ID ITAM_HUMAN Reviewed; 1152 AA. AC P11215; Q4VAK0; Q4VAK1; Q4VAK2; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 27-MAR-2024, entry version 243. DE RecName: Full=Integrin alpha-M; DE AltName: Full=CD11 antigen-like family member B; DE AltName: Full=CR-3 alpha chain; DE AltName: Full=Cell surface glycoprotein MAC-1 subunit alpha; DE AltName: Full=Leukocyte adhesion receptor MO1; DE AltName: Full=Neutrophil adherence receptor; DE AltName: CD_antigen=CD11b; DE Flags: Precursor; GN Name=ITGAM; Synonyms=CD11B, CR3A; 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] (ISOFORM 2). RX PubMed=2457584; DOI=10.1016/s0021-9258(18)37770-6; RA Corbi A.L., Kishimoto T.K., Miller L.J., Springer T.A.; RT "The human leukocyte adhesion glycoprotein Mac-1 (complement receptor type RT 3, CD11b) alpha subunit. Cloning, primary structure, and relation to the RT integrins, von Willebrand factor and factor B."; RL J. Biol. Chem. 263:12403-12411(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2833753; DOI=10.1073/pnas.85.8.2776; RA Arnaout M.A., Remold-O'Donnell E., Pierce M.W., Harris P., Tenen D.G.; RT "Molecular cloning of the alpha subunit of human and guinea pig leukocyte RT adhesion glycoprotein Mo1: chromosomal localization and homology to the RT alpha subunits of integrins."; RL Proc. Natl. Acad. Sci. U.S.A. 85:2776-2780(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2454931; DOI=10.1083/jcb.106.6.2153; RA Arnaout M.A., Gupta S.K., Pierce M.W., Tenen D.G.; RT "Amino acid sequence of the alpha subunit of human leukocyte adhesion RT receptor Mo1 (complement receptor type 3)."; RL J. Cell Biol. 106:2153-2158(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=8419480; RA Fleming J.C., Pahl H.L., Gonzalez D.A., Smith T.F., Tenen D.G.; RT "Structural analysis of the CD11b gene and phylogenetic analysis of the RT alpha-integrin gene family demonstrate remarkable conservation of genomic RT organization and suggest early diversification during evolution."; RL J. Immunol. 150:480-490(1993). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-77; RP THR-441; VAL-858 AND SER-1146. 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-1152 (ISOFORM 2). RX PubMed=2563162; DOI=10.1073/pnas.86.1.257; RA Hickstein D.D., Hickey M.J., Ozols J., Baker D.M., Back A.L., Roth G.J.; RT "cDNA sequence for the alpha M subunit of the human neutrophil adherence RT receptor indicates homology to integrin alpha subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 86:257-261(1989). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9, AND TISSUE SPECIFICITY. RX PubMed=1683702; DOI=10.1073/pnas.88.23.10525; RA Shelley C.S., Arnaout M.A.; RT "The promoter of the CD11b gene directs myeloid-specific and RT developmentally regulated expression."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10525-10529(1991). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. RC TISSUE=Blood; RX PubMed=1346576; RA Pahl H.L., Rosmarin A.G., Tenen D.G.; RT "Characterization of the myeloid-specific CD11b promoter."; RL Blood 79:865-870(1992). RN [9] RP PROTEIN SEQUENCE OF 17-31. RX PubMed=3539202; DOI=10.1016/0167-4838(86)90037-3; RA Pierce M.W., Remold-O'Donnell E., Todd R.F. III, Arnaout M.A.; RT "N-terminal sequence of human leukocyte glycoprotein Mo1: conservation RT across species and homology to platelet IIb/IIIa."; RL Biochim. Biophys. Acta 874:368-371(1986). RN [10] RP FUNCTION, AND INTERACTION WITH CFH. RX PubMed=9558116; RA DiScipio R.G., Daffern P.J., Schraufstaetter I.U., Sriramarao P.; RT "Human polymorphonuclear leukocytes adhere to complement factor H through RT an interaction that involves alphaMbeta2 (CD11b/CD18)."; RL J. Immunol. 160:4057-4066(1998). RN [11] RP INTERACTION WITH JAM3. RX PubMed=12208882; DOI=10.1084/jem.20020267; RA Santoso S., Sachs U.J.H., Kroll H., Linder M., Ruf A., Preissner K.T., RA Chavakis T.; RT "The junctional adhesion molecule 3 (JAM-3) on human platelets is a RT counterreceptor for the leukocyte integrin Mac-1."; RL J. Exp. Med. 196:679-691(2002). RN [12] RP INTERACTION WITH JAM3. RX PubMed=15194813; DOI=10.1091/mbc.e04-04-0317; RA Zen K., Babbin B.A., Liu Y., Whelan J.B., Nusrat A., Parkos C.A.; RT "JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated RT neutrophil transepithelial migration."; RL Mol. Biol. Cell 15:3926-3937(2004). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-900; ASN-940 AND ASN-946. 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 [14] RP FUNCTION, AND INTERACTION WITH CFH. RX PubMed=20008295; DOI=10.4049/jimmunol.0901702; RA Losse J., Zipfel P.F., Jozsi M.; RT "Factor H and factor H-related protein 1 bind to human neutrophils via RT complement receptor 3, mediate attachment to Candida albicans, and enhance RT neutrophil antimicrobial activity."; RL J. Immunol. 184:912-921(2010). RN [15] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGB2, 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 [16] 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 [17] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGB2, 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 [18] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 148-331. RX PubMed=7867070; DOI=10.1016/0092-8674(95)90517-0; RA Lee J.O., Rieu P., Arnaout M.A., Liddington R.; RT "Crystal structure of the A domain from the alpha subunit of integrin CR3 RT (CD11b/CD18)."; RL Cell 80:631-638(1995). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 148-334. RX PubMed=8747460; DOI=10.1016/s0969-2126(01)00271-4; RA Lee J.O., Bankston L.A., Arnaout M.A., Liddington R.C.; RT "Two conformations of the integrin A-domain (I-domain): a pathway for RT activation?"; RL Structure 3:1333-1340(1995). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 148-337. RX PubMed=9687375; DOI=10.1016/s0969-2126(98)00093-8; RA Baldwin E.T., Sarver R.W., Bryant G.L. Jr., Curry K.A., Fairbanks M.B., RA Finzel B.C., Garlick R.L., Heinrikson R.L., Horton N.C., Kelley L.L., RA Mildner A.M., Moon J.B., Mott J.E., Mutchler V.T., Tomich C.S., RA Watenpaugh K.D., Wiley V.H.; RT "Cation binding to the integrin CD11b I domain and activation model RT assessment."; RL Structure 6:923-935(1998). RN [21] RP 3D-STRUCTURE MODELING OF 17-616. RX PubMed=9560195; DOI=10.1073/pnas.95.9.4870; RA Oxvig C., Springer T.A.; RT "Experimental support for a beta-propeller domain in integrin alpha- RT subunits and a calcium binding site on its lower surface."; RL Proc. Natl. Acad. Sci. U.S.A. 95:4870-4875(1998). RN [22] RP INVOLVEMENT IN SUSCEPTIBILITY TO SLEB6, AND VARIANT HIS-77. RX PubMed=18204448; DOI=10.1038/ng.71; RA Nath S.K., Han S., Kim-Howard X., Kelly J.A., Viswanathan P., RA Gilkeson G.S., Chen W., Zhu C., McEver R.P., Kimberly R.P., RA Alarcon-Riquelme M.E., Vyse T.J., Li Q.-Z., Wakeland E.K., Merrill J.T., RA James J.A., Kaufman K.M., Guthridge J.M., Harley J.B.; RT "A nonsynonymous functional variant in integrin-alpha(M) (encoded by ITGAM) RT is associated with systemic lupus erythematosus."; RL Nat. Genet. 40:152-154(2008). RN [23] RP INVOLVEMENT IN SUSCEPTIBILITY TO SLEB6. RX PubMed=18204446; DOI=10.1038/ng.81; RA Harley J.B., Alarcon-Riquelme M.E., Criswell L.A., Jacob C.O., RA Kimberly R.P., Moser K.L., Tsao B.P., Vyse T.J., Langefeld C.D., Nath S.K., RA Guthridge J.M., Cobb B.L., Mirel D.B., Marion M.C., Williams A.H., RA Divers J., Wang W., Frank S.G., Namjou B., Gabriel S.B., Lee A.T., RA Gregersen P.K., Behrens T.W., Taylor K.E., Fernando M., Zidovetzki R., RA Gaffney P.M., Edberg J.C., Rioux J.D., Ojwang J.O., James J.A., RA Merrill J.T., Gilkeson G.S., Seldin M.F., Yin H., Baechler E.C., Li Q.-Z., RA Wakeland E.K., Bruner G.R., Kaufman K.M., Kelly J.A.; RT "Genome-wide association scan in women with systemic lupus erythematosus RT identifies susceptibility variants in ITGAM, PXK, KIAA1542 and other RT loci."; RL Nat. Genet. 40:204-210(2008). CC -!- FUNCTION: Integrin ITGAM/ITGB2 is implicated in various adhesive CC interactions of monocytes, macrophages and granulocytes as well as in CC mediating the uptake of complement-coated particles and pathogens CC (PubMed:9558116, PubMed:20008295). It is identical with CR-3, the CC receptor for the iC3b fragment of the third complement component. It CC probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is CC also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 CC and P2 peptides of fibrinogen gamma chain. Regulates neutrophil CC migration (PubMed:28807980). In association with beta subunit CC ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed CC neutrophils (PubMed:21193407). May regulate phagocytosis-induced CC apoptosis in extravasated neutrophils (By similarity). May play a role CC in mast cell development (By similarity). Required with TYROBP/DAP12 in CC microglia to control production of microglial superoxide ions which CC promote the neuronal apoptosis that occurs during brain development (By CC similarity). {ECO:0000250|UniProtKB:P05555, CC ECO:0000269|PubMed:20008295, ECO:0000269|PubMed:21193407, CC ECO:0000269|PubMed:28807980, ECO:0000269|PubMed:9558116, ECO:0000305}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. ITGAM associates CC with ITGB2. Found in a complex with CD177 and ITGB2/CD18 CC (PubMed:21193407). Interacts with JAM3 (PubMed:15194813, CC PubMed:12208882). Interacts with THBD (PubMed:27055590). Interacts with CC complement factor H/CFH; this interaction mediates adhesion of CC neutrophils to pathogens leading to pathogen clearance. CC {ECO:0000269|PubMed:12208882, ECO:0000269|PubMed:15194813, CC ECO:0000269|PubMed:20008295, ECO:0000269|PubMed:21193407, CC ECO:0000269|PubMed:27055590, ECO:0000269|PubMed:9558116}. CC -!- INTERACTION: CC P11215; O95870: ABHD16A; NbExp=3; IntAct=EBI-2568251, EBI-348517; CC P11215; Q13520: AQP6; NbExp=3; IntAct=EBI-2568251, EBI-13059134; CC P11215; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2568251, EBI-11343438; CC P11215; P11912: CD79A; NbExp=3; IntAct=EBI-2568251, EBI-7797864; CC P11215; Q9HA82: CERS4; NbExp=3; IntAct=EBI-2568251, EBI-2622997; CC P11215; P58418: CLRN1; NbExp=3; IntAct=EBI-2568251, EBI-17274839; CC P11215; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2568251, EBI-6942903; CC P11215; Q9UBT3: DKK4; NbExp=3; IntAct=EBI-2568251, EBI-18030204; CC P11215; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-2568251, EBI-18535450; CC P11215; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2568251, EBI-781551; CC P11215; P48165: GJA8; NbExp=3; IntAct=EBI-2568251, EBI-17458373; CC P11215; P08034: GJB1; NbExp=3; IntAct=EBI-2568251, EBI-17565645; CC P11215; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-2568251, EBI-3917143; CC P11215; O15529: GPR42; NbExp=3; IntAct=EBI-2568251, EBI-18076404; CC P11215; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-2568251, EBI-18053395; CC P11215; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2568251, EBI-749265; CC P11215; P48051: KCNJ6; NbExp=3; IntAct=EBI-2568251, EBI-12017638; CC P11215; P43628: KIR2DL3; NbExp=3; IntAct=EBI-2568251, EBI-8632435; CC P11215; O14880: MGST3; NbExp=3; IntAct=EBI-2568251, EBI-724754; CC P11215; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-2568251, EBI-6163737; CC P11215; Q6IN84: MRM1; NbExp=3; IntAct=EBI-2568251, EBI-5454865; CC P11215; P15941-11: MUC1; NbExp=3; IntAct=EBI-2568251, EBI-17263240; CC P11215; O15173: PGRMC2; NbExp=3; IntAct=EBI-2568251, EBI-1050125; CC P11215; P57054: PIGP; NbExp=3; IntAct=EBI-2568251, EBI-17630288; CC P11215; P21246: PTN; NbExp=3; IntAct=EBI-2568251, EBI-473725; CC P11215; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-2568251, EBI-11337973; CC P11215; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-2568251, EBI-7545592; CC P11215; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-2568251, EBI-8636004; CC P11215; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-2568251, EBI-17247926; CC P11215; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2568251, EBI-18159983; CC P11215; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-2568251, EBI-17295964; CC P11215; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-2568251, EBI-8032987; CC P11215; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2568251, EBI-8638294; CC P11215; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-2568251, EBI-12195227; CC P11215; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-2568251, EBI-18178701; CC P11215; Q9Y320: TMX2; NbExp=3; IntAct=EBI-2568251, EBI-6447886; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21193407}; CC Single-pass type I membrane protein {ECO:0000305}. Membrane raft CC {ECO:0000269|PubMed:21193407}; Single-pass type I membrane protein CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P11215-1; Sequence=Displayed; CC Name=2; CC IsoId=P11215-2; Sequence=VSP_047365; CC -!