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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.
13-FEB-2019, entry version 213.
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]
FUNCTION, AND INTERACTION WITH CFH.
PubMed=9558116;
DiScipio R.G., Daffern P.J., Schraufstaetter I.U., Sriramarao P.;
"Human polymorphonuclear leukocytes adhere to complement factor H
through an interaction that involves alphaMbeta2 (CD11b/CD18).";
J. Immunol. 160:4057-4066(1998).
[11]
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).
[12]
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).
[13]
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).
[14]
FUNCTION, AND INTERACTION WITH CFH.
PubMed=20008295; DOI=10.4049/jimmunol.0901702;
Losse J., Zipfel P.F., Jozsi M.;
"Factor H and factor H-related protein 1 bind to human neutrophils via
complement receptor 3, mediate attachment to Candida albicans, and
enhance neutrophil antimicrobial activity.";
J. Immunol. 184:912-921(2010).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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 and
pathogens (PubMed:9558116, PubMed:20008295). 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:20008295, ECO:0000269|PubMed:21193407,
ECO:0000269|PubMed:28807980, ECO:0000269|PubMed:9558116,
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). Interacts with complement factor H/CFH; this
interaction mediates adhesion of neutrophils to pathogens leading
to pathogen clearance. {ECO:0000269|PubMed:12208882,
ECO:0000269|PubMed:15194813, ECO:0000269|PubMed:20008295,
ECO:0000269|PubMed:21193407, ECO:0000269|PubMed:27055590,
ECO:0000269|PubMed:9558116}.
-!- 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; -.
GlyConnect; 1411; -.
iPTMnet; P11215; -.
PhosphoSitePlus; P11215; -.
BioMuta; ITGAM; -.
DMDM; 1708572; -.
EPD; P11215; -.
jPOST; P11215; -.
MaxQB; P11215; -.
PaxDb; P11215; -.
PeptideAtlas; P11215; -.
PRIDE; P11215; -.
ProteomicsDB; 52719; -.
Ensembl; ENST00000287497; ENSP00000287497; ENSG00000169896. [P11215-1]
Ensembl; ENST00000544665; ENSP00000441691; ENSG00000169896. [P11215-2]
Ensembl; ENST00000648685; ENSP00000496959; 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; ENSGT00940000161282; -.
HOGENOM; HOG000113114; -.
HOVERGEN; HBG100530; -.
InParanoid; P11215; -.
KO; K06461; -.
OMA; MMSEGGP; -.
OrthoDB; 73876at2759; -.
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.
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:0001540; F:amyloid-beta binding; IC:ARUK-UCL.
GO; GO:0038024; F:cargo receptor activity; ISS:ARUK-UCL.
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:0097190; P:apoptotic signaling pathway; ISS:ARUK-UCL.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:1905114; P:cell surface receptor signaling pathway involved in cell-cell signaling; ISS:ARUK-UCL.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; NAS:ARUK-UCL.
GO; GO:0150062; P:complement-mediated synapse pruning; ISS: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:0030900; P:forebrain development; ISS:ARUK-UCL.
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:0110090; P:positive regulation of hippocampal neuron apoptotic process; ISS:ARUK-UCL.
GO; GO:1903980; P:positive regulation of microglial cell activation; ISS:ARUK-UCL.
GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; ISS:UniProtKB.
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:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
GO; GO:0150064; P:vertebrate eye-specific patterning; ISS:ARUK-UCL.
Gene3D; 2.130.10.130; -; 1.
