GENTAUR Molecular Products.

 ITAM_HUMAN              Reviewed;        1152 AA.
 P11215; Q4VAK0; Q4VAK1; Q4VAK2;
 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
 01-OCT-1996, sequence version 2.
 12-SEP-2018, entry version 208.
 RecName: Full=Integrin alpha-M;
 AltName: Full=CD11 antigen-like family member B;
 AltName: Full=CR-3 alpha chain;
 AltName: Full=Cell surface glycoprotein MAC-1 subunit alpha;
 AltName: Full=Leukocyte adhesion receptor MO1;
 AltName: Full=Neutrophil adherence receptor;
 AltName: CD_antigen=CD11b;
 Flags: Precursor;
 Name=ITGAM; Synonyms=CD11B, CR3A;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
 PubMed=2457584;
 Corbi A.L., Kishimoto T.K., Miller L.J., Springer T.A.;
 "The human leukocyte adhesion glycoprotein Mac-1 (complement receptor
 type 3, CD11b) alpha subunit. Cloning, primary structure, and relation
 to the integrins, von Willebrand factor and factor B.";
 J. Biol. Chem. 263:12403-12411(1988).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
 PubMed=2833753; DOI=10.1073/pnas.85.8.2776;
 Arnaout M.A., Remold-O'Donnell E., Pierce M.W., Harris P., Tenen D.G.;
 "Molecular cloning of the alpha subunit of human and guinea pig
 leukocyte adhesion glycoprotein Mo1: chromosomal localization and
 homology to the alpha subunits of integrins.";
 Proc. Natl. Acad. Sci. U.S.A. 85:2776-2780(1988).
 [3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
 PubMed=2454931; DOI=10.1083/jcb.106.6.2153;
 Arnaout M.A., Gupta S.K., Pierce M.W., Tenen D.G.;
 "Amino acid sequence of the alpha subunit of human leukocyte adhesion
 receptor Mo1 (complement receptor type 3).";
 J. Cell Biol. 106:2153-2158(1988).
 [4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
 PubMed=8419480;
 Fleming J.C., Pahl H.L., Gonzalez D.A., Smith T.F., Tenen D.G.;
 "Structural analysis of the CD11b gene and phylogenetic analysis of
 the alpha-integrin gene family demonstrate remarkable conservation of
 genomic organization and suggest early diversification during
 evolution.";
 J. Immunol. 150:480-490(1993).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
 HIS-77; THR-441; VAL-858 AND SER-1146.
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [6]
 NUCLEOTIDE SEQUENCE [MRNA] OF 9-1152 (ISOFORM 2).
 PubMed=2563162; DOI=10.1073/pnas.86.1.257;
 Hickstein D.D., Hickey M.J., Ozols J., Baker D.M., Back A.L.,
 Roth G.J.;
 "cDNA sequence for the alpha M subunit of the human neutrophil
 adherence receptor indicates homology to integrin alpha subunits.";
 Proc. Natl. Acad. Sci. U.S.A. 86:257-261(1989).
 [7]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9, AND TISSUE SPECIFICITY.
 PubMed=1683702; DOI=10.1073/pnas.88.23.10525;
 Shelley C.S., Arnaout M.A.;
 "The promoter of the CD11b gene directs myeloid-specific and
 developmentally regulated expression.";
 Proc. Natl. Acad. Sci. U.S.A. 88:10525-10529(1991).
 [8]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
 TISSUE=Blood;
 PubMed=1346576;
 Pahl H.L., Rosmarin A.G., Tenen D.G.;
 "Characterization of the myeloid-specific CD11b promoter.";
 Blood 79:865-870(1992).
 [9]
 PROTEIN SEQUENCE OF 17-31.
 PubMed=3539202; DOI=10.1016/0167-4838(86)90037-3;
 Pierce M.W., Remold-O'Donnell E., Todd R.F. III, Arnaout M.A.;
 "N-terminal sequence of human leukocyte glycoprotein Mo1: conservation
 across species and homology to platelet IIb/IIIa.";
 Biochim. Biophys. Acta 874:368-371(1986).
 [10]
 INTERACTION WITH JAM3.
 PubMed=12208882; DOI=10.1084/jem.20020267;
 Santoso S., Sachs U.J.H., Kroll H., Linder M., Ruf A., Preissner K.T.,
 Chavakis T.;
 "The junctional adhesion molecule 3 (JAM-3) on human platelets is a
 counterreceptor for the leukocyte integrin Mac-1.";
 J. Exp. Med. 196:679-691(2002).
 [11]
 INTERACTION WITH JAM3.
 PubMed=15194813; DOI=10.1091/mbc.E04-04-0317;
 Zen K., Babbin B.A., Liu Y., Whelan J.B., Nusrat A., Parkos C.A.;
 "JAM-C is a component of desmosomes and a ligand for CD11b/CD18-
 mediated neutrophil transepithelial migration.";
 Mol. Biol. Cell 15:3926-3937(2004).
 [12]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-900; ASN-940 AND ASN-946.
 TISSUE=Liver;
 PubMed=19159218; DOI=10.1021/pr8008012;
 Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
 "Glycoproteomics analysis of human liver tissue by combination of
 multiple enzyme digestion and hydrazide chemistry.";
 J. Proteome Res. 8:651-661(2009).
 [13]
 FUNCTION, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGB2,
 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
 SPECTROMETRY.
 PubMed=21193407; DOI=10.1074/jbc.M110.171256;
 Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A.,
 Luft F., Kettritz R.;
 "Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-
 ANCA neutrophil activation.";
 J. Biol. Chem. 286:7070-7081(2011).
 [14]
 INTERACTION WITH THBD.
 PubMed=27055590; DOI=10.1016/j.bbrc.2016.04.007;
 Kawamoto E., Okamoto T., Takagi Y., Honda G., Suzuki K., Imai H.,
 Shimaoka M.;
 "LFA-1 and Mac-1 integrins bind to the serine/threonine-rich domain of
 thrombomodulin.";
 Biochem. Biophys. Res. Commun. 473:1005-1012(2016).
 [15]
 FUNCTION, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGB2,
 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
 PubMed=28807980; DOI=10.1182/blood-2017-03-768507;
 Bai M., Grieshaber-Bouyer R., Wang J., Schmider A.B., Wilson Z.S.,
 Zeng L., Halyabar O., Godin M.D., Nguyen H.N., Levescot A., Cunin P.,
 Lefort C.T., Soberman R.J., Nigrovic P.A.;
 "CD177 modulates human neutrophil migration through activation-
 mediated integrin and chemoreceptor regulation.";
 Blood 130:2092-2100(2017).
 [16]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 148-331.
 PubMed=7867070; DOI=10.1016/0092-8674(95)90517-0;
 Lee J.O., Rieu P., Arnaout M.A., Liddington R.;
 "Crystal structure of the A domain from the alpha subunit of integrin
 CR3 (CD11b/CD18).";
 Cell 80:631-638(1995).
 [17]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 148-334.
 PubMed=8747460; DOI=10.1016/S0969-2126(01)00271-4;
 Lee J.O., Bankston L.A., Arnaout M.A., Liddington R.C.;
 "Two conformations of the integrin A-domain (I-domain): a pathway for
 activation?";
 Structure 3:1333-1340(1995).
 [18]
 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 148-337.
 PubMed=9687375; DOI=10.1016/S0969-2126(98)00093-8;
 Baldwin E.T., Sarver R.W., Bryant G.L. Jr., Curry K.A.,
 Fairbanks M.B., Finzel B.C., Garlick R.L., Heinrikson R.L.,
 Horton N.C., Kelley L.L., Mildner A.M., Moon J.B., Mott J.E.,
 Mutchler V.T., Tomich C.S., Watenpaugh K.D., Wiley V.H.;
 "Cation binding to the integrin CD11b I domain and activation model
 assessment.";
 Structure 6:923-935(1998).
 [19]
 3D-STRUCTURE MODELING OF 17-616.
 PubMed=9560195; DOI=10.1073/pnas.95.9.4870;
 Oxvig C., Springer T.A.;
 "Experimental support for a beta-propeller domain in integrin alpha-
 subunits and a calcium binding site on its lower surface.";
 Proc. Natl. Acad. Sci. U.S.A. 95:4870-4875(1998).
 [20]
 INVOLVEMENT IN SUSCEPTIBILITY TO SLEB6, AND VARIANT HIS-77.
 PubMed=18204448; DOI=10.1038/ng.71;
 Nath S.K., Han S., Kim-Howard X., Kelly J.A., Viswanathan P.,
 Gilkeson G.S., Chen W., Zhu C., McEver R.P., Kimberly R.P.,
 Alarcon-Riquelme M.E., Vyse T.J., Li Q.-Z., Wakeland E.K.,
 Merrill J.T., James J.A., Kaufman K.M., Guthridge J.M., Harley J.B.;
 "A nonsynonymous functional variant in integrin-alpha(M) (encoded by
 ITGAM) is associated with systemic lupus erythematosus.";
 Nat. Genet. 40:152-154(2008).
 [21]
 INVOLVEMENT IN SUSCEPTIBILITY TO SLEB6.
 PubMed=18204446; DOI=10.1038/ng.81;
 Harley J.B., Alarcon-Riquelme M.E., Criswell L.A., Jacob C.O.,
 Kimberly R.P., Moser K.L., Tsao B.P., Vyse T.J., Langefeld C.D.,
 Nath S.K., Guthridge J.M., Cobb B.L., Mirel D.B., Marion M.C.,
 Williams A.H., Divers J., Wang W., Frank S.G., Namjou B.,
 Gabriel S.B., Lee A.T., Gregersen P.K., Behrens T.W., Taylor K.E.,
 Fernando M., Zidovetzki R., Gaffney P.M., Edberg J.C., Rioux J.D.,
 Ojwang J.O., James J.A., Merrill J.T., Gilkeson G.S., Seldin M.F.,
 Yin H., Baechler E.C., Li Q.-Z., Wakeland E.K., Bruner G.R.,
 Kaufman K.M., Kelly J.A.;
 "Genome-wide association scan in women with systemic lupus
 erythematosus identifies susceptibility variants in ITGAM, PXK,
 KIAA1542 and other loci.";
 Nat. Genet. 40:204-210(2008).
 -!- FUNCTION: Integrin ITGAM/ITGB2 is implicated in various adhesive
     interactions of monocytes, macrophages and granulocytes as well as
     in mediating the uptake of complement-coated particles. It is
     identical with CR-3, the receptor for the iC3b fragment of the
     third complement component. It probably recognizes the R-G-D
     peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for
     fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides
     of fibrinogen gamma chain. Regulates neutrophil migration
     (PubMed:28807980). In association with beta subunit ITGB2/CD18,
     required for CD177-PRTN3-mediated activation of TNF primed
     neutrophils (PubMed:21193407). May regulate phagocytosis-induced
     apoptosis in extravasated neutrophils (By similarity). May play a
     role in mast cell development (By similarity).
     {ECO:0000250|UniProtKB:P05555, ECO:0000269|PubMed:21193407,
     ECO:0000269|PubMed:28807980, ECO:0000305}.
 -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. ITGAM
     associates with ITGB2. Found in a complex with CD177 and
     ITGB2/CD18 (PubMed:21193407). Interacts with JAM3
     (PubMed:15194813, PubMed:12208882). Interacts with THBD
     (PubMed:27055590). {ECO:0000269|PubMed:12208882,
     ECO:0000269|PubMed:15194813, ECO:0000269|PubMed:21193407,
     ECO:0000269|PubMed:27055590}.