- TISSUE SPECIFICITY: Predominantly expressed in monocytes and CC granulocytes (PubMed:1346576). Expressed in neutrophils (at protein CC level) (PubMed:21193407). {ECO:0000269|PubMed:1346576, CC ECO:0000269|PubMed:21193407}. CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with CC I-domains do not undergo protease cleavage. CC -!- DISEASE: Systemic lupus erythematosus 6 (SLEB6) [MIM:609939]: A CC chronic, relapsing, inflammatory, and often febrile multisystemic CC disorder of connective tissue, characterized principally by involvement CC of the skin, joints, kidneys and serosal membranes. It is of unknown CC etiology, but is thought to represent a failure of the regulatory CC mechanisms of the autoimmune system. The disease is marked by a wide CC range of system dysfunctions, an elevated erythrocyte sedimentation CC rate, and the formation of LE cells in the blood or bone marrow. CC {ECO:0000269|PubMed:18204446, ECO:0000269|PubMed:18204448}. CC Note=Disease susceptibility may be associated with variants affecting CC the gene represented in this entry. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}. 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; J03925; AAA59544.1; -; mRNA. DR EMBL; M18044; AAA59491.1; -; mRNA. DR EMBL; S52227; AAB24821.1; -; Genomic_DNA. DR EMBL; S52152; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52153; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52154; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52155; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52157; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52159; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52161; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52164; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52165; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52167; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52169; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52170; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52173; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52174; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52180; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52181; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52184; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52189; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52191; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52192; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52203; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52212; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52213; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52216; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52219; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52220; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52221; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52222; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; S52226; AAB24821.1; JOINED; Genomic_DNA. DR EMBL; BC096346; AAH96346.1; -; mRNA. DR EMBL; BC096347; AAH96347.1; -; mRNA. DR EMBL; BC096348; AAH96348.1; -; mRNA. DR EMBL; BC099660; AAH99660.1; -; mRNA. DR EMBL; J04145; AAA59903.1; -; mRNA. DR EMBL; M76724; AAA58410.1; -; Genomic_DNA. DR EMBL; M84477; AAA51960.1; -; Genomic_DNA. DR CCDS; CCDS45470.1; -. [P11215-1] DR CCDS; CCDS54004.1; -. [P11215-2] DR PIR; A31108; RWHU1B. DR RefSeq; NP_000623.2; NM_000632.3. [P11215-1] DR RefSeq; NP_001139280.1; NM_001145808.1. [P11215-2] DR PDB; 1BHO; X-ray; 2.70 A; 1/2=149-337. DR PDB; 1BHQ; X-ray; 2.70 A; 1/2=149-337. DR PDB; 1IDN; X-ray; 2.70 A; 1/2=149-337. DR PDB; 1IDO; X-ray; 1.70 A; A=143-331. DR PDB; 1JLM; X-ray; 2.00 A; A=143-334. DR PDB; 1M1U; X-ray; 2.30 A; A=139-331. DR PDB; 1MF7; X-ray; 1.25 A; A=144-333. DR PDB; 1N9Z; X-ray; 2.50 A; A=144-335. DR PDB; 1NA5; X-ray; 1.50 A; A=144-335. DR PDB; 2LKE; NMR; -; A=1129-1152. DR PDB; 2LKJ; NMR; -; A=1129-1152. DR PDB; 3Q3G; X-ray; 2.70 A; E/G/I/L=148-337. DR PDB; 3QA3; X-ray; 3.00 A; E/G/I/L=148-337. DR PDB; 4M76; X-ray; 2.80 A; B=143-337. DR PDB; 4XW2; X-ray; 2.00 A; A=145-337. DR PDB; 6RHW; X-ray; 2.75 A; C=143-337. DR PDB; 7AKK; X-ray; 3.40 A; D/H=143-337. DR PDB; 7P2D; X-ray; 3.20 A; A=17-771. DR PDB; 7USL; EM; 2.70 A; A=17-1104. DR PDB; 7USM; EM; 2.70 A; A=17-1104. DR PDB; 8CE6; X-ray; 1.58 A; A=149-337. DR PDB; 8CE9; X-ray; 2.11 A; A/B=149-337. DR PDBsum; 1BHO; -. DR PDBsum; 1BHQ; -. DR PDBsum; 1IDN; -. DR PDBsum; 1IDO; -. DR PDBsum; 1JLM; -. DR PDBsum; 1M1U; -. DR PDBsum; 1MF7; -. DR PDBsum; 1N9Z; -. DR PDBsum; 1NA5; -. DR PDBsum; 2LKE; -. DR PDBsum; 2LKJ; -. DR PDBsum; 3Q3G; -. DR PDBsum; 3QA3; -. DR PDBsum; 4M76; -. DR PDBsum; 4XW2; -. DR PDBsum; 6RHW; -. DR PDBsum; 7AKK; -. DR PDBsum; 7P2D; -. DR PDBsum; 7USL; -. DR PDBsum; 7USM; -. DR PDBsum; 8CE6; -. DR PDBsum; 8CE9; -. DR AlphaFoldDB; P11215; -. DR BMRB; P11215; -. DR EMDB; EMD-26738; -. DR EMDB; EMD-26739; -. DR SASBDB; P11215; -. DR SMR; P11215; -. DR BioGRID; 109890; 61. DR ComplexPortal; CPX-1826; Integrin alphaM-beta2 complex. DR CORUM; P11215; -. DR IntAct; P11215; 39. DR MINT; P11215; -. DR STRING; 9606.ENSP00000496959; -. DR BindingDB; P11215; -. DR ChEMBL; CHEMBL3826; -. DR GlyConnect; 1411; 13 N-Linked glycans (8 sites). DR GlyCosmos; P11215; 19 sites, 12 glycans. DR GlyGen; P11215; 19 sites, 12 N-linked glycans (8 sites). DR iPTMnet; P11215; -. DR PhosphoSitePlus; P11215; -. DR BioMuta; ITGAM; -. DR DMDM; 1708572; -. DR EPD; P11215; -. DR jPOST; P11215; -. DR MassIVE; P11215; -. DR MaxQB; P11215; -. DR PaxDb; 9606-ENSP00000441691; -. DR PeptideAtlas; P11215; -. DR PRIDE; P11215; -. DR ProteomicsDB; 52719; -. [P11215-1] DR Pumba; P11215; -. DR ABCD; P11215; 16 sequenced antibodies. DR Antibodypedia; 797; 3545 antibodies from 51 providers. DR CPTC; P11215; 1 antibody. DR DNASU; 3684; -. DR Ensembl; ENST00000544665.9; ENSP00000441691.3; ENSG00000169896.18. [P11215-1] DR Ensembl; ENST00000648685.1; ENSP00000496959.1; ENSG00000169896.18. [P11215-2] DR GeneID; 3684; -. DR KEGG; hsa:3684; -. DR MANE-Select; ENST00000544665.9; ENSP00000441691.3; NM_000632.4; NP_000623.2. DR UCSC; uc002ebq.4; human. [P11215-1] DR AGR; HGNC:6149; -. DR CTD; 3684; -. DR DisGeNET; 3684; -. DR GeneCards; ITGAM; -. DR HGNC; HGNC:6149; ITGAM. DR HPA; ENSG00000169896; Tissue enriched (bone). DR MalaCards; ITGAM; -. DR MIM; 120980; gene. DR MIM; 609939; phenotype. DR neXtProt; NX_P11215; -. DR OpenTargets; ENSG00000169896; -. DR Orphanet; 536; Systemic lupus erythematosus. DR PharmGKB; PA29949; -. DR VEuPathDB; HostDB:ENSG00000169896; -. DR eggNOG; KOG3637; Eukaryota. DR GeneTree; ENSGT00940000161282; -. DR HOGENOM; CLU_004111_3_0_1; -. DR InParanoid; P11215; -. DR OMA; CQRIKCD; -. DR OrthoDB; 3816176at2759; -. DR PhylomeDB; P11215; -. DR TreeFam; TF105391; -. DR PathwayCommons; P11215; -. DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade. 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; P11215; -. DR SIGNOR; P11215; -. DR BioGRID-ORCS; 3684; 10 hits in 1145 CRISPR screens. DR ChiTaRS; ITGAM; human. DR EvolutionaryTrace; P11215; -. DR GeneWiki; Integrin_alpha_M; -. DR GenomeRNAi; 3684; -. DR Pharos; P11215; Tbio. DR PRO; PR:P11215; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P11215; Protein. DR Bgee; ENSG00000169896; Expressed in monocyte and 159 other cell types or tissues. DR ExpressionAtlas; P11215; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0034688; C:integrin alphaM-beta2 complex; ISS:ARUK-UCL. DR GO; GO:0008305; C:integrin complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB. 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; IC:ARUK-UCL. DR GO; GO:0038024; F:cargo receptor activity; ISS:ARUK-UCL. 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:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; NAS:ARUK-UCL. DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central. DR GO; GO:0002430; P:complement receptor mediated signaling pathway; ISS:ARUK-UCL. DR GO; GO:0150062; P:complement-mediated synapse pruning; ISS:ARUK-UCL. DR GO; GO:0010668; P:ectodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0030900; P:forebrain development; ISS:ARUK-UCL. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0001774; P:microglial cell activation; ISS:ARUK-UCL. DR GO; GO:0045963; P:negative regulation of dopamine metabolic process; ISS:ARUK-UCL. DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL. DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; ISS:UniProtKB. DR GO; GO:0043315; P:positive regulation of neutrophil degranulation; IGI:UniProtKB. DR GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; ISS:ARUK-UCL. DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:ARUK-UCL. DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IGI:UniProtKB. DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL. DR GO; GO:1904643; P:response to curcumin; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0140459; P:response to Gram-positive bacterium; IEA:Ensembl. DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0150064; P:vertebrate eye-specific patterning; ISS:ARUK-UCL. DR CDD; cd01469; vWA_integrins_alpha_subunit; 1. DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2. DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR013649; Integrin_alpha_Ig-like_1. DR InterPro; IPR048285; Integrin_alpha_Ig-like_2. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR InterPro; IPR048633; ITGAX-like_Ig_3. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1. DR PANTHER; PTHR23220:SF130; INTEGRIN ALPHA-M; 1. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_A_Ig_1; 1. DR Pfam; PF20805; Integrin_A_Ig_2; 1. DR Pfam; PF00357; Integrin_alpha; 1. DR Pfam; PF21520; ITGAX-like_Ig_3; 1. DR Pfam; PF00092; VWA; 1. DR PRINTS; PR01185; INTEGRINA. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00191; Int_alpha; 5. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. DR PROSITE; PS50234; VWFA; 1. DR Genevisible; P11215; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity; KW Innate immunity; Integrin; Magnesium; Membrane; Metal-binding; Receptor; KW Reference proteome; Repeat; Signal; Systemic lupus erythematosus; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..16 FT /evidence="ECO:0000269|PubMed:3539202" FT CHAIN 17..1152 FT /note="Integrin alpha-M" FT /id="PRO_0000016289" FT TOPO_DOM 17..1104 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1105..1128 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1129..1152 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 18..75 FT /note="FG-GAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 76..135 FT /note="FG-GAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT DOMAIN 150..328 FT /note="VWFA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT REPEAT 339..390 FT /note="FG-GAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 391..442 FT /note="FG-GAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 443..503 FT /note="FG-GAP 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 506..564 FT /note="FG-GAP 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 569..629 FT /note="FG-GAP 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT MOTIF 1131..1135 FT /note="GFFKR motif" FT BINDING 465 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 467 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 469 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 473 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 529 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 531 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 533 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 537 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 592 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 596 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 600 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT CARBOHYD 86 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 240 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 391 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 469 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 692 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 696 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 734 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 801 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 880 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 900 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 911 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 940 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 946 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 978 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 993 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1021 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1044 