FCG2B_HUMAN
ID FCG2B_HUMAN Reviewed; 310 AA.
AC P31994; A6H8N3; O95649; Q53X85; Q5VXA9; Q8NIA1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor II-b;
DE Short=IgG Fc receptor II-b;
DE AltName: Full=CDw32;
DE AltName: Full=Fc-gamma RII-b;
DE Short=Fc-gamma-RIIb;
DE Short=FcRII-b;
DE AltName: CD_antigen=CD32;
DE Flags: Precursor;
GN Name=FCGR2B; Synonyms=CD32, FCG2, IGFR2;
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] (ISOFORMS IIB1; IIB2; 4 AND 5), AND VARIANT
RP THR-232.
RC TISSUE=Lymphocyte;
RA Ng S., Sinclair N.R.S., Anderson C., Bell D.A., Cairns E.;
RT "Fc-gamma-RIIb nucleotide sequences in SLE and non-SLE humans in vivo
RT derived lymphocytes.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
RC TISSUE=Placenta;
RX PubMed=2531080; DOI=10.1002/j.1460-2075.1989.tb08540.x;
RA Stuart S.G., Simister N.E., Clarkson S.B., Kacinski B.M., Shapiro M.,
RA Mellman I.;
RT "Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in
RT macrophages, lymphocytes and IgG-transporting placental epithelium.";
RL EMBO J. 8:3657-3666(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1; IIB2 AND IIB3), AND VARIANT
RP PHE-205.
RX PubMed=2529342; DOI=10.1084/jem.170.4.1369;
RA Brooks D.G., Qiu W.Q., Luster A.D., Ravetch J.V.;
RT "Structure and expression of human IgG FcRII(CD32). Functional
RT heterogeneity is encoded by the alternatively spliced products of multiple
RT genes.";
RL J. Exp. Med. 170:1369-1385(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
RC TISSUE=Placenta;
RX PubMed=2142460; DOI=10.1002/eji.1830200624;
RA Engelhardt W., Geerds C., Frey J.;
RT "Distribution, inducibility and biological function of the cloned and
RT expressed human beta Fc receptor II.";
RL Eur. J. Immunol. 20:1367-1377(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIB2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IIB1 AND IIB2).
RC TISSUE=Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 132-253, INVOLVEMENT IN SLE, AND VARIANT
RP THR-232.
RX PubMed=12115230; DOI=10.1002/art.10257;
RA Kyogoku C., Dijstelbloem H.M., Tsuchiya N., Hatta Y., Kato H.,
RA Yamaguchi A., Fukazawa T., Jansen M.D., Hashimoto H., van de Winkel J.G.J.,
RA Kallenberg C.G.M., Tokunaga K.;
RT "Fc gamma receptor gene polymorphisms in Japanese patients with systemic
RT lupus erythematosus: contribution of FCGR2B to genetic susceptibility.";
RL Arthritis Rheum. 46:1242-1254(2002).
RN [9]
RP INTERACTION WITH FGR.
RX PubMed=8327512; DOI=10.1073/pnas.90.13.6305;
RA Hamada F., Aoki M., Akiyama T., Toyoshima K.;
RT "Association of immunoglobulin G Fc receptor II with Src-like protein-
RT tyrosine kinase Fgr in neutrophils.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993).
RN [10]
RP PHOSPHORYLATION AT TYR-292.
RX PubMed=8756631; DOI=10.1128/mcb.16.9.4735;
RA Bewarder N., Weinrich V., Budde P., Hartmann D., Flaswinkel H., Reth M.,
RA Frey J.;
RT "In vivo and in vitro specificity of protein tyrosine kinases for
RT immunoglobulin G receptor (FcgammaRII) phosphorylation.";
RL Mol. Cell. Biol. 16:4735-4743(1996).
RN [11]
RP INTERACTION WITH LYN.
RX PubMed=9232445; DOI=10.1016/s0165-2478(97)00055-2;
RA Sarmay G., Koncz G., Pecht I., Gergely J.;
RT "Fc gamma receptor type IIb induced recruitment of inositol and protein
RT phosphatases to the signal transductory complex of human B-cell.";
RL Immunol. Lett. 57:159-164(1997).
