ITAM_HUMAN
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 03-AUG-2022, entry version 234.
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}.
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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 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 AlphaFoldDB; P11215; -.
DR BMRB; P11215; -.
DR SASBDB; P11215; -.
DR SMR; P11215; -.
DR BioGRID; 109890; 59.
DR ComplexPortal; CPX-1826; Integrin alphaM-beta2 complex.
DR CORUM; P11215; -.
DR IntAct; P11215; 39.
DR MINT; P11215; -.
DR STRING; 9606.ENSP00000441691; -.
DR BindingDB; P11215; -.
DR ChEMBL; CHEMBL3826; -.
DR GlyConnect; 1411; 13 N-Linked glycans (8 sites).
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; P11215; -.
DR PeptideAtlas; P11215; -.
DR PRIDE; P11215; -.
DR ProteomicsDB; 52719; -. [P11215-1]
DR ABCD; P11215; 16 sequenced antibodies.
DR Antibodypedia; 797; 3250 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 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; DYSIGSC; -.
DR OrthoDB; 73876at2759; -.
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; 6 hits in 1070 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 158 other tissues.
DR ExpressionAtlas; P11215; baseline and differential.
DR Genevisible; P11215; HS.
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:0097190; P:apoptotic signaling pathway; 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:1905114; P:cell surface receptor signaling pathway involved in cell-cell signaling; ISS:ARUK-UCL.
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: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: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:0110090; P:positive regulation of hippocampal neuron apoptotic process; ISS:ARUK-UCL.
DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
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:0150064; P:vertebrate eye-specific patterning; ISS:ARUK-UCL.
DR Gene3D; 2.130.10.130; -; 2.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
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 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 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
