ID FCG3B_HUMAN Reviewed; 233 AA. AC O75015; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 2. DT 13-FEB-2019, entry version 178. DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-B; DE AltName: Full=Fc-gamma RIII-beta; DE Short=Fc-gamma RIII; DE Short=Fc-gamma RIIIb; DE Short=FcRIII; DE Short=FcRIIIb; DE AltName: Full=FcR-10; DE AltName: Full=IgG Fc receptor III-1; DE AltName: CD_antigen=CD16b; DE Flags: Precursor; GN Name=FCGR3B; Synonyms=CD16B, FCG3, FCGR3, IGFR3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE FCGR3B*02), AND POLYMORPHISM. RX PubMed=2526846; DOI=10.1084/jem.170.2.481; RA Ravetch J.V., Perussia B.; RT "Alternative membrane forms of Fc gamma RIII(CD16) on human natural RT killer cells and neutrophils. Cell type-specific expression of two RT genes that differ in single nucleotide substitutions."; RL J. Exp. Med. 170:481-497(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE FCGR3B*02), AND POLYMORPHISM. RC TISSUE=Placenta; RX PubMed=2967436; DOI=10.1038/333568a0; RA Simmons D., Seed B.; RT "The Fc gamma receptor of natural killer cells is a phospholipid- RT linked membrane protein."; RL Nature 333:568-570(1988). RN [3] RP ERRATUM. RA Simmons D., Seed B.; RL Nature 340:662-662(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE FCGR3B*01), AND POLYMORPHISM. RC TISSUE=Leukocyte; RX PubMed=2521732; DOI=10.1073/pnas.86.3.1013; RA Peltz G.A., Grundy H.O., Lebo R.V., Yssel H., Barsh G.S., Moore K.W.; RT "Human Fc-gamma-RIII: cloning, expression, and identification of the RT chromosomal locus of two Fc receptors for IgG."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1013-1017(1989). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2525780; DOI=10.1073/pnas.86.13.5079; RA Scallon B.J., Scigliano E., Freedman V.H., Miedel M.C., Pan Y.C., RA Unkeless J.C., Kochan J.P.; RT "A human immunoglobulin G receptor exists in both polypeptide-anchored RT and phosphatidylinositol-glycan-anchored forms."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5079-5083(1989). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE FCGR3B*02), AND POLYMORPHISM. RC TISSUE=Peripheral blood; RX PubMed=15245367; DOI=10.1111/j.1399-0039.2004.00259.x; RA Bertrand G., Duprat E., Lefranc M.-P., Marti J., Coste J.; RT "Characterization of human FCGR3B*02 (HNA-1b, NA2) cDNAs and IMGT RT standardized description of FCGR3B alleles."; RL Tissue Antigens 64:119-131(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-65. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 (ALLELE FCGR3B*02), AND RP POLYMORPHISM. RC TISSUE=Placenta; RX PubMed=7836402; DOI=10.1074/jbc.270.3.1350; RA Gessner J.E., Grussenmeyer T., Kolanus W., Schmidt R.E.; RT "The human low affinity immunoglobulin G Fc receptor III-A and III-B RT genes. Molecular characterization of the promoter regions."; RL J. Biol. Chem. 270:1350-1361(1995). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH IGG1 FC, AND RP DISULFIDE BOND. RX PubMed=10917521; DOI=10.1038/35018508; RA Sondermann P., Huber R., Oosthuizen V., Jacob U.; RT "The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc RT gammaRIII complex."; RL Nature 406:267-273(2000). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 19-192, AND DISULFIDE BONDS. RX PubMed=11021536; DOI=10.1016/S1074-7613(00)00038-8; RA Zhang Y., Boesen C.C., Radaev S., Brooks A.G., Fridman W.H., RA Sautes-Fridman C., Sun P.D.; RT "Crystal structure of the extracellular domain of a human Fc gamma RT RIII."; RL Immunity 13:387-395(2000). RN [11] RP POLYMORPHISM, AND VARIANT SH ASP-78. RX PubMed=9028335; RA Bux J., Stein E.L., Bierling P., Fromont P., Clay M., Stroncek D., RA Santoso S.; RT "Characterization of a new alloantigen (SH) on the human neutrophil Fc RT gamma receptor IIIb."; RL Blood 89:1027-1034(1997). CC -!