RN [12]
RP INTERACTION WITH MEASLES VIRUS N PROTEIN (MICROBIAL INFECTION).
RX PubMed=15914856; DOI=10.1099/vir.0.80791-0;
RA Laine D., Bourhis J.-M., Longhi S., Flacher M., Cassard L., Canard B.,
RA Sautes-Fridman C., Rabourdin-Combe C., Valentin H.;
RT "Measles virus nucleoprotein induces cell-proliferation arrest and
RT apoptosis through NTAIL-NR and NCORE-FcgammaRIIB1 interactions,
RT respectively.";
RL J. Gen. Virol. 86:1771-1784(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 46-217, AND DISULFIDE BONDS.
RX PubMed=10064577; DOI=10.1093/emboj/18.5.1095;
RA Sondermann P., Huber R., Jacob U.;
RT "Crystal structure of the soluble form of the human fcgamma-receptor IIb: a
RT new member of the immunoglobulin superfamily at 1.7 A resolution.";
RL EMBO J. 18:1095-1103(1999).
RN [14]
RP VARIANT ASP-258.
RX PubMed=8466861; DOI=10.1093/intimm/5.3.239;
RA Warmerdam P.A., van den Herik-Oudijk I.E., Parren P.W., Westerdaal N.A.,
RA van de Winkel J.G., Capel P.J.;
RT "Interaction of a human Fc gamma RIIb1 (CD32) isoform with murine and human
RT IgG subclasses.";
RL Int. Immunol. 5:239-247(1993).
RN [15]
RP POLYMORPHISM, INVOLVEMENT IN RESISTANCE TO MALARIA, VARIANT THR-232, AND
RP CHARACTERIZATION OF VARIANT THR-232.
RX PubMed=17435165; DOI=10.1073/pnas.0608889104;
RA Clatworthy M.R., Willcocks L., Urban B., Langhorne J., Williams T.N.,
RA Peshu N., Watkins N.A., Floto R.A., Smith K.G.;
RT "Systemic lupus erythematosus-associated defects in the inhibitory receptor
RT FcgammaRIIb reduce susceptibility to malaria.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7169-7174(2007).
RN [16]
RP POLYMORPHISM, INVOLVEMENT IN SLE, VARIANT THR-232, AND INVOLVEMENT IN
RP RESISTANCE TO MALARIA.
RX PubMed=20385827; DOI=10.1073/pnas.0915133107;
RA Willcocks L.C., Carr E.J., Niederer H.A., Rayner T.F., Williams T.N.,
RA Yang W., Scott J.A., Urban B.C., Peshu N., Vyse T.J., Lau Y.L., Lyons P.A.,
RA Smith K.G.;
RT "A defunctioning polymorphism in FCGR2B is associated with protection
RT against malaria but susceptibility to systemic lupus erythematosus.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7881-7885(2010).
CC -!- FUNCTION: Receptor for the Fc region of complexed or aggregated
CC immunoglobulins gamma. Low affinity receptor. Involved in a variety of
CC effector and regulatory functions such as phagocytosis of immune
CC complexes and modulation of antibody production by B-cells. Binding to
CC this receptor results in down-modulation of previous state of cell
CC activation triggered via antigen receptors on B-cells (BCR), T-cells
CC (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate
CC endocytosis or phagocytosis. Isoform IIB2 does not trigger
CC phagocytosis.
CC -!- SUBUNIT: Interacts with INPP5D/SHIP1. Interacts with FGR. Interacts
CC with LYN. {ECO:0000269|PubMed:8327512, ECO:0000269|PubMed:9232445}.
CC -!- SUBUNIT: (Microbial infection) Isoform IIB1 interacts with measles
CC virus protein N. Protein N is released in the blood following lysis of
CC measles infected cells. This interaction presumably block inflammatory
CC immune response. {ECO:0000269|PubMed:15914856}.