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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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1963: The effect of Glucocorticoids on target gene expression
WP2328: Allograft rejection
WP1614: 1- and 2-Methylnaphthalene degradation
WP566: canonical wnt - zebrafish
WP1566: Citrate cycle (TCA cycle)
WP1655: Geraniol degradation
WP2292: Chemokine signaling pathway
WP1003: Ovarian Infertility Genes
WP1011: T Cell Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP1047: TNF-alpha NF-kB Signaling Pathway
WP1069: Integrin-mediated cell adhesion
WP1120: Ovarian Infertility Genes
WP1130: T Cell Receptor Signaling Pathway
WP1144: B Cell Receptor Signaling Pathway
WP1163: TNF-alpha NF-kB Signaling Pathway
WP1185: Integrin-mediated cell adhesion
WP1209: EBV LMP1 signaling
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1340: Ovarian Infertility Genes
WP1345: T Cell Receptor Signaling Pathway
WP1354: B Cell Receptor Signaling Pathway
WP1369: TNF-alpha NF-kB Signaling Pathway
WP1386: Integrin-mediated cell adhesion

Related Genes :
[ITGAM CD11B CR3A] 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)
[ITGAL CD11A] Integrin alpha-L (CD11 antigen-like family member A) (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (CD antigen CD11a)
[TIF1 TIF41A YKR059W; TIF2 TIF41B YJL138C J0660] ATP-dependent RNA helicase eIF4A (EC 3.6.4.13) (Eukaryotic initiation factor 4A) (eIF-4A) (Stimulator factor I 37 kDa component) (Translation initiation factor 1/2) (p37)
[Itgb2] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGB2 CD18 MFI7] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[CD177 NB1 PRV1 UNQ595/PRO1181] CD177 antigen (Human neutrophil alloantigen 2a) (HNA-2a) (NB1 glycoprotein) (NB1 GP) (Polycythemia rubra vera protein 1) (PRV-1) (CD antigen CD177)
[SELL LNHR LYAM1] L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte surface antigen Leu-8) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (TQ1) (gp90-MEL) (CD antigen CD62L)
[Itga4] Integrin alpha-4 (CD49 antigen-like family member D) (Integrin alpha-IV) (Lymphocyte Peyer patch adhesion molecules subunit alpha) (LPAM subunit alpha) (VLA-4 subunit alpha) (CD antigen CD49d)
[ITGAV MSK8 VNRA VTNR] Integrin alpha-V (Vitronectin receptor) (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain]
[Sell Lnhr Ly-22 Ly22] L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (Lymphocyte antigen 22) (Ly-22) (Lymphocyte surface MEL-14 antigen) (CD antigen CD62L)
[ITGA4 CD49D] Integrin alpha-4 (CD49 antigen-like family member D) (Integrin alpha-IV) (VLA-4 subunit alpha) (CD antigen CD49d)
[SIRPA BIT MFR MYD1 PTPNS1 SHPS1 SIRP] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (Signal-regulatory protein alpha-2) (Sirp-alpha-2) (Signal-regulatory protein alpha-3) (Sirp-alpha-3) (p84) (CD antigen CD172a)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[ITGA2 CD49B] Integrin alpha-2 (CD49 antigen-like family member B) (Collagen receptor) (Platelet membrane glycoprotein Ia) (GPIa) (VLA-2 subunit alpha) (CD antigen CD49b)
[CD44 LHR MDU2 MDU3 MIC4] CD44 antigen (CDw44) (Epican) (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[ITGB2 CD18] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGB2 CD18] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGB2 CD18] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[POL RR33_52434gpPOL] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[ITGA6] Integrin alpha-6 (CD49 antigen-like family member F) (VLA-6) (CD antigen CD49f) [Cleaved into: Integrin alpha-6 heavy chain; Integrin alpha-6 light chain; Processed integrin alpha-6 (Alpha6p)]
[Sell Lnhr Ly-22] L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (Lymphocyte antigen 22) (Ly-22) (Lymphocyte surface MEL-14 antigen) (CD antigen CD62L)
[Itgav] Integrin alpha-V (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain]
[EPCAM GA733-2 M1S2 M4S1 MIC18 TACSTD1 TROP1] Epithelial cell adhesion molecule (Ep-CAM) (Adenocarcinoma-associated antigen) (Cell surface glycoprotein Trop-1) (Epithelial cell surface antigen) (Epithelial glycoprotein) (EGP) (Epithelial glycoprotein 314) (EGP314) (hEGP314) (KS 1/4 antigen) (KSA) (Major gastrointestinal tumor-associated protein GA733-2) (Tumor-associated calcium signal transducer 1) (CD antigen CD326)
[Sirpa Bit Myd1 Ptpns1 Shps1 Sirp] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (mSIRP-alpha1) (p84) (CD antigen CD172a)
[Cd79a Iga Mb-1] B-cell antigen receptor complex-associated protein alpha chain (Ig-alpha) (MB-1 membrane glycoprotein) (Membrane-bound immunoglobulin-associated protein) (Surface IgM-associated protein) (CD antigen CD79a)
[CD79A IGA MB1] B-cell antigen receptor complex-associated protein alpha chain (Ig-alpha) (MB-1 membrane glycoprotein) (Membrane-bound immunoglobulin-associated protein) (Surface IgM-associated protein) (CD antigen CD79a)
[LILRB2 ILT4 LIR2 MIR10] Leukocyte immunoglobulin-like receptor subfamily B member 2 (LIR-2) (Leukocyte immunoglobulin-like receptor 2) (CD85 antigen-like family member D) (Immunoglobulin-like transcript 4) (ILT-4) (Monocyte/macrophage immunoglobulin-like receptor 10) (MIR-10) (CD antigen CD85d)
[CD84 SLAMF5] SLAM family member 5 (Cell surface antigen MAX.3) (Hly9-beta) (Leukocyte differentiation antigen CD84) (Signaling lymphocytic activation molecule 5) (CD antigen CD84)
[LILRB1 ILT2 LIR1 MIR7] Leukocyte immunoglobulin-like receptor subfamily B member 1 (LIR-1) (Leukocyte immunoglobulin-like receptor 1) (CD85 antigen-like family member J) (Immunoglobulin-like transcript 2) (ILT-2) (Monocyte/macrophage immunoglobulin-like receptor 7) (MIR-7) (CD antigen CD85j)

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