 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21193407};
     Single-pass type I membrane protein {ECO:0000305}. Membrane raft
     {ECO:0000269|PubMed:21193407}; Single-pass type I membrane protein
     {ECO:0000305}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=1;
       IsoId=P11215-1; Sequence=Displayed;
     Name=2;
       IsoId=P11215-2; Sequence=VSP_047365;
 -!- TISSUE SPECIFICITY: Predominantly expressed in monocytes and
     granulocytes (PubMed:1346576). Expressed in neutrophils (at
     protein level) (PubMed:21193407). {ECO:0000269|PubMed:1346576,
     ECO:0000269|PubMed:21193407}.
 -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
     with I-domains do not undergo protease cleavage.
 -!- DISEASE: Systemic lupus erythematosus 6 (SLEB6) [MIM:609939]: A
     chronic, relapsing, inflammatory, and often febrile multisystemic
     disorder of connective tissue, characterized principally by
     involvement of the skin, joints, kidneys and serosal membranes. It
     is of unknown etiology, but is thought to represent a failure of
     the regulatory mechanisms of the autoimmune system. The disease is
     marked by a wide range of system dysfunctions, an elevated
     erythrocyte sedimentation rate, and the formation of LE cells in
     the blood or bone marrow. {ECO:0000269|PubMed:18204446,
     ECO:0000269|PubMed:18204448}. Note=Disease susceptibility may be
     associated with variations affecting the gene represented in this
     entry.
 -!- SIMILARITY: Belongs to the integrin alpha chain family.
     {ECO:0000305}.
 -----------------------------------------------------------------------
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 EMBL; J03925; AAA59544.1; -; mRNA.
 EMBL; M18044; AAA59491.1; -; mRNA.
 EMBL; S52227; AAB24821.1; -; Genomic_DNA.
 EMBL; S52152; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52153; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52154; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52155; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52157; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52159; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52161; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52164; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52165; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52167; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52169; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52170; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52173; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52174; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52180; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52181; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52184; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52189; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52191; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52192; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52203; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52212; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52213; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52216; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52219; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52220; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52221; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52222; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; S52226; AAB24821.1; JOINED; Genomic_DNA.
 EMBL; BC096346; AAH96346.1; -; mRNA.
 EMBL; BC096347; AAH96347.1; -; mRNA.
 EMBL; BC096348; AAH96348.1; -; mRNA.
 EMBL; BC099660; AAH99660.1; -; mRNA.
 EMBL; J04145; AAA59903.1; -; mRNA.
 EMBL; M76724; AAA58410.1; -; Genomic_DNA.
 EMBL; M84477; AAA51960.1; -; Genomic_DNA.
 CCDS; CCDS45470.1; -. [P11215-1]
 CCDS; CCDS54004.1; -. [P11215-2]
 PIR; A31108; RWHU1B.
 RefSeq; NP_000623.2; NM_000632.3. [P11215-1]
 RefSeq; NP_001139280.1; NM_001145808.1. [P11215-2]
 UniGene; Hs.172631; -.
 PDB; 1A8X; Model; -; A=17-1152.
 PDB; 1BHO; X-ray; 2.70 A; 1/2=149-337.
 PDB; 1BHQ; X-ray; 2.70 A; 1/2=149-337.
 PDB; 1IDN; X-ray; 2.70 A; 1/2=149-337.
 PDB; 1IDO; X-ray; 1.70 A; A=143-331.
 PDB; 1JLM; X-ray; 2.00 A; A=143-334.
 PDB; 1M1U; X-ray; 2.30 A; A=139-331.
 PDB; 1MF7; X-ray; 1.25 A; A=144-333.
 PDB; 1N9Z; X-ray; 2.50 A; A=144-335.
 PDB; 1NA5; X-ray; 1.50 A; A=144-335.
 PDB; 2LKE; NMR; -; A=1129-1152.