- FUNCTION: Receptor for the Fc region of immunoglobulins gamma. Low CC affinity receptor. Binds complexed or aggregated IgG and also CC monomeric IgG. Contrary to III-A, is not capable to mediate CC antibody-dependent cytotoxicity and phagocytosis. May serve as a CC trap for immune complexes in the peripheral circulation which does CC not activate neutrophils. CC -!- SUBUNIT: Monomer. Interacts with INPP5D/SHIP1 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. CC Secreted. Note=Secreted after cleavage. CC -!- TISSUE SPECIFICITY: Expressed specifically by polymorphonuclear CC leukocytes (neutrophils). Also expressed by stimulated CC eosinophils. CC -!- PTM: Glycosylated. Glycosylation plays an inhibitory role in the CC interaction with IgG3. CC -!- PTM: The soluble form is produced by a proteolytic cleavage. CC -!- POLYMORPHISM: There are three allelic forms of FCGR3B: FCGR3B*01 CC (NA-1), FCGR3B*02 (HNA-1b, NA-2) (shown here) and SH. FCGR3B*01 CC and FCGR3B*02 are detectable with antibodies against the biallelic CC neutrophil-specific antigen system NA. The more active FCGR3B*01 CC allele has been associated with severe renal disease in certain CC systemic vasculitides. {ECO:0000269|PubMed:15245367, CC ECO:0000269|PubMed:2521732, ECO:0000269|PubMed:2526846, CC ECO:0000269|PubMed:2967436, ECO:0000269|PubMed:7836402, CC ECO:0000269|PubMed:9028335}. CC -!- MISCELLANEOUS: Encoded by one of two nearly indentical genes: CC FCGR3A and FCGR3B (Shown here) which are expressed in a tissue- CC specific manner. The 'Phe-203' in FCGR3A determines the CC transmembrane domains whereas the Ser-203 in FCGR3B determines the CC GPI-anchoring. 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; X16863; CAA34753.1; -; mRNA. DR EMBL; X07934; CAA30758.1; -; mRNA. DR EMBL; J04162; AAA35881.1; -; mRNA. DR EMBL; M24854; AAA53507.1; -; mRNA. DR EMBL; AJ581669; CAE46408.1; -; mRNA. DR EMBL; AL451067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z46223; CAA86296.1; -; Genomic_DNA. DR CCDS; CCDS41433.1; -. DR CCDS; CCDS58040.1; -. DR PIR; JU0284; JU0284. DR RefSeq; NP_000561.3; NM_000570.4. DR RefSeq; NP_001231682.1; NM_001244753.1. DR RefSeq; NP_001257964.1; NM_001271035.1. DR RefSeq; NP_001257965.1; NM_001271036.1. DR RefSeq; NP_001257966.1; NM_001271037.1. DR UniGene; Hs.372679; -. DR UniGene; Hs.694258; -. DR UniGene; Hs.736230; -. DR PDB; 1E4J; X-ray; 2.50 A; A=18-193. DR PDB; 1E4K; X-ray; 3.20 A; C=18-193. DR PDB; 1FNL; X-ray; 1.80 A; A=19-192. DR PDB; 1T83; X-ray; 3.00 A; C=19-194. DR PDB; 1T89; X-ray; 3.50 A; C=19-194. DR PDB; 6EAQ; X-ray; 2.22 A; C=19-193. DR PDBsum; 1E4J; -. DR PDBsum; 1E4K; -. DR PDBsum; 1FNL; -. DR PDBsum; 1T83; -. DR PDBsum; 1T89; -. DR PDBsum; 6EAQ; -. DR ProteinModelPortal; O75015; -. DR SMR; O75015; -. DR BioGrid; 108509; 22. DR IntAct; O75015; 2. DR STRING; 9606.ENSP00000294800; -. DR BindingDB; O75015; -. DR ChEMBL; CHEMBL5842; -. DR DrugBank; DB00054; Abciximab. DR DrugBank; DB00051; Adalimumab. DR DrugBank; DB00092; Alefacept. DR DrugBank; DB00087; Alemtuzumab. DR DrugBank; DB00074; Basiliximab. DR DrugBank; DB00112; Bevacizumab. DR DrugBank; DB00002; Cetuximab. DR DrugBank; DB00111; Daclizumab. DR DrugBank; DB00095; Efalizumab. DR DrugBank; DB00005; Etanercept. DR DrugBank; DB00056; Gemtuzumab ozogamicin. DR DrugBank; DB00078; Ibritumomab tiuxetan. DR DrugBank; DB00028; Immune Globulin Human. DR DrugBank; DB00075; Muromonab. DR DrugBank; DB00108; Natalizumab. DR DrugBank; DB00110; Palivizumab. DR DrugBank; DB00073; Rituximab. DR DrugBank; DB00081; Tositumomab. DR DrugBank; DB00072; Trastuzumab. DR GlyConnect; 1463; -. DR iPTMnet; O75015; -. DR PhosphoSitePlus; O75015; -. DR BioMuta; FCGR3B; -. DR jPOST; O75015; -. DR PaxDb; O75015; -. DR PeptideAtlas; O75015; -. DR PRIDE; O75015; -. DR ProteomicsDB; 49693; -. DR Ensembl; ENST00000294800; ENSP00000294800; ENSG00000162747. DR Ensembl; ENST00000367964; ENSP00000356941; ENSG00000162747. DR GeneID; 2215; -. DR KEGG; hsa:2215; -. DR UCSC; uc021pdo.2; human. DR CTD; 2215; -. DR DisGeNET; 2215; -. DR