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Integrin alpha-M (CD11 antigen-like family member B) (CR-3 alpha chain) (Cell surface glycoprotein MAC-1 subunit alpha) (Leukocyte adhesion receptor MO1) (Neutrophil adherence receptor) (CD antigen CD11b)

 ITAM_HUMAN              Reviewed;        1152 AA.
P11215; Q4VAK0; Q4VAK1; Q4VAK2;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
22-NOV-2017, entry version 199.
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.
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]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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 alpha-M/beta-2 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 alpha-M/beta-2 is also a receptor for
fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides
of fibrinogen gamma chain.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-M
associates with beta-2. Interacts with JAM3 (PubMed:15194813,
PubMed:12208882). Interacts with THBD (PubMed:27055590).
{ECO:0000269|PubMed:12208882, ECO:0000269|PubMed:15194813,
ECO:0000269|PubMed:27055590}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- 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.
-!- 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; 9.
CORUM; P11215; -.
IntAct; P11215; 3.
MINT; MINT-1489258; -.
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; -.
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 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; -.
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; IDA: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:0010668; P:ectodermal cell differentiation; IEP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
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.
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; 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;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; 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:rs11861251).
{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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