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1050 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1075 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 66..73 FT /evidence="ECO:0000250" FT DISULFID 105..123 FT /evidence="ECO:0000250" FT DISULFID 654..711 FT /evidence="ECO:0000250" FT DISULFID 770..776 FT /evidence="ECO:0000250" FT DISULFID 847..864 FT /evidence="ECO:0000250" FT DISULFID 998..1022 FT /evidence="ECO:0000250" FT DISULFID 1027..1032 FT /evidence="ECO:0000250" FT VAR_SEQ 499 FT /note="G -> GQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2457584, FT ECO:0000303|PubMed:2563162" FT /id="VSP_047365" FT VARIANT 77 FT /note="R -> H (influences susceptibility to SLE; FT dbSNP:rs1143679)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18204448" FT /id="VAR_043870" FT VARIANT 441 FT /note="M -> T (in dbSNP:rs1143680)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_043871" FT VARIANT 858 FT /note="A -> V (in dbSNP:rs1143683)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_043872" FT VARIANT 1146 FT /note="P -> S (in dbSNP:rs1143678)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_043873" FT CONFLICT 965 FT /note="L -> P (in Ref. 2; AAA59491)" FT /evidence="ECO:0000305" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 32..35 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 36..41 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 42..44 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:7USM" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 91..96 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 101..112 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 117..126 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:7P2D" FT STRAND 149..156 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 163..180 FT /evidence="ECO:0007829|PDB:1MF7" FT STRAND 185..200 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 202..207 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 211..215 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 227..236 FT /evidence="ECO:0007829|PDB:1MF7" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 241..243 FT /evidence="ECO:0007829|PDB:1MF7" FT STRAND 249..259 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 272..277 FT /evidence="ECO:0007829|PDB:1MF7" FT STRAND 280..288 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 308..311 FT /evidence="ECO:0007829|PDB:1MF7" FT STRAND 312..317 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 318..324 FT /evidence="ECO:0007829|PDB:1MF7" FT HELIX 325..333 FT /evidence="ECO:0007829|PDB:1MF7" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 355..359 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 361..367 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 371..374 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 378..385 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 387..390 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 397..399 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 406..413 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 416..423 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 426..428 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 430..438 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 441..449 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 459..464 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 474..483 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 485..495 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 515..520 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 524..528 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 530..534 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 537..542 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 545..548 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 550..555 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 559..561 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 568..572 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 573..575 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 585..591 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 593..597 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 600..605 