed=15572059; DOI=10.1016/j.jtbi.2004.08.024;
RA Walter N.A.R., Stebbing J., Messier W.;
RT "The potential significance of adaptive evolution and dimerization in
RT chimpanzee intercellular cell adhesion molecules (ICAMs).";
RL J. Theor. Biol. 232:339-346(2005).
RN [12]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION (MICROBIAL INFECTION), AND INTERACTION
RP WITH RHINOVIRUS CAPSID PROTEINS.
RX PubMed=2538243; DOI=10.1016/0092-8674(89)90688-0;
RA Greve J.M., Davis G., Meyer A.M., Forte C.P., Yost S.C., Marlor C.W.,
RA Kamarck M.E., McClelland A.;
RT "The major human rhinovirus receptor is ICAM-1.";
RL Cell 56:839-847(1989).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RHINOVIRUS CAPSID
RP PROTEINS.
RX PubMed=1968231; DOI=10.1038/344070a0;
RA Marlin S.D., Staunton D.E., Springer T.A., Stratowa C., Sommergruber W.,
RA Merluzzi V.J.;
RT "A soluble form of intercellular adhesion molecule-1 inhibits rhinovirus
RT infection.";
RL Nature 344:70-72(1990).
RN [14]
RP INTERACTION WITH MUC1, AND FUNCTION.
RX PubMed=11173916; DOI=10.1159/000051917;
RA Hayashi T., Takahashi T., Motoya S., Ishida T., Itoh F., Adachi M.,
RA Hinoda Y., Imai K.;
RT "MUC1 mucin core protein binds to the domain 1 of ICAM-1.";
RL Digestion 63 Suppl. 1:87-92(2001).
RN [15]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS A21
RP CAPSID PROTEINS.
RX PubMed=11160747; DOI=10.1128/jvi.75.5.2444-2451.2001;
RA Xiao C., Bator C.M., Bowman V.D., Rieder E., He Y., Hebert B., Bella J.,
RA Baker T.S., Wimmer E., Kuhn R.J., Rossmann M.G.;
RT "Interaction of coxsackievirus A21 with its cellular receptor, ICAM-1.";
RL J. Virol. 75:2444-2451(2001).
RN [16]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=11413168; DOI=10.1172/jci12432;
RA Coscoy L., Ganem D.;
RT "A viral protein that selectively downregulates ICAM-1 and B7-2 and
RT modulates T cell costimulation.";
RL J. Clin. Invest. 107:1599-1606(2001).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267.
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 UBIQUITINATION.
RX PubMed=17174307; DOI=10.1016/j.febslet.2006.11.075;
RA Hoer S., Smith L., Lehner P.J.;
RT "MARCH-IX mediates ubiquitination and downregulation of ICAM-1.";
RL FEBS Lett. 581:45-51(2007).
RN [19]
RP INTERACTION WITH ARHGEF26, AND FUNCTION.
RX PubMed=17875742; DOI=10.1083/jcb.200612053;
RA van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E.,
RA Garcia-Mata R., Burridge K.;
RT "RhoG regulates endothelial apical cup assembly downstream from ICAM1
RT engagement and is involved in leukocyte trans-endothelial migration.";
RL J. Cell Biol. 178:1279-1293(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202 AND ASN-267.
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 [22]
RP GLYCOSYLATION AT ASN-145.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [23]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-267.
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP INTERACTION WITH CD81, INTERACTION WITH CD9, AND INTERACTION WITH CD247.
RX PubMed=23858057; DOI=10.1128/mcb.00302-13;
RA Rocha-Perugini V., Zamai M., Gonzalez-Granado J.M., Barreiro O., Tejera E.,
RA Yanez-Mo M., Caiolfa V.R., Sanchez-Madrid F.;
RT "CD81 controls sustained T cell activation signaling and defines the
RT maturation stages of cognate immunological synapses.";
RL Mol. Cell. Biol. 33:3644-3658(2013).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-530, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
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 [30]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 28-217, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-130; ASN-145; ASN-183 AND ASN-202.
