FCG3B_HUMAN
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 03-AUG-2022, entry version 196.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-B;
DE AltName: Full=Fc-gamma RIII-beta;
DE Short=CD16-I {ECO:0000303|PubMed:1825220};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 killer
RT cells and neutrophils. Cell type-specific expression of two genes that
RT 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-linked
RT membrane protein.";
RL Nature 333:568-570(1988).
RN [3]
RP ERRATUM OF PUBMED:2967436.
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 and
RT 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., 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 [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 genes.
RT Molecular characterization of the promoter regions.";
RL J. Biol. Chem. 270:1350-1361(1995).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-203.
RX PubMed=1825220;
RA Lanier L.L., Yu G., Phillips J.H.;
RT "Analysis of Fc gamma RIII (CD16) membrane expression and association with
RT CD3 zeta and Fc epsilon RI-gamma by site-directed mutation.";
RL J. Immunol. 146:1571-1576(1991).
RN [10]
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 gammaRIII
RT complex.";
RL Nature 406:267-273(2000).
RN [11]
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 RIII.";
RL Immunity 13:387-395(2000).
RN [12]
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 monomeric
CC IgG. Contrary to III-A, is not capable to mediate antibody-dependent
CC cytotoxicity and phagocytosis. May serve as a trap for immune complexes
CC in the peripheral circulation which does not activate neutrophils.
CC -!- SUBUNIT: Monomer. Interacts with INPP5D/SHIP1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1825220};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1825220}. Secreted.
CC Note=Secreted after cleavage.
CC -!- TISSUE SPECIFICITY: Expressed specifically by polymorphonuclear
CC leukocytes (neutrophils). Also expressed by stimulated 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 (NA-
CC 1), FCGR3B*02 (HNA-1b, NA-2) (shown here) and SH. FCGR3B*01 and
CC FCGR3B*02 are detectable with antibodies against the biallelic
CC neutrophil-specific antigen system NA. The more active FCGR3B*01 allele
CC has been associated with severe renal disease in certain systemic
CC vasculitides. {ECO:0000269|PubMed:15245367, ECO:0000269|PubMed:2521732,
CC ECO:0000269|PubMed:2526846, ECO:0000269|PubMed:2967436,
CC ECO:0000269|PubMed:7836402, ECO:0000269|PubMed:9028335}.
CC -!- MISCELLANEOUS: Encoded by one of two nearly indentical genes: FCGR3A
CC and FCGR3B (Shown here) which are expressed in a tissue-specific
CC manner. The 'Phe-203' in FCGR3A determines the transmembrane domains
CC whereas the Ser-203 in FCGR3B determines the GPI-anchoring.
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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 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 AlphaFoldDB; O75015; -.
DR SMR; O75015; -.
DR BioGRID; 108509; 49.
DR IntAct; O75015; 1.
DR STRING; 9606.ENSP00000433642; -.
DR BindingDB; O75015; -.
DR ChEMBL; CHEMBL5842; -.
DR DrugBank; DB00092; Alefacept.
DR DrugBank; DB00087; Alemtuzumab.
DR DrugBank; DB06607; Catumaxomab.
DR DrugBank; DB00002; Cetuximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00056; Gemtuzumab ozogamicin.
DR DrugBank; DB00028; Human immunoglobulin G.
DR DrugBank; DB00075; Muromonab.
DR DrugBank; DB00108; Natalizumab.
DR DrugBank; DB00110; Palivizumab.
DR DrugBank; DB11767; Sarilumab.
DR TCDB; 8.A.23.2.7; the basigin (basigin) family.
DR GlyConnect; 1463; 2 N-Linked glycans (1 site).
DR GlyGen; O75015; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; O75015; -.
DR PhosphoSitePlus; O75015; -.
DR BioMuta; FCGR3B; -.
DR jPOST; O75015; -.
DR MassIVE; O75015; -.
DR PaxDb; O75015; -.
DR PeptideAtlas; O75015; -.