CC -!- INTERACTION:
CC P31994; P01857: IGHG1; NbExp=31; IntAct=EBI-724784, EBI-356114;
CC P31994; Q92835: INPP5D; NbExp=3; IntAct=EBI-724784, EBI-1380477;
CC P31994; Q92876: KLK6; NbExp=3; IntAct=EBI-724784, EBI-2432309;
CC P31994; P16333: NCK1; NbExp=2; IntAct=EBI-724784, EBI-389883;
CC P31994; P19174: PLCG1; NbExp=2; IntAct=EBI-724784, EBI-79387;
CC P31994; P29350: PTPN6; NbExp=3; IntAct=EBI-724784, EBI-78260;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=IIB1 {ECO:0000303|PubMed:2529342};
CC IsoId=P31994-1; Sequence=Displayed;
CC Name=IIB2 {ECO:0000303|PubMed:2529342};
CC IsoId=P31994-2; Sequence=VSP_002643;
CC Name=IIB3 {ECO:0000303|PubMed:2529342};
CC IsoId=P31994-3; Sequence=VSP_002642;
CC Name=4;
CC IsoId=P31994-4; Sequence=VSP_058635;
CC Name=5;
CC IsoId=P31994-5; Sequence=VSP_058635, VSP_002643;
CC -!- TISSUE SPECIFICITY: Is the most broadly distributed Fc-gamma-receptor.
CC Expressed in monocyte, neutrophils, macrophages, basophils,
CC eosinophils, Langerhans cells, B-cells, platelets cells and placenta
CC (endothelial cells). Not detected in natural killer cells.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- PTM: Phosphorylated by the SRC-type Tyr-kinases LYN and BLK.
CC {ECO:0000269|PubMed:8756631}.
CC -!- POLYMORPHISM: FCGR2B polymorphisms can influence susceptibility or
CC resistance to malaria [MIM:611162]. {ECO:0000269|PubMed:17435165,
CC ECO:0000269|PubMed:20385827}.
CC -!- DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic,
CC relapsing, inflammatory, and often febrile multisystemic disorder of
CC connective tissue, characterized principally by involvement of the
CC skin, joints, kidneys and serosal membranes. It is of unknown etiology,
CC but is thought to represent a failure of the regulatory mechanisms of
CC the autoimmune system. The disease is marked by a wide range of system
CC dysfunctions, an elevated erythrocyte sedimentation rate, and the
CC formation of LE cells in the blood or bone marrow.
CC {ECO:0000269|PubMed:12115230, ECO:0000269|PubMed:20385827}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- CAUTION: Has sometimes been attributed to correspond to FcR-IIC.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35645.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FCGR2BID397.html";
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DR EMBL; U87560; AAD00627.1; -; mRNA.
DR EMBL; U87561; AAD00628.1; -; mRNA.
DR EMBL; U87562; AAD00629.1; -; mRNA.
DR EMBL; U87563; AAD00630.1; -; mRNA.
DR EMBL; U87564; AAD00631.1; -; mRNA.
DR EMBL; U87565; AAD00632.1; -; mRNA.
DR EMBL; U87566; AAD00633.1; -; mRNA.
DR EMBL; U87567; AAD00634.1; -; mRNA.
DR EMBL; U87568; AAD00635.1; -; mRNA.
DR EMBL; U87569; AAD00636.1; -; mRNA.
DR EMBL; U87570; AAD00637.1; -; mRNA.
DR EMBL; U87571; AAD00638.1; -; mRNA.
DR EMBL; U87572; AAD00639.1; -; mRNA.
DR EMBL; U87573; AAD00640.1; -; mRNA.
DR EMBL; U87574; AAD00641.1; -; mRNA.
DR EMBL; U87575; AAD00642.1; -; mRNA.
DR EMBL; U87576; AAD00643.1; -; mRNA.
DR EMBL; U87577; AAD00644.1; -; mRNA.
DR EMBL; X17653; CAA35644.1; -; mRNA.
DR EMBL; X17653; CAA35645.1; ALT_INIT; mRNA.
DR EMBL; M31933; AAA35841.1; -; mRNA.
DR EMBL; M31934; AAA35842.1; -; mRNA.