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 608..614 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 617..631 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 633..636 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 640..642 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 645..647 FT /evidence="ECO:0007829|PDB:7P2D" FT STRAND 650..659 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 672..680 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 681..683 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 684..686 FT /evidence="ECO:0007829|PDB:7USM" FT TURN 692..694 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 695..705 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 710..717 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 729..739 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 743..746 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 759..764 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 770..773 FT /evidence="ECO:0007829|PDB:7USM" FT STRAND 780..785 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 792..794 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 798..800 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 803..808 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 813..815 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 817..822 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 826..832 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 845..848 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 860..871 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 875..885 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 894..902 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 911..913 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 914..924 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 928..931 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 938..940 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 949..958 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 965..979 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 981..992 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 997..1003 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 1010..1016 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 1019..1021 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 1024..1037 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 1042..1051 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 1060..1062 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 1064..1073 FT /evidence="ECO:0007829|PDB:7USL" FT TURN 1076..1078 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 1086..1088 FT /evidence="ECO:0007829|PDB:7USL" FT STRAND 1089..1098 FT /evidence="ECO:0007829|PDB:7USL" FT HELIX 1130..1132 FT /evidence="ECO:0007829|PDB:2LKE" FT HELIX 1133..1143 FT /evidence="ECO:0007829|PDB:2LKE" FT STRAND 1147..1149 FT /evidence="ECO:0007829|PDB:2LKE" SQ SEQUENCE 1152 AA; 127179 MW; DF77408ED5EE25F9 CRC64; MALRVLLLTA LTLCHGFNLD TENAMTFQEN ARGFGQSVVQ LQGSRVVVGA PQEIVAANQR GSLYQCDYST GSCEPIRLQV PVEAVNMSLG LSLAATTSPP QLLACGPTVH QTCSENTYVK GLCFLFGSNL RQQPQKFPEA LRGCPQEDSD IAFLIDGSGS IIPHDFRRMK EFVSTVMEQL KKSKTLFSLM QYSEEFRIHF TFKEFQNNPN PRSLVKPITQ LLGRTHTATG IRKVVRELFN ITNGARKNAF KILVVITDGE KFGDPLGYED VIPEADREGV IRYVIGVGDA FRSEKSRQEL NTIASKPPRD HVFQVNNFEA LKTIQNQLRE KIFAIEGTQT GSSSSFEHEM SQEGFSAAIT SNGPLLSTVG SYDWAGGVFL YTSKEKSTFI NMTRVDSDMN DAYLGYAAAI ILRNRVQSLV LGAPRYQHIG LVAMFRQNTG MWESNANVKG TQIGAYFGAS LCSVDVDSNG STDLVLIGAP HYYEQTRGGQ VSVCPLPRGR ARWQCDAVLY GEQGQPWGRF GAALTVLGDV NGDKLTDVAI GAPGEEDNRG AVYLFHGTSG SGISPSHSQR IAGSKLSPRL QYFGQSLSGG QDLTMDGLVD LTVGAQGHVL LLRSQPVLRV KAIMEFNPRE VARNVFECND QVVKGKEAGE VRVCLHVQKS TRDRLREGQI QSVVTYDLAL DSGRPHSRAV FNETKNSTRR QTQVLGLTQT CETLKLQLPN CIEDPVSPIV LRLNFSLVGT PLSAFGNLRP VLAEDAQRLF TALFPFEKNC GNDNICQDDL SITFSFMSLD CLVVGGPREF NVTVTVRNDG EDSYRTQVTF FFPLDLSYRK VSTLQNQRSQ RSWRLACESA SSTEVSGALK STSCSINHPI FPENSEVTFN ITFDVDSKAS LGNKLLLKAN VTSENNMPRT NKTEFQLELP VKYAVYMVVT SHGVSTKYLN FTASENTSRV MQHQYQVSNL GQRSLPISLV FLVPVRLNQT VIWDRPQVTF SENLSSTCHT KERLPSHSDF LAELRKAPVV NCSIAVCQRI QCDIPFFGIQ EEFNATLKGN LSFDWYIKTS HNHLLIVSTA EILFNDSVFT LLPGQGAFVR SQTETKVEPF EVPNPLPLIV GSSVGGLLLL ALITAALYKL GFFKRQYKDM MSEGGPPGAE PQ //