Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O75015 (FCG3B_HUMAN)

Last modified July 22, 2008. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Low affinity immunoglobulin gamma Fc region receptor III-B
Alternative name(s):
    IgG Fc receptor III-1
    Fc-gamma RIII-beta
      Short name=Fc-gamma RIIIb
      Short name=FcRIIIb
      Short name=Fc-gamma RIII
      Short name=FcRIII
    FcR-10
    CD_antigen=CD16b
Gene names
Name: FCGR3B
Synonyms: CD16B, FCG3, FCGR3, IGFR3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils.

Subunit structure

Monomer. Interacts with INPP5D/SHIP1 By similarity.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor. Secreted. Note= Secreted after cleavage.

Tissue specificity

Expressed specifically by polymorphonuclear leukocytes (neutrophils). Also expressed by stimulated eosinophils.

Post-translational modification

Glycosylated. Glycosylation plays an inhibitory role in the interaction with IgG3.

The soluble form is produced by a proteolytic cleavage.

Polymorphism

There are three allelic forms of FCGR3B: FCGR3B*01 (NA-1), FCGR3B*02 (HNA-1b, NA-2) (shown here) and SH. FCGR3B*01 and FCGR3B*02 are detectable with antibodies against the biallelic neutrophil-specific antigen system NA.

Involvement in disease

The more active FCGR3B*01 allele has been associated with severe renal disease in certain systemic vasculitides.

Miscellaneous

Encoded by one of two nearly indentical genes: FCGR3A and FCGR3B (Shown here) which are expressed in a tissue-specific manner. The Phe-203 in FCGR3A determines the transmembrane domains whereas the Ser-203 in FCGR3B determines the GPI-anchoring.

Sequence similarities

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Hide | Top

Ontologies

Keywords

   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
   LigandIgG-binding protein
   Molecular functionReceptor
   PTMGPI-anchor
Glycoprotein
Lipoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processimmune response

Traceable author statement. Source: ProtInc

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 200184Low affinity immunoglobulin gamma Fc region receptor III-B
Propeptide201 – 23333Removed in mature form Potential

Regions

Domain40 – 9657Ig-like C2-type 1
Domain121 – 17959Ig-like C2-type 2

Amino acid modifications

Lipidation2001GPI-anchor amidated serine Potential
Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 89
Disulfide bond128 ↔ 172

Natural variations

Natural variant361S → R in allele FCGR3B*01.
Natural variant651S → N in allele FCGR3B*01. dbSNP rs448740.
Natural variant781A → D in allele SH.
Natural variant821N → D in allele FCGR3B*01.
Natural variant1061I → V in allele FCGR3B*01.

Secondary structure

1 ......................................... 233
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
O75015-1 [UniParc].

Last modified November 1, 1999. Version 2.
Checksum: 7AB5159432761726

FASTA23326,216
        10         20         30         40         50         60 
MWQLLLPTAL LLLVSAGMRT EDLPKAVVFL EPQWYSVLEK DSVTLKCQGA YSPEDNSTQW 

        70         80         90        100        110        120 
FHNESLISSQ ASSYFIDAAT VNDSGEYRCQ TNLSTLSDPV QLEVHIGWLL LQAPRWVFKE 

       130        140        150        160        170        180 
EDPIHLRCHS WKNTALHKVT YLQNGKDRKY FHHNSDFHIP KATLKDSGSY FCRGLVGSKN 

