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 27-MAR-2024, entry version 238. 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="https://atlasgeneticsoncology.org/gene/397/FCGR2B"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyConnect; 2999; 29 N-Linked glycans. [P31994-3] DR GlyCosmos; P31994; 3 sites, No reported glycans. 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; 9606-ENSP00000351497; -. DR PeptideAtlas; 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; 1165 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 AGR; HGNC:3618; -. 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; ITDGGYM; -. DR OrthoDB; 5261894at2759; -. 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; 14 hits in 1145 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 150 other cell types or tissues. 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: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:0038094; P:Fc-gamma receptor signaling pathway; 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:0002252; P:immune effector process; IDA:ARUK-UCL. 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:0006909; P:phagocytosis; IDA: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:ARUK-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:1903381; P:regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; ISS:BHF-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 CDD; cd05752; Ig1_FcgammaR_like; 1. DR CDD; cd05753; Ig2_FcgammaR_like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR11481; IMMUNOGLOBULIN FC RECEPTOR; 1. DR PANTHER; PTHR11481:SF97; LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR II-A-RELATED; 1. DR Pfam; PF13895; Ig_2; 2. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 2. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR Genevisible; P31994; HS. 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 (risk factor for SLE; confers resistance to FT malaria; found at an increased frequency in African and FT Asian populations from areas where malaria is endemic; FT enhances phagocytosis of Plasmodium falciparum-infected FT erythrocytes in vitro; 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 //