DR EMBL; M31935; AAA35843.1; -; mRNA.
DR EMBL; X52473; CAA36713.1; -; mRNA.
DR EMBL; CR407635; CAG28563.1; -; mRNA.
DR EMBL; AL359541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031992; AAH31992.1; -; mRNA.
DR EMBL; BC146678; AAI46679.1; -; mRNA.
DR EMBL; AB050934; BAB92093.1; -; mRNA.
DR CCDS; CCDS30924.1; -. [P31994-1]
DR CCDS; CCDS30925.1; -. [P31994-2]
DR CCDS; CCDS53414.1; -. [P31994-3]
DR PIR; JL0119; JL0119.
DR RefSeq; NP_001002273.1; NM_001002273.2. [P31994-5]
DR RefSeq; NP_001002274.1; NM_001002274.2. [P31994-2]
DR RefSeq; NP_001002275.1; NM_001002275.2. [P31994-4]
DR RefSeq; NP_001177757.1; NM_001190828.1. [P31994-3]
DR RefSeq; NP_003992.3; NM_004001.4. [P31994-1]
DR RefSeq; XP_016856160.1; XM_017000671.1.
DR RefSeq; XP_016856161.1; XM_017000672.1.
DR PDB; 2FCB; X-ray; 1.74 A; A=46-217.
DR PDB; 3WJJ; X-ray; 2.60 A; C=45-217.
DR PDB; 5OCC; X-ray; 2.50 A; A=43-218.
DR PDBsum; 2FCB; -.
DR PDBsum; 3WJJ; -.
DR PDBsum; 5OCC; -.
DR AlphaFoldDB; P31994; -.
DR SMR; P31994; -.
DR BioGRID; 108507; 16.
DR DIP; DIP-36638N; -.
DR ELM; P31994; -.
DR IntAct; P31994; 19.
DR MINT; P31994; -.
DR STRING; 9606.ENSP00000351497; -.
DR ChEMBL; CHEMBL4662940; -.
DR DrugBank; DB00054; Abciximab.
DR DrugBank; DB00087; Alemtuzumab.
DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR DrugBank; DB00112; Bevacizumab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00028; Human immunoglobulin G.
DR DrugBank; DB00110; Palivizumab.
DR DrugBank; DB11767; Sarilumab.
DR DrugBank; DB00081; Tositumomab.
DR MEROPS; I43.001; -.
DR GlyGen; P31994; 4 sites.
DR iPTMnet; P31994; -.
DR PhosphoSitePlus; P31994; -.
DR BioMuta; FCGR2B; -.
DR DMDM; 8039788; -.
DR CPTAC; CPTAC-1183; -.
DR jPOST; P31994; -.
DR MassIVE; P31994; -.
DR MaxQB; P31994; -.
DR PaxDb; P31994; -.
DR PeptideAtlas; P31994; -.
DR PRIDE; P31994; -.
DR ProteomicsDB; 54822; -. [P31994-1]
DR ProteomicsDB; 54823; -. [P31994-2]
DR ProteomicsDB; 54824; -. [P31994-3]
DR ABCD; P31994; 7 sequenced antibodies.
DR Antibodypedia; 3585; 1000 antibodies from 41 providers.
DR DNASU; 2213; -.
DR Ensembl; ENST00000236937.13; ENSP00000236937.9; ENSG00000072694.22. [P31994-2]
DR Ensembl; ENST00000358671.10; ENSP00000351497.5; ENSG00000072694.22. [P31994-1]
DR Ensembl; ENST00000367961.8; ENSP00000356938.4; ENSG00000072694.22. [P31994-3]
DR GeneID; 2213; -.
DR KEGG; hsa:2213; -.
DR MANE-Select; ENST00000358671.10; ENSP00000351497.5; NM_001394477.1; NP_001381406.1.
DR UCSC; uc001gaz.3; human. [P31994-1]
DR CTD; 2213; -.
DR DisGeNET; 2213; -.
DR GeneCards; FCGR2B; -.
DR HGNC; HGNC:3618; FCGR2B.
DR HPA; ENSG00000072694; Tissue enriched (placenta).