RX PubMed=9539702; DOI=10.1073/pnas.95.8.4134;
RA Casasnovas J.M., Stehle T., Liu J.H., Wang J.H., Springer T.A.;
RT "A dimeric crystal structure for the N-terminal two domains of
RT intercellular adhesion molecule-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4134-4139(1998).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212 IN COMPLEX WITH HUMAN
RP RHINOVIRUS 14, DISULFIDE BONDS, GLYCOSYLATION AT ASN-202, AND SUBUNIT.
RX PubMed=9539703; DOI=10.1073/pnas.95.8.4140;
RA Bella J., Kolatkar P.R., Marlor C.W., Greve J.M., Rossmann M.G.;
RT "The structure of the two amino-terminal domains of human ICAM-1 suggests
RT how it functions as a rhinovirus receptor and as an LFA-1 integrin
RT ligand.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4140-4145(1998).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212.
RX PubMed=10562537; DOI=10.1093/emboj/18.22.6249;
RA Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G.;
RT "Structural studies of two rhinovirus serotypes complexed with fragments of
RT their cellular receptor.";
RL EMBO J. 18:6249-6259(1999).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 28-318 IN COMPLEX WITH ITGAL VWFA
RP DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-130; ASN-145; ASN-183 AND
RP ASN-202, AND SUBUNIT.
RX PubMed=12526797; DOI=10.1016/s0092-8674(02)01257-6;
RA Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A.,
RA Zhang R., Joachimiak A., Takagi J., Wang J.H., Springer T.A.;
RT "Structures of the alpha L I domain and its complex with ICAM-1 reveal a
RT shape-shifting pathway for integrin regulation.";
RL Cell 112:99-111(2003).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 212-477, SUBUNIT, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-267; ASN-296 AND ASN-385.
RX PubMed=15099525; DOI=10.1016/s1097-2765(04)00204-7;
RA Yang Y., Jun C.D., Liu J.H., Zhang R., Joachimiak A., Springer T.A.,
RA Wang J.H.;
RT "Structural basis for dimerization of ICAM-1 on the cell surface.";
RL Mol. Cell 14:269-276(2004).
RN [35]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.0 ANGSTROMS) OF 24-473 IN COMPLEX WITH
RP COXSACKIEVIRUS A21, AND SUBUNIT.
RX PubMed=16004874; DOI=10.1016/j.str.2005.04.011;
RA Xiao C., Bator-Kelly C.M., Rieder E., Chipman P.R., Craig A., Kuhn R.J.,
RA Wimmer E., Rossmann M.G.;
RT "The crystal structure of coxsackievirus A21 and its interaction with ICAM-
RT 1.";
RL Structure 13:1019-1033(2005).
RN [36]
RP VARIANTS ARG-241 AND GLU-469.
RX PubMed=7525451; DOI=10.1006/geno.1994.1303;
RA Vora D.K., Rosenbloom C.L., Beaudet A.L., Cottingham R.W.;
RT "Polymorphisms and linkage analysis for ICAM-1 and the selectin gene
RT cluster.";
RL Genomics 21:473-477(1994).
RN [37]
RP VARIANT ARG-241.
RX PubMed=8557254; DOI=10.1007/bf00218826;
RA Wenzel K., Ernst M., Rohde K., Baumann G., Speer A.;
RT "DNA polymorphisms in adhesion molecule genes -- a new risk factor for
RT early atherosclerosis.";
RL Hum. Genet. 97:15-20(1996).
RN [38]
RP VARIANT KILIFI MET-56, AND ASSOCIATION WITH SUSCEPTIBILITY TO MALARIA.
RX PubMed=9259284; DOI=10.1093/hmg/6.8.1357;
RA Fernandez-Reyes D., Craig A.G., Kyes S.A., Peshu N., Snow R.W.,
RA Berendt A.R., Marsh K., Newbold C.I.;
RT "A high frequency African coding polymorphism in the N-terminal domain of
RT ICAM-1 predisposing to cerebral malaria in Kenya.";
RL Hum. Mol. Genet. 6:1357-1360(1997).
RN [39]
RP VARIANT KILIFI MET-56, AND VARIANT GLU-469.
RX PubMed=10391210; DOI=10.1038/10297;
RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
RA Cooper R., Lipshutz R., Chakravarti A.;
RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood-
RT pressure homeostasis.";
RL Nat. Genet. 22:239-247(1999).
CC -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein
CC LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial
CC migration, ICAM1 engagement promotes the assembly of endothelial apical
CC cups through ARHGEF26/SGEF and RHOG activation.
CC {ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:17875742}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for major receptor
CC group rhinovirus A-B capsid proteins. {ECO:0000269|PubMed:1968231,
CC ECO:0000269|PubMed:2538243}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus
CC A21 capsid proteins. {ECO:0000269|PubMed:11160747,
CC ECO:0000269|PubMed:16004874, ECO:0000269|PubMed:9539703}.
CC -!- FUNCTION: (Microbial infection) Upon Kaposi's sarcoma-associated
CC herpesvirus/HHV-8 infection, is degraded by viral E3 ubiquitin ligase
CC MIR2, presumably to prevent lysis of infected cells by cytotoxic T-
CC lymphocytes and NK cell. {ECO:0000269|PubMed:11413168}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with MUC1 and promotes cell
CC aggregation in epithelial cells. Interacts with ARHGEF26/SGEF.
CC Interacts (on T cell side) with CD81, CD247 and CD9 at immunological
CC synapses between antigen-presenting cells and T cells.
CC {ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:12526797,
CC ECO:0000269|PubMed:15099525, ECO:0000269|PubMed:17875742,
CC ECO:0000269|PubMed:23858057, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Interacts with major receptor group
CC rhinovirus A-B capsid proteins (PubMed:1968231, PubMed:2538243).
CC {ECO:0000269|PubMed:1968231, ECO:0000269|PubMed:2538243}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Coxsackievirus A21 capsid
CC proteins (PubMed:11160747, PubMed:16004874, PubMed:9539703).
CC {ECO:0000269|PubMed:11160747, ECO:0000269|PubMed:16004874,
CC ECO:0000269|PubMed:9539703}.
CC -!- INTERACTION:
CC P05362; Q99828: CIB1; NbExp=3; IntAct=EBI-1035358, EBI-372594;
CC P05362; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1035358, EBI-3867333;
CC P05362; P20701: ITGAL; NbExp=3; IntAct=EBI-1035358, EBI-961214;
CC P05362; Q14145: KEAP1; NbExp=3; IntAct=EBI-1035358, EBI-751001;
CC P05362; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1035358, EBI-10171774;
CC P05362; Q9BRX2: PELO; NbExp=3; IntAct=EBI-1035358, EBI-1043580;
CC P05362; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-1035358, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to
CC endocytosis.
CC -!- POLYMORPHISM: Homozygotes with ICAM1-Kalifi Met-56 seem to have an
CC increased risk for cerebral malaria [MIM:611162].
CC {ECO:0000269|PubMed:9259284}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ICAM1ID40909ch19p13.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Intercellular adhesion molecule
CC entry;
CC URL="https://en.wikipedia.org/wiki/Intercellular_adhesion_molecule";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/icam1/";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1z7z";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=ICAM-1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_261";
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DR EMBL; X06990; CAA30051.1; -; mRNA.
DR EMBL; J03132; AAA52709.1; -; mRNA.
DR EMBL; M24283; AAA52708.1; -; mRNA.
DR EMBL; X59286; CAA41977.1; -; Genomic_DNA.
DR EMBL; X59287; CAA41977.1; JOINED; Genomic_DNA.
DR EMBL; X59288; CAA41977.1; JOINED; Genomic_DNA.
DR EMBL; BT006854; AAP35500.1; -; mRNA.
DR EMBL; AY225514; AAO30128.1; -; Genomic_DNA.
DR EMBL; AK312636; BAG35520.1; -; mRNA.
DR EMBL; CH471106; EAW84086.1; -; Genomic_DNA.
DR EMBL; BC015969; AAH15969.1; -; mRNA.
DR EMBL; X57151; CAA40441.1; -; Genomic_DNA.
DR EMBL; AF340039; AAQ14902.1; -; mRNA.
DR CCDS; CCDS12231.1; -.
DR PIR; A29849; A29849.
DR RefSeq; NP_000192.2; NM_000201.2.
DR PDB; 1D3E; EM; 28.00 A; I=28-212.
DR PDB; 1D3I; EM; 26.00 A; I=28-212.
DR PDB; 1D3L; X-ray; 3.25 A; A=28-212.
DR PDB; 1IAM; X-ray; 2.10 A; A=28-212.
DR PDB; 1IC1; X-ray; 3.00 A; A/B=28-217.
DR PDB; 1MQ8; X-ray; 3.30 A; A/C=28-318.
DR PDB; 1P53; X-ray; 3.06 A; A/B=212-477.
DR PDB; 1Z7Z; EM; 8.00 A; I=28-477.
DR PDB; 2OZ4; X-ray; 2.70 A; A=213-477.
DR PDB; 3TCX; X-ray; 3.60 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=29-112.
DR PDB; 5MZA; X-ray; 2.78 A; B=28-212.
DR PDB; 6EIT; EM; 3.90 A; 4=28-112.
DR PDB; 6S8U; X-ray; 3.67 A; B=28-212.
DR PDB; 7BG7; EM; 2.40 A; B=28-480.
DR PDBsum; 1D3E; -.
DR PDBsum; 1D3I; -.
DR PDBsum; 1D3L; -.
DR PDBsum; 1IAM; -.
DR PDBsum; 1IC1; -.
DR PDBsum; 1MQ8; -.
DR PDBsum; 1P53; -.
DR PDBsum; 1Z7Z; -.
DR PDBsum; 2OZ4; -.
DR PDBsum; 3TCX; -.
DR PDBsum; 5MZA; -.
DR PDBsum; 6EIT; -.
DR PDBsum; 6S8U; -.
DR PDBsum; 7BG7; -.
DR AlphaFoldDB; P05362; -.
DR SMR; P05362; -.
DR BioGRID; 109610; 387.
DR DIP; DIP-36658N; -.
DR IntAct; P05362; 47.
DR MINT; P05362; -.
DR STRING; 9606.ENSP00000264832; -.
DR BindingDB; P05362; -.
DR ChEMBL; CHEMBL3070; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR DrugBank; DB12598; Nafamostat.
DR DrugBank; DB00108; Natalizumab.
DR DrugCentral; P05362; -.
DR TCDB; 8.A.23.4.1; the basigin (basigin) family.
DR GlyConnect; 1423; 1 N-Linked glycan (1 site).
DR GlyGen; P05362; 10 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P05362; -.
DR PhosphoSitePlus; P05362; -.
DR BioMuta; ICAM1; -.
DR DMDM; 68067956; -.
DR CPTAC; CPTAC-219; -.
DR CPTAC; CPTAC-220; -.
DR CPTAC; non-CPTAC-2679; -.
DR EPD; P05362; -.
DR jPOST; P05362; -.
DR MassIVE; P05362; -.
DR MaxQB; P05362; -.
DR PaxDb; P05362; -.
DR PeptideAtlas; P05362; -.
DR PRIDE; P05362; -.
DR ProteomicsDB; 51830; -.
DR ABCD; P05362; 8 sequenced antibodies.
DR Antibodypedia; 795; 3102 antibodies from 53 providers.
DR CPTC; P05362; 1 antibody.
DR DNASU; 3383; -.
DR Ensembl; ENST00000264832.8; ENSP00000264832.2; ENSG00000090339.9.
DR GeneID; 3383; -.
DR KEGG; hsa:3383; -.
DR MANE-Select; ENST00000264832.8; ENSP00000264832.2; NM_000201.3; NP_000192.2.
DR UCSC; uc002mnq.3; human.
DR CTD; 3383; -.
DR DisGeNET; 3383; -.
DR GeneCards; ICAM1; -.
DR HGNC; HGNC:5344; ICAM1.
DR HPA; ENSG00000090339; Tissue enhanced (lung, urinary bladder).
DR MalaCards; ICAM1; -.
DR MIM; 147840; gene.
DR MIM; 611162; phenotype.
DR neXtProt; NX_P05362; -.
DR OpenTargets; ENSG00000090339; -.
DR PharmGKB; PA29592; -.
DR VEuPathDB; HostDB:ENSG00000090339; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR GeneTree; ENSGT00940000162311; -.
DR HOGENOM; CLU_036160_1_1_1; -.
DR InParanoid; P05362; -.
DR OMA; NLTVYWF; -.
DR OrthoDB; 731140at2759; -.
DR PhylomeDB; P05362; -.
DR TreeFam; TF333745; -.
DR PathwayCommons; P05362; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SABIO-RK; P05362; -.
DR SignaLink; P05362; -.
DR SIGNOR; P05362; -.
DR BioGRID-ORCS; 3383; 26 hits in 1076 CRISPR screens.
DR ChiTaRS; ICAM1; human.
DR EvolutionaryTrace; P05362; -.
DR GeneWiki; ICAM-1; -.
DR GenomeRNAi; 3383; -.
DR Pharos; P05362; Tchem.
DR PRO; PR:P05362; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P05362; protein.
DR Bgee; ENSG00000090339; Expressed in vena cava and 179 other tissues.
DR ExpressionAtlas; P05362; baseline and differential.
DR Genevisible; P05362; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005178; F:integrin binding; IDA:MGI.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0044406; P:adhesion of symbiont to host; IDA:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IDA:BHF-UCL.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0061028; P:establishment of endothelial barrier; IGI:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:BHF-UCL.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:BHF-UCL.
DR GO; GO:0050900; P:leukocyte migration; IEP:BHF-UCL.
DR GO; GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IMP:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:BHF-UCL.
DR GO; GO:0001910; P:regulation of leukocyte mediated cytotoxicity; TAS:BHF-UCL.
DR GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:BHF-UCL.
DR GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Ensembl.
DR GO; GO:0072683; P:T cell extravasation; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR003987; ICAM_VCAM_N.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..27
FT CHAIN 28..532
FT /note="Intercellular adhesion molecule 1"
FT /id="PRO_0000014783"
FT TOPO_DOM 28..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..103
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..193
FT /note="Ig-like C2-type 2"
FT DOMAIN 230..297
FT /note="Ig-like C2-type 3"
FT DOMAIN 325..378
FT /note="Ig-like C2-type 4"
FT DOMAIN 412..464
FT /note="Ig-like C2-type 5"
FT MOTIF 152..154
FT /note="Cell attachment site; atypical"
FT /evidence="ECO:0000255"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 530
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12526797,
FT ECO:0000269|PubMed:9539702"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:12526797,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:9539702"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12526797,
FT ECO:0000269|PubMed:9539702"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12526797,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9539702,
FT ECO:0000269|PubMed:9539703"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15099525,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15099525"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15099525"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..92
FT /evidence="ECO:0000269|PubMed:12526797,
FT ECO:0000269|PubMed:9539702, ECO:0000269|PubMed:9539703,
FT ECO:0007744|PDB:1IAM, ECO:0007744|PDB:1IC1,
FT ECO:0007744|PDB:1MQ8"
FT DISULFID 52..96
FT /evidence="ECO:0000269|PubMed:12526797,
FT ECO:0000269|PubMed:9539702, ECO:0000269|PubMed:9539703,
FT ECO:0007744|PDB:1IAM, ECO:0007744|PDB:1IC1,
FT ECO:0007744|PDB:1MQ8"
FT DISULFID 135..186
FT /evidence="ECO:0000269|PubMed:12526797,