DR PRIDE; O75015; -.
DR ProteomicsDB; 49693; -.
DR ABCD; O75015; 13 sequenced antibodies.
DR Antibodypedia; 10871; 704 antibodies from 26 providers.
DR DNASU; 2215; -.
DR Ensembl; ENST00000367964.6; ENSP00000356941.2; ENSG00000162747.12.
DR GeneID; 2215; -.
DR KEGG; hsa:2215; -.
DR UCSC; uc021pdo.2; human.
DR CTD; 2215; -.
DR DisGeNET; 2215; -.
DR GeneCards; FCGR3B; -.
DR HGNC; HGNC:3620; FCGR3B.
DR HPA; ENSG00000162747; Tissue enhanced (bone marrow, lymphoid tissue).
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 VEuPathDB; HostDB:ENSG00000162747; -.
DR eggNOG; ENOG502RU1M; Eukaryota.
DR HOGENOM; CLU_023383_1_0_1; -.
DR InParanoid; O75015; -.
DR OrthoDB; 866496at2759; -.
DR PhylomeDB; O75015; -.
DR TreeFam; TF335097; -.
DR PathwayCommons; O75015; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O75015; -.
DR SIGNOR; O75015; -.
DR BioGRID-ORCS; 2215; 8 hits in 995 CRISPR screens.
DR EvolutionaryTrace; O75015; -.
DR GeneWiki; FCGR3B; -.
DR GenomeRNAi; 2215; -.
DR Pharos; O75015; Tbio.
DR PRO; PR:O75015; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75015; protein.
DR Bgee; ENSG00000162747; Expressed in blood and 146 other tissues.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0034235; F:GPI anchor binding; IDA:UniProtKB.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
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; Disulfide bond; Glycoprotein; GPI-anchor;
KW IgG-binding protein; Immunoglobulin domain; Lipoprotein; Membrane;
KW Receptor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..200
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-B"
FT /id="PRO_0000015151"
FT PROPEP 201..233
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015152"
FT DOMAIN 40..96
FT /note="Ig-like C2-type 1"
FT DOMAIN 121..179
FT /note="Ig-like C2-type 2"
FT LIPID 200
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
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 47..89
FT /evidence="ECO:0000269|PubMed:10917521,
FT ECO:0000269|PubMed:11021536, ECO:0007744|PDB:1FNL"
FT DISULFID 128..172
FT /evidence="ECO:0000269|PubMed:10917521,
FT ECO:0000269|PubMed:11021536, ECO:0007744|PDB:1FNL"
FT VARIANT 36
FT /note="S -> R (in allele FCGR3B*01; dbSNP:rs200688856)"
FT /id="VAR_003956"
FT VARIANT 65
FT /note="S -> N (in allele FCGR3B*01; dbSNP:rs448740)"
FT /evidence="ECO:0000269|PubMed:16710414"
FT /id="VAR_003963"
FT VARIANT 78
FT /note="A -> D (in allele SH; dbSNP:rs5030738)"
FT /evidence="ECO:0000269|PubMed:9028335"
FT /id="VAR_008802"
FT VARIANT 82
FT /note="N -> D (in allele FCGR3B*01; dbSNP:rs147574249)"
FT /id="VAR_003957"
FT VARIANT 106
FT /note="I -> V (in allele FCGR3B*01; dbSNP:rs2290834)"
FT /id="VAR_003964"
FT MUTAGEN 203
FT /note="S->P: Abolishes membrane anchoring via
FT glycosylphosphatidylinositol."
FT /evidence="ECO:0000269|PubMed:1825220"
FT MUTAGEN 203
FT /note="S->T,Y,A,D,K: Has no effect on membrane anchoring
FT via glycosylphosphatidylinositol."
FT /evidence="ECO:0000269|PubMed:1825220"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1FNL"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1T89"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1FNL"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6EAQ"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1FNL"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1FNL"
FT STRAND 186..191
FT /evidence="ECO:0007829|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