DR MalaCards; FCGR2B; -.
DR MIM; 152700; phenotype.
DR MIM; 604590; gene.
DR MIM; 611162; phenotype.
DR neXtProt; NX_P31994; -.
DR OpenTargets; ENSG00000072694; -.
DR Orphanet; 536; Systemic lupus erythematosus.
DR PharmGKB; PA28064; -.
DR VEuPathDB; HostDB:ENSG00000072694; -.
DR eggNOG; ENOG502SVEW; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_1_2_1; -.
DR InParanoid; P31994; -.
DR OMA; DLEPPWI; -.
DR OrthoDB; 1246375at2759; -.
DR PhylomeDB; P31994; -.
DR TreeFam; TF335097; -.
DR PathwayCommons; P31994; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P31994; -.
DR SIGNOR; P31994; -.
DR BioGRID-ORCS; 2213; 13 hits in 1062 CRISPR screens.
DR ChiTaRS; FCGR2B; human.
DR EvolutionaryTrace; P31994; -.
DR GeneWiki; FCGR2B; -.
DR GenomeRNAi; 2213; -.
DR Pharos; P31994; Tbio.
DR PRO; PR:P31994; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P31994; protein.
DR Bgee; ENSG00000072694; Expressed in placenta and 148 other tissues.
DR Genevisible; P31994; HS.
DR GO; GO:0044297; C:cell body; ISS:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0019864; F:IgG binding; IDA:ARUK-UCL.
DR GO; GO:0019772; F:low-affinity IgG receptor activity; IDA:ARUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:ARUK-UCL.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISS:ARUK-UCL.
DR GO; GO:0021549; P:cerebellum development; ISS:BHF-UCL.
DR GO; GO:0006952; P:defense response; ISS:ARUK-UCL.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; IDA:ARUK-UCL.
DR GO; GO:0002316; P:follicular B cell differentiation; TAS:ARUK-UCL.
DR GO; GO:0002266; P:follicular dendritic cell activation; TAS:ARUK-UCL.
DR GO; GO:0002436; P:immune complex clearance by monocytes and macrophages; TAS:ARUK-UCL.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISS:ARUK-UCL.
DR GO; GO:0006954; P:inflammatory response; TAS:ARUK-UCL.
DR GO; GO:0002313; P:mature B cell differentiation involved in immune response; TAS:ARUK-UCL.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; ISS:ARUK-UCL.
DR GO; GO:0001814; P:negative regulation of antibody-dependent cellular cytotoxicity; TAS:ARUK-UCL.
DR GO; GO:0050869; P:negative regulation of B cell activation; TAS:ARUK-UCL.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISS:ARUK-UCL.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0001818; P:negative regulation of cytokine production; TAS:ARUK-UCL.
DR GO; GO:0043318; P:negative regulation of cytotoxic T cell degranulation; TAS:ARUK-UCL.
DR GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; TAS:ARUK-UCL.
DR GO; GO:2001199; P:negative regulation of dendritic cell differentiation; TAS:ARUK-UCL.
DR GO; GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; ISS:ARUK-UCL.
DR GO; GO:0050777; P:negative regulation of immune response; ISS:ARUK-UCL.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; ISS:ARUK-UCL.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISS:ARUK-UCL.
DR GO; GO:0043031; P:negative regulation of macrophage activation; TAS:ARUK-UCL.
DR GO; GO:1902564; P:negative regulation of neutrophil activation; TAS:ARUK-UCL.
DR GO; GO:0050765; P:negative regulation of phagocytosis; TAS:ARUK-UCL.
DR GO; GO:0001811; P:negative regulation of type I hypersensitivity; ISS:ARUK-UCL.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
DR GO; GO:0002922; P:positive regulation of humoral immune response; TAS:ARUK-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:BHF-UCL.
DR GO; GO:1901216; P:positive regulation of neuron death; ISS:BHF-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:ARUK-UCL.
DR GO; GO:1905898; P:positive regulation of response to endoplasmic reticulum stress; ISS:ARUK-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:ARUK-UCL.