EuPathDB; HostDB:ENSG00000162747.9; -. DR GeneCards; FCGR3B; -. DR H-InvDB; HIX0056770; -. DR HGNC; HGNC:3620; FCGR3B. DR MalaCards; FCGR3B; -. DR MIM; 610665; gene. DR neXtProt; NX_O75015; -. DR Orphanet; 464370; Neonatal alloimmune neutropenia. DR Orphanet; 536; Systemic lupus erythematosus. DR PharmGKB; PA28066; -. DR eggNOG; ENOG410IKYD; Eukaryota. DR eggNOG; ENOG41114N1; LUCA. DR HOGENOM; HOG000251632; -. DR HOVERGEN; HBG051602; -. DR InParanoid; O75015; -. DR KO; K06463; -. DR OrthoDB; 866496at2759; -. DR PhylomeDB; O75015; -. DR TreeFam; TF335097; -. DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR EvolutionaryTrace; O75015; -. DR GeneWiki; FCGR3B; -. DR GenomeRNAi; 2215; -. DR PRO; PR:O75015; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000162747; Expressed in 169 organ(s), highest expression level in blood. DR ExpressionAtlas; O75015; baseline and differential. DR Genevisible; O75015; HS. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. 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 Pfam; PF13895; Ig_2; 2. DR SMART; SM00409; IG; 2. DR SUPFAM; SSF48726; SSF48726; 2. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Glycoprotein; GPI-anchor; IgG-binding protein; Immunoglobulin domain; KW Lipoprotein; Membrane; Polymorphism; Receptor; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1 16 {ECO:0000255}. FT CHAIN 17 200 Low affinity immunoglobulin gamma Fc FT region receptor III-B. FT /FTId=PRO_0000015151. FT PROPEP 201 233 Removed in mature form. {ECO:0000255}. FT /FTId=PRO_0000015152. FT DOMAIN 40 96 Ig-like C2-type 1. FT DOMAIN 121 179 Ig-like C2-type 2. FT LIPID 200 200 GPI-anchor amidated serine. FT {ECO:0000255}. FT CARBOHYD 56 56 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 63 63 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 82 82 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 92 92 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 180 180 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 187 187 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 47 89 {ECO:0000244|PDB:1FNL, FT ECO:0000269|PubMed:10917521, FT ECO:0000269|PubMed:11021536}. FT DISULFID 128 172 {ECO:0000244|PDB:1FNL, FT ECO:0000269|PubMed:10917521, FT ECO:0000269|PubMed:11021536}. FT VARIANT 36 36 S -> R (in allele FCGR3B*01). FT /FTId=VAR_003956. FT VARIANT 65 65 S -> N (in allele FCGR3B*01; FT dbSNP:rs448740). FT {ECO:0000269|PubMed:16710414}. FT /FTId=VAR_003963. FT VARIANT 78 78 A -> D (in allele SH; dbSNP:rs5030738). FT {ECO:0000269|PubMed:9028335}. FT /FTId=VAR_008802. FT VARIANT 82 82 N -> D (in allele FCGR3B*01). FT /FTId=VAR_003957. FT VARIANT 106 106 I -> V (in allele FCGR3B*01). FT /FTId=VAR_003964. FT STRAND 27 32 {ECO:0000244|PDB:1FNL}. FT STRAND 35 38 {ECO:0000244|PDB:1FNL}. FT STRAND 43 48 {ECO:0000244|PDB:1FNL}. FT STRAND 59 62 {ECO:0000244|PDB:1FNL}. FT STRAND 65 70 {ECO:0000244|PDB:1FNL}. FT STRAND 72 78 {ECO:0000244|PDB:1FNL}. FT HELIX 81 83 {ECO:0000244|PDB:1FNL}. FT STRAND 85 90 {ECO:0000244|PDB:1FNL}. FT STRAND 92 94 {ECO:0000244|PDB:1FNL}. FT STRAND 100 105 {ECO:0000244|PDB:1FNL}. FT STRAND 107 112 {ECO:0000244|PDB:1FNL}. FT STRAND 116 119 {ECO:0000244|PDB:1FNL}. FT STRAND 120 122 {ECO:0000244|PDB:1T89}. FT STRAND 124 130 {ECO:0000244|PDB:1FNL}. FT HELIX 131 133 {ECO:0000244|PDB:6EAQ}. FT STRAND 137 143 {ECO:0000244|PDB:1FNL}. FT STRAND 146 153 {ECO:0000244|PDB:1FNL}. FT STRAND 157 161 {ECO:0000244|PDB:1FNL}. FT HELIX 164 166 {ECO:0000244|PDB:1FNL}. FT STRAND 168 176 {ECO:0000244|PDB:1FNL}. FT STRAND 179 182 {ECO:0000244|PDB:1FNL}. FT STRAND 186 191 {ECO:0000244|PDB:1FNL}. SQ SEQUENCE 233 AA; 26216 MW; 7AB5159432761726 CRC64; MWQLLLPTAL LLLVSAGMRT EDLPKAVVFL EPQWYSVLEK DSVTLKCQGA YSPEDNSTQW FHNESLISSQ ASSYFIDAAT VNDSGEYRCQ TNLSTLSDPV QLEVHIGWLL LQAPRWVFKE EDPIHLRCHS WKNTALHKVT YLQNGKDRKY FHHNSDFHIP KATLKDSGSY FCRGLVGSKN VSSETVNITI TQGLAVSTIS SFSPPGYQVS FCLVMVLLFA VDTGLYFSVK TNI //