       190        200        210        220        230 
VSSETVNITI TQGLAVSTIS SFSPPGYQVS FCLVMVLLFA VDTGLYFSVK TNI

« Hide

Hide | Top

References

[1]"Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer cells and neutrophils. Cell type-specific expression of two genes that differ in single nucleotide substitutions."
Ravetch J.V., Perussia B.
J. Exp. Med. 170:481-497(1989) [PubMed: 2526846] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ALLELE FCGR3B*02).
[2]"The Fc gamma receptor of natural killer cells is a phospholipid-linked membrane protein."
Simmons D., Seed B.
Nature 333:568-570(1988) [PubMed: 2967436] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE FCGR3B*02).
Tissue: Placenta.
[3]Erratum
Simmons D., Seed B.
Nature 340:662-662(1989)
[4]"Human Fc-gamma-RIII: cloning, expression, and identification of the chromosomal locus of two Fc receptors for IgG."
Peltz G.A., Grundy H.O., Lebo R.V., Yssel H., Barsh G.S., Moore K.W.
Proc. Natl. Acad. Sci. U.S.A. 86:1013-1017(1989) [PubMed: 2521732] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE FCGR3B*01).
Tissue: Leukocyte.
[5]"A human immunoglobulin G receptor exists in both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms."
Scallon B.J., Scigliano E., Freedman V.H., Miedel M.C., Pan Y.C., Unkeless J.C., Kochan J.P.
Proc. Natl. Acad. Sci. U.S.A. 86:5079-5083(1989) [PubMed: 2525780] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Characterization of human FCGR3B*02 (HNA-1b, NA2) cDNAs and IMGT standardized description of FCGR3B alleles."
Bertrand G., Duprat E., Lefranc M.-P., Marti J., Coste J.
Tissue Antigens 64:119-131(2004) [PubMed: 15245367] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ALLELE FCGR3B*02).
Tissue: Peripheral blood.
[7]"The human low affinity immunoglobulin G Fc receptor III-A and III-B genes. Molecular characterization of the promoter regions."
Gessner J.E., Grussenmeyer T., Kolanus W., Schmidt R.E.
J. Biol. Chem. 270:1350-1361(1995) [PubMed: 7836402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 (ALLELE FCGR3B*02).
Tissue: Placenta.
[8]"The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex."
Sondermann P., Huber R., Oosthuizen V., Jacob U.
Nature 406:267-273(2000) [PubMed: 10917521] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH IGG1 FC.
[9]"Crystal structure of the extracellular domain of a human Fc gamma RIII."
Zhang Y., Boesen C.C., Radaev S., Brooks A.G., Fridman W.H., Sautes-Fridman C., Sun P.D.
Immunity 13:387-395(2000) [PubMed: 11021536] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-192.
[10]"Characterization of a new alloantigen (SH) on the human neutrophil Fc gamma receptor IIIb."
Bux J., Stein E.L., Bierling P., Fromont P., Clay M., Stroncek D., Santoso S.
Blood 89:1027-1034(1997) [PubMed: 9028335] [Abstract]
Cited for: VARIANT SH ASP-78.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

X16863 mRNA. Translation: CAA34753.1.
X07934 mRNA. Translation: CAA30758.1.
J04162 mRNA. Translation: AAA35881.1.
M24854 mRNA. Translation: AAA53507.1.
AJ581669 mRNA. Translation: CAE46408.1.
Z46223 Genomic DNA. Translation: CAA86296.1.
PIRJU0284.
RefSeqNP_000561.3.
UniGeneHs.372679

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1E4JX-ray2.50A18-193[»]
1E4KX-ray3.20C18-193[»]
1FNLX-ray1.80A19-192[»]
1T83X-ray3.00C19-194[»]
1T89X-ray3.50C19-194[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSG00000162747. Homo sapiens. [Contig view]
GeneID2215.
KEGGhsa:2215.

Organism-specific databases

H-InvDBHIX0056770.
HGNCHGNC:3620. FCGR3B.
MIM610665. gene.
PharmGKBPA28066.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMO75015.
HOVERGENO75015.

Gene expression databases

ArrayExpressO75015.
CleanExHS_FCGR3B.
GermOnlineENSG00000162747. Homo sapiens.

Family and domain databases

InterProIPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
PfamPF00047. ig. 2 hits.
[Graphical view]
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProDomO75015.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

DrugBankDB00054. Abciximab.
DB00051. Adalimumab.
DB00092. Alefacept.
DB00087. Alemtuzumab.
DB00074. Basiliximab.
DB00112. Bevacizumab.
DB00002. Cetuximab.
DB00111. Daclizumab.
DB00095. Efalizumab.
DB00005. Etanercept.
DB00056. Gemtuzumab ozogamicin.
DB00078. Ibritumomab.
DB00028. Immune globulin.
DB00075. Muromonab.
DB00108. Natalizumab.
DB00110. Palivizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.
LinkHubO75015.
SOURCESearch...
ProtoNetSearch...

Hide | Top

Entry information

Entry nameFCG3B_HUMAN
AccessionPrimary (citable) accession number: O75015
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 22, 2008
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents