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 27-MAR-2024, entry version 259. 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 MET-56, AND VARIANTS ARG-241; RP 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 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 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: Variant p.Lys56Met, known as ICAM1-Kilifi, may influence CC susceptibility to 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="https://atlasgeneticsoncology.org/gene/40909/ICAM1"; 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-12172; -. DR EMDB; EMD-3880; -. DR SMR; P05362; -. DR BioGRID; 109610; 392. DR DIP; DIP-36658N; -. DR IntAct; P05362; 50. 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 UniLectin; P05362; -. DR GlyConnect; 1423; 1 N-Linked glycan (1 site). DR GlyCosmos; P05362; 8 sites, 1 glycan. DR GlyGen; P05362; 12 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (2 sites). DR iPTMnet; P05362; -. DR PhosphoSitePlus; P05362; -. DR SwissPalm; P05362; -. DR BioMuta; ICAM1; -. DR DMDM; 68067956; -. DR CPTAC; CPTAC-219; -. DR CPTAC; CPTAC-220; -. DR CPTAC; CPTAC-5943; -. DR CPTAC; non-CPTAC-2679; -. DR EPD; P05362; -. DR jPOST; P05362; -. DR MassIVE; P05362; -. DR MaxQB; P05362; -. DR PaxDb; 9606-ENSP00000264832; -. DR PeptideAtlas; P05362; -. DR ProteomicsDB; 51830; -. DR Pumba; P05362; -. DR ABCD; P05362; 9 sequenced antibodies. DR Antibodypedia; 795; 3640 antibodies from 54 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 AGR; HGNC:5344; -. 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; 4014106at2759; -. 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; 36 hits in 1166 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 181 other cell types or tissues. DR ExpressionAtlas; P05362; baseline and differential. 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: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 CDD; cd05755; IgC2_2_ICAM-1_like; 1. DR CDD; cd20996; IgI_N_ICAM-1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. DR InterPro; IPR003988; ICAM. DR InterPro; IPR048679; ICAM1_3_5_D2. DR InterPro; IPR013768; ICAM_N. DR InterPro; IPR047012; ICAM_VCAM. 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 PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1. DR PANTHER; PTHR13771:SF18; INTERCELLULAR ADHESION MOLECULE 1; 1. DR Pfam; PF21146; ICAM1_3_5_D2; 1. DR Pfam; PF03921; ICAM_N; 1. DR Pfam; PF13895; Ig_2; 1. DR PRINTS; PR01473; ICAM. DR PRINTS; PR01472; ICAMVCAM1. DR SMART; SM00409; IG; 3. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR Genevisible; P05362; HS. 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 (probable risk factor for cerebral malaria at FT homozygosity; 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 //