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O75015 (FCG3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low affinity immunoglobulin gamma Fc region receptor III-B
Alternative name(s):
Fc-gamma RIII-beta
Short name=Fc-gamma RIII
Short name=Fc-gamma RIIIb
Short name=FcRIII
Short name=FcRIIIb
FcR-10
IgG Fc receptor III-1
CD_antigen=CD16b
Gene names
Name:FCGR3B
Synonyms:CD16B, FCG3, FCGR3, IGFR3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

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-anchorGPI-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. 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.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
   LigandIgG-binding protein
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processimmune response

Traceable author statement PubMed 2139735. Source: ProtInc

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 200184Low affinity immunoglobulin gamma Fc region receptor III-B
PRO_0000015151
Propeptide201 – 23333Removed in mature form Potential
PRO_0000015152

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.
VAR_003956
Natural variant651S → N in allele FCGR3B*01. Ref.7
Corresponds to variant rs448740 [ dbSNP | Ensembl ].
VAR_003963
Natural variant781A → D in allele SH. Ref.11
Corresponds to variant rs5030738 [ dbSNP | Ensembl ].
VAR_008802
Natural variant821N → D in allele FCGR3B*01.
VAR_003957
Natural variant1061I → V in allele FCGR3B*01.
VAR_003964

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O75015 [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

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE FCGR3B*02).
Tissue: Peripheral blood.
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-65.
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 (ALLELE FCGR3B*02).
Tissue: Placenta.
[9]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH IGG1 FC.
[10]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-192.
[11]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SH ASP-78.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AL451067 Genomic DNA. No translation available.
Z46223 Genomic DNA. Translation: CAA86296.1.
PIRJU0284.
RefSeqNP_000561.3. NM_000570.4.
NP_001231682.1. NM_001244753.1.
NP_001257964.1. NM_001271035.1.
NP_001257965.1. NM_001271036.1.
NP_001257966.1. NM_001271037.1.
UniGeneHs.372679.
Hs.694258.
Hs.736230.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E4JX-ray2.50A18-193[»]
1E4KX-ray3.20C18-193[»]
1FNLX-ray1.80A19-192[»]
1T83X-ray3.00C19-194[»]
1T89X-ray3.50C19-194[»]
ProteinModelPortalO75015.
SMRO75015. Positions 23-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO75015. 1 interaction.
STRING9606.ENSP00000294800.

Chemistry

BindingDBO75015.
ChEMBLCHEMBL5842.
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.

Protein family/group databases

MEROPSI43.001.

Proteomic databases

PaxDbO75015.
PRIDEO75015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294800; ENSP00000294800; ENSG00000162747.
ENST00000367964; ENSP00000356941; ENSG00000162747.
GeneID2215.
KEGGhsa:2215.
UCSCuc021pdo.1. human.

Organism-specific databases

CTD2215.
GeneCardsGC01M161592.
H-InvDBHIX0056770.
HGNCHGNC:3620. FCGR3B.
MIM610665. gene.
neXtProtNX_O75015.
Orphanet855. Hashimoto struma.
536. Systemic lupus erythematosus.
PharmGKBPA28066.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47725.
HOGENOMHOG000251632.
HOVERGENHBG051602.
InParanoidO75015.
KOK06463.
OrthoDBEOG7SXW4Z.
PhylomeDBO75015.
TreeFamTF335097.

Gene expression databases

ArrayExpressO75015.
BgeeO75015.
CleanExHS_FCGR3B.
GenevestigatorO75015.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75015.
GeneWikiFCGR3B.
GenomeRNAi2215.
NextBio8985.
PROO75015.
SOURCESearch...

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: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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

Human cell differentiation molecules

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