 PDB; 2LKJ; NMR; -; A=1129-1152.
 PDB; 3Q3G; X-ray; 2.70 A; E/G/I/L=148-337.
 PDB; 3QA3; X-ray; 3.00 A; E/G/I/L=148-337.
 PDB; 4M76; X-ray; 2.80 A; B=143-337.
 PDB; 4XW2; X-ray; 2.00 A; A=145-337.
 PDBsum; 1A8X; -.
 PDBsum; 1BHO; -.
 PDBsum; 1BHQ; -.
 PDBsum; 1IDN; -.
 PDBsum; 1IDO; -.
 PDBsum; 1JLM; -.
 PDBsum; 1M1U; -.
 PDBsum; 1MF7; -.
 PDBsum; 1N9Z; -.
 PDBsum; 1NA5; -.
 PDBsum; 2LKE; -.
 PDBsum; 2LKJ; -.
 PDBsum; 3Q3G; -.
 PDBsum; 3QA3; -.
 PDBsum; 4M76; -.
 PDBsum; 4XW2; -.
 ProteinModelPortal; P11215; -.
 SMR; P11215; -.
 BioGrid; 109890; 10.
 ComplexPortal; CPX-1826; Integrin alphaM-beta2 complex.
 CORUM; P11215; -.
 IntAct; P11215; 31.
 MINT; P11215; -.
 STRING; 9606.ENSP00000441691; -.
 BindingDB; P11215; -.
 ChEMBL; CHEMBL3826; -.
 iPTMnet; P11215; -.
 PhosphoSitePlus; P11215; -.
 BioMuta; ITGAM; -.
 DMDM; 1708572; -.
 EPD; P11215; -.
 MaxQB; P11215; -.
 PaxDb; P11215; -.
 PeptideAtlas; P11215; -.
 PRIDE; P11215; -.
 ProteomicsDB; 52719; -.
 Ensembl; ENST00000287497; ENSP00000287497; ENSG00000169896. [P11215-1]
 Ensembl; ENST00000544665; ENSP00000441691; ENSG00000169896. [P11215-2]
 GeneID; 3684; -.
 KEGG; hsa:3684; -.
 UCSC; uc002ebq.4; human. [P11215-1]
 CTD; 3684; -.
 DisGeNET; 3684; -.
 EuPathDB; HostDB:ENSG00000169896.16; -.
 GeneCards; ITGAM; -.
 HGNC; HGNC:6149; ITGAM.
 HPA; CAB025091; -.
 HPA; CAB072870; -.
 HPA; HPA002274; -.
 MalaCards; ITGAM; -.
 MIM; 120980; gene.
 MIM; 609939; phenotype.
 neXtProt; NX_P11215; -.
 OpenTargets; ENSG00000169896; -.
 Orphanet; 536; Systemic lupus erythematosus.
 PharmGKB; PA29949; -.
 eggNOG; ENOG410IPBA; Eukaryota.
 eggNOG; ENOG410ZFBE; LUCA.
 GeneTree; ENSGT00760000118782; -.
 HOGENOM; HOG000113114; -.
 HOVERGEN; HBG100530; -.
 InParanoid; P11215; -.
 KO; K06461; -.
 OMA; VTSENNM; -.
 OrthoDB; EOG091G01BZ; -.
 PhylomeDB; P11215; -.
 TreeFam; TF105391; -.
 Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
 Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
 Reactome; R-HSA-216083; Integrin cell surface interactions.
 Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
 Reactome; R-HSA-6798695; Neutrophil degranulation.
 SignaLink; P11215; -.
 SIGNOR; P11215; -.
 ChiTaRS; ITGAM; human.
 EvolutionaryTrace; P11215; -.
 GeneWiki; Integrin_alpha_M; -.
 GenomeRNAi; 3684; -.
 PRO; PR:P11215; -.
 Proteomes; UP000005640; Chromosome 16.