DR GO; GO:0002819; P:regulation of adaptive immune response; TAS:ARUK-UCL.
DR GO; GO:0002622; P:regulation of B cell antigen processing and presentation; TAS:ARUK-UCL.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; IGI:ARUK-UCL.
DR GO; GO:0090264; P:regulation of immune complex clearance by monocytes and macrophages; TAS:ARUK-UCL.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0045088; P:regulation of innate immune response; TAS:ARUK-UCL.
DR GO; GO:0010469; P:regulation of signaling receptor activity; TAS:ARUK-UCL.
DR GO; GO:0009617; P:response to bacterium; ISS:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Chromosomal rearrangement; Disulfide bond; Glycoprotein;
KW Host-virus interaction; IgG-binding protein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Proto-oncogene; Receptor; Reference proteome;
KW Repeat; Signal; Systemic lupus erythematosus; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..310
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT II-b"
FT /id="PRO_0000015147"
FT TOPO_DOM 43..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..127
FT /note="Ig-like C2-type 1"
FT DOMAIN 131..213
FT /note="Ig-like C2-type 2"
FT MOTIF 290..295
FT /note="ITIM motif"
FT MOD_RES 292
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:8756631"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:10064577"
FT DISULFID 152..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:10064577"
FT VAR_SEQ 39..45
FT /note="Missing (in isoform IIB3)"
FT /evidence="ECO:0000303|PubMed:2529342"
FT /id="VSP_002642"
FT VAR_SEQ 46
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_058635"
FT VAR_SEQ 254..272
FT /note="Missing (in isoform IIB2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2142460, ECO:0000303|PubMed:2529342,
FT ECO:0000303|PubMed:2531080, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.5"
FT /id="VSP_002643"
FT VARIANT 83
FT /note="Q -> P (in dbSNP:rs5017567)"
FT /id="VAR_059430"
FT VARIANT 205
FT /note="Y -> F (in dbSNP:rs1050499)"
FT /evidence="ECO:0000269|PubMed:2529342"
FT /id="VAR_027045"
FT VARIANT 232
FT /note="I -> T (associated with susceptibility to SLE;
FT associated with resistance to malaria; found at an
FT increased frequency in African and Asian populations from
FT areas where malaria is endemic; enhances phagocytosis of
FT Plasmodium falciparum-infected erythrocytes in vitro;
FT dbSNP:rs1050501)"
FT /evidence="ECO:0000269|PubMed:12115230,
FT ECO:0000269|PubMed:17435165, ECO:0000269|PubMed:20385827,
FT ECO:0000269|Ref.1"
FT /id="VAR_015515"
FT VARIANT 258
FT /note="Y -> D (in dbSNP:rs148534844)"
FT /evidence="ECO:0000269|PubMed:8466861"
FT /id="VAR_008798"
FT CONFLICT 178
FT /note="D -> I (in Ref. 2; CAA35644/CAA35645)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="T -> I (in Ref. 2; CAA35644/CAA35645)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="V -> G (in Ref. 2; CAA35644/CAA35645)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="P -> S (in Ref. 2; CAA35644/CAA35645)"
FT /evidence="ECO:0000305"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2FCB"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5OCC"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:2FCB"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2FCB"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2FCB"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2FCB"
SQ SEQUENCE 310 AA; 34044 MW; 2186F8538FF01F36 CRC64;
MGILSFLPVL ATESDWADCK SPQPWGHMLL WTAVLFLAPV AGTPAAPPKA VLKLEPQWIN
VLQEDSVTLT CRGTHSPESD SIQWFHNGNL IPTHTQPSYR FKANNNDSGE YTCQTGQTSL
SDPVHLTVLS EWLVLQTPHL EFQEGETIVL RCHSWKDKPL VKVTFFQNGK SKKFSRSDPN
FSIPQANHSH SGDYHCTGNI GYTLYSSKPV TITVQAPSSS PMGIIVAVVT GIAVAAIVAA
VVALIYCRKK RISALPGYPE CREMGETLPE KPANPTNPDE ADKVGAENTI TYSLLMHPDA
LEEPDDQNRI