FT ECO:0000269|PubMed:9539702, ECO:0000269|PubMed:9539703,
FT ECO:0007744|PDB:1IAM, ECO:0007744|PDB:1IC1,
FT ECO:0007744|PDB:1MQ8"
FT DISULFID 237..290
FT /evidence="ECO:0000269|PubMed:15099525,
FT ECO:0007744|PDB:1P53"
FT DISULFID 332..371
FT /evidence="ECO:0000269|PubMed:15099525,
FT ECO:0007744|PDB:1P53"
FT DISULFID 403..419
FT /evidence="ECO:0000269|PubMed:15099525,
FT ECO:0007744|PDB:1P53"
FT DISULFID 431..457
FT /evidence="ECO:0000269|PubMed:15099525,
FT ECO:0007744|PDB:1P53"
FT VARIANT 56
FT /note="K -> M (in Kilifi; at homozygosity it is associated
FT with increased susceptibility to cerebral malaria;
FT dbSNP:rs5491)"
FT /evidence="ECO:0000269|PubMed:10391210,
FT ECO:0000269|PubMed:9259284, ECO:0000269|Ref.6"
FT /id="VAR_010204"
FT VARIANT 155
FT /note="K -> N (in dbSNP:rs5492)"
FT /id="VAR_014651"
FT VARIANT 241
FT /note="G -> R (in dbSNP:rs1799969)"
FT /evidence="ECO:0000269|PubMed:7525451,
FT ECO:0000269|PubMed:8557254, ECO:0000269|Ref.6"
FT /id="VAR_014186"
FT VARIANT 315
FT /note="V -> M (in dbSNP:rs5495)"
FT /id="VAR_014652"
FT VARIANT 352
FT /note="P -> L (in dbSNP:rs1801714)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_014653"
FT VARIANT 397
FT /note="R -> Q (in dbSNP:rs5497)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_014654"
FT VARIANT 469
FT /note="K -> E (in dbSNP:rs5498)"
FT /evidence="ECO:0000269|PubMed:10391210,
FT ECO:0000269|PubMed:15572059, ECO:0000269|PubMed:1680919,
FT ECO:0000269|PubMed:3340213, ECO:0000269|PubMed:3349522,
FT ECO:0000269|PubMed:7525451"
FT /id="VAR_014187"
FT VARIANT 478
FT /note="R -> W (in dbSNP:rs5030400)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_016267"
FT CONFLICT 9..10
FT /note="AL -> PV (in Ref. 10; CAA40441)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="L -> F (in Ref. 11; AAQ14902)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="A -> V (in Ref. 11; AAQ14902)"
FT /evidence="ECO:0000305"
FT STRAND 29..39
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 71..84
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1IC1"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:1IAM"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1IAM"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1IAM"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5MZA"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:1IAM"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1IAM"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:5MZA"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:2OZ4"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 267..278
FT /evidence="ECO:0007829|PDB:2OZ4"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 284..294
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 297..308
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:2OZ4"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 378..397
FT /evidence="ECO:0007829|PDB:2OZ4"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:2OZ4"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:2OZ4"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:2OZ4"
FT STRAND 464..475
FT /evidence="ECO:0007829|PDB:2OZ4"
SQ SEQUENCE 532 AA; 57825 MW; 550089365A733AFB CRC64;
MAPSSPRPAL PALLVLLGAL FPGPGNAQTS VSPSKVILPR GGSVLVTCST SCDQPKLLGI
ETPLPKKELL LPGNNRKVYE LSNVQEDSQP MCYSNCPDGQ STAKTFLTVY WTPERVELAP
LPSWQPVGKN LTLRCQVEGG APRANLTVVL LRGEKELKRE PAVGEPAEVT TTVLVRRDHH
GANFSCRTEL DLRPQGLELF ENTSAPYQLQ TFVLPATPPQ LVSPRVLEVD TQGTVVCSLD
GLFPVSEAQV HLALGDQRLN PTVTYGNDSF SAKASVSVTA EDEGTQRLTC AVILGNQSQE
TLQTVTIYSF PAPNVILTKP EVSEGTEVTV KCEAHPRAKV TLNGVPAQPL GPRAQLLLKA
TPEDNGRSFS CSATLEVAGQ LIHKNQTREL RVLYGPRLDE RDCPGNWTWP ENSQQTPMCQ
AWGNPLPELK CLKDGTFPLP IGESVTVTRD LEGTYLCRAR STQGEVTRKV TVNVLSPRYE
IVIITVVAAA VIMGTAGLST YLYNRQRKIK KYRLQQAQKG TPMKPNTQAT PP