 Bgee; ENSG00000169896; Expressed in 188 organ(s), highest expression level in bone marrow cell.
 CleanEx; HS_ITGAM; -.
 ExpressionAtlas; P11215; baseline and differential.
 Genevisible; P11215; HS.
 GO; GO:0009986; C:cell surface; IDA:UniProtKB.
 GO; GO:0009897; C:external side of plasma membrane; NAS:ARUK-UCL.
 GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
 GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO; GO:0034688; C:integrin alphaM-beta2 complex; NAS:ARUK-UCL.
 GO; GO:0008305; C:integrin complex; TAS:ProtInc.
 GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
 GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
 GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
 GO; GO:0001851; F:complement component C3b binding; ISS:ARUK-UCL.
 GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0046982; F:protein heterodimerization activity; NAS:ARUK-UCL.
 GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
 GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
 GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; NAS:ARUK-UCL.
 GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO; GO:0010668; P:ectodermal cell differentiation; IEP:UniProtKB.
 GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
 GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO; GO:0001774; P:microglial cell activation; ISS:ARUK-UCL.
 GO; GO:0045963; P:negative regulation of dopamine metabolic process; ISS:ARUK-UCL.
 GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
 GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
 GO; GO:1903980; P:positive regulation of microglial cell activation; ISS:ARUK-UCL.
 GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
 GO; GO:0043315; P:positive regulation of neutrophil degranulation; IGI:UniProtKB.
 GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; ISS:ARUK-UCL.
 GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:ARUK-UCL.
 GO; GO:0032930; P:positive regulation of superoxide anion generation; IGI:UniProtKB.
 GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
 Gene3D; 2.130.10.130; -; 2.
 Gene3D; 3.40.50.410; -; 1.
 InterPro; IPR013517; FG-GAP.
 InterPro; IPR013519; Int_alpha_beta-p.
 InterPro; IPR000413; Integrin_alpha.
 InterPro; IPR013649; Integrin_alpha-2.
 InterPro; IPR018184; Integrin_alpha_C_CS.
 InterPro; IPR028994; Integrin_alpha_N.
 InterPro; IPR032695; Integrin_dom_sf.
 InterPro; IPR002035; VWF_A.
 InterPro; IPR036465; vWFA_dom_sf.
 Pfam; PF01839; FG-GAP; 1.
 Pfam; PF00357; Integrin_alpha; 1.
 Pfam; PF08441; Integrin_alpha2; 1.
 Pfam; PF00092; VWA; 1.
 PRINTS; PR01185; INTEGRINA.
 SMART; SM00191; Int_alpha; 5.
 SMART; SM00327; VWA; 1.
 SUPFAM; SSF53300; SSF53300; 1.
 SUPFAM; SSF69179; SSF69179; 3.
 PROSITE; PS51470; FG_GAP; 7.
 PROSITE; PS00242; INTEGRIN_ALPHA; 1.
 PROSITE; PS50234; VWFA; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Calcium; Cell adhesion;
 Cell membrane; Complete proteome; Direct protein sequencing;
 Disulfide bond; Glycoprotein; Immunity; Innate immunity; Integrin;
 Magnesium; Membrane; Metal-binding; Polymorphism; Receptor;
 Reference proteome; Repeat; Signal; Systemic lupus erythematosus;
 Transmembrane; Transmembrane helix.
 SIGNAL        1     16       {ECO:0000269|PubMed:3539202}.
 CHAIN        17   1152       Integrin alpha-M.
                              /FTId=PRO_0000016289.
 TOPO_DOM     17   1104       Extracellular. {ECO:0000255}.
 TRANSMEM   1105   1128       Helical. {ECO:0000255}.
 TOPO_DOM   1129   1152       Cytoplasmic. {ECO:0000255}.
 REPEAT       18     75       FG-GAP 1. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT       76    135       FG-GAP 2. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 DOMAIN      150    328       VWFA. {ECO:0000255|PROSITE-
                              ProRule:PRU00219}.
 REPEAT      339    390       FG-GAP 3. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT      391    442       FG-GAP 4. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT      443    503       FG-GAP 5. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT      506    564       FG-GAP 6. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT      569    629       FG-GAP 7. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 CA_BIND     465    473       {ECO:0000255}.
 CA_BIND     529    537       {ECO:0000255}.
 CA_BIND     592    600       {ECO:0000255}.
 MOTIF      1131   1135       GFFKR motif.
 CARBOHYD     86     86       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    240    240       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    391    391       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    469    469       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    692    692       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    696    696       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    734    734       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    801    801       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    880    880       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    900    900       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:19159218}.
 CARBOHYD    911    911       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    940    940       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:19159218}.
 CARBOHYD    946    946       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:19159218}.
 CARBOHYD    978    978       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    993    993       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1021   1021       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1044   1044       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1050   1050       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1075   1075       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID     66     73       {ECO:0000250}.
 DISULFID    105    123       {ECO:0000250}.
 DISULFID    654    711       {ECO:0000250}.
 DISULFID    770    776       {ECO:0000250}.
 DISULFID    847    864       {ECO:0000250}.
 DISULFID    998   1022       {ECO:0000250}.
 DISULFID   1027   1032       {ECO:0000250}.
 VAR_SEQ     499    499       G -> GQ (in isoform 2).
                              {ECO:0000303|PubMed:2457584,
                              ECO:0000303|PubMed:2563162}.
                              /FTId=VSP_047365.
 VARIANT      77     77       R -> H (influences susceptibility to SLE;
                              dbSNP:rs1143679).
                              {ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:18204448}.
                              /FTId=VAR_043870.
 VARIANT     441    441       M -> T (in dbSNP:rs1143680).
                              {ECO:0000269|PubMed:15489334}.
                              /FTId=VAR_043871.
 VARIANT     858    858       A -> V (in dbSNP:rs1143683).
                              {ECO:0000269|PubMed:15489334}.
                              /FTId=VAR_043872.
 VARIANT    1146   1146       P -> S (in dbSNP:rs1143678).
                              {ECO:0000269|PubMed:15489334}.
                              /FTId=VAR_043873.
 CONFLICT    965    965       L -> P (in Ref. 2; AAA59491).
                              {ECO:0000305}.
 STRAND      149    156       {ECO:0000244|PDB:1MF7}.
 HELIX       163    180       {ECO:0000244|PDB:1MF7}.
 STRAND      185    200       {ECO:0000244|PDB:1MF7}.
 HELIX       202    207       {ECO:0000244|PDB:1MF7}.
 HELIX       211    215       {ECO:0000244|PDB:1MF7}.
 HELIX       227    236       {ECO:0000244|PDB:1MF7}.
 TURN        237    239       {ECO:0000244|PDB:1MF7}.
 HELIX       241    243       {ECO:0000244|PDB:1MF7}.
 STRAND      249    259       {ECO:0000244|PDB:1MF7}.
 HELIX       268    270       {ECO:0000244|PDB:1MF7}.
 HELIX       272    277       {ECO:0000244|PDB:1MF7}.
 STRAND      280    288       {ECO:0000244|PDB:1MF7}.
 HELIX       289    291       {ECO:0000244|PDB:1MF7}.
 HELIX       294    303       {ECO:0000244|PDB:1MF7}.
 HELIX       308    311       {ECO:0000244|PDB:1MF7}.
 STRAND      312    317       {ECO:0000244|PDB:1MF7}.
 HELIX       318    324       {ECO:0000244|PDB:1MF7}.
 HELIX       325    333       {ECO:0000244|PDB:1MF7}.
 HELIX      1130   1132       {ECO:0000244|PDB:2LKE}.
 HELIX      1133   1143       {ECO:0000244|PDB:2LKE}.
 STRAND     1147   1149       {ECO:0000244|PDB:2LKE}.
 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

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