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Reviewed, UniProtKB/Swiss-Prot P31994 (FCG2B_HUMAN)

Last modified July 22, 2008. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Low affinity immunoglobulin gamma Fc region receptor II-b
      Short name=IgG Fc receptor II-b
Alternative name(s):
    Fc-gamma RII-b
    Fc-gamma-RIIb
      Short name=FcRII-b
    CDw32
    CD_antigen=CD32
Gene names
Name: FCGR2B
Synonyms: CD32, FCG2, IGFR2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length310 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 complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis.

Subunit structure

Isoform IIB1 interacts with measles virus N protein. N protein is released in the blood following lysis of measles infected cells. This interaction presumably block inflammatory immune response. Interacts with INPP5D/SHIP1.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Is the most broadly distributed Fc-gamma-receptor. Expressed in monocyte, neutrophils, macrophages, basophils, eosinophils, Langerhans cells, B-cells, platelets cells and placenta (endothelial cells). Not detected in natural killer cells.

Domain

Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.

Involvement in disease

A chromosomal aberration involving FCGR2B is found in a follicular lymphoma. Translocation t(1;22)(q22;q11). The translocation leads to the hyperexpression of the receptor. This may play a role in the tumor progression.

Sequence similarities

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

Caution

Has sometimes been attributed to correspond to FcR-IIC.

Ontologies

Keywords

   Biological processHost-virus interaction
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
   LigandIgG-binding protein
   Molecular functionReceptor
   PTMGlycoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processimmune response Ref.4

Traceable author statement. Source: ProtInc

signal transduction Ref.4

Traceable author statement. Source: ProtInc

   Cellular componentplasma membrane

Non-traceable author statement. Source: ProtInc

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IGHG1P018572EBI-724784,EBI-356114

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform IIB1 (identifier: P31994-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform IIB2 (identifier: P31994-2)

The sequence of this isoform differs from the canonical sequence as follows:
     254-272: Missing.
Isoform IIB3 (identifier: P31994-3)

The sequence of this isoform differs from the canonical sequence as follows:
     39-45: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 4242 Potential
Chain43 – 310268Low affinity immunoglobulin gamma Fc region receptor II-b

Regions

Topological domain43 – 217175Extracellular Potential
Transmembrane218 – 24023 Potential
Topological domain241 – 31070Cytoplasmic Potential
Domain48 – 12780Ig-like C2-type 1
Domain131 – 21383Ig-like C2-type 2
Motif290 – 2956ITIM motif

Amino acid modifications

Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Disulfide bond71 ↔ 113
Disulfide bond152 ↔ 196

Natural variations

Alternative sequence39 – 457Missing in isoform IIB3.
Alternative sequence254 – 27219Missing in isoform IIB2.
Natural variant2051Y → F: dbSNP rs17416919.
Natural variant2321I → T
Natural variant2581Y → D

Experimental info

Sequence conflict461Missing in AAD00637, AAD00638, AAD00639 and AAD00644. Ref.1
Sequence conflict1781D → I in CAA35644 and CAA35645. Ref.2
Sequence conflict2301T → I in CAA35644 and CAA35645. Ref.2
Sequence conflict2421V → G in CAA35644 and CAA35645. Ref.2
Sequence conflict2751P → S Ref.2

Secondary structure

...................................... 310
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform IIB1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 2186F8538FF01F36

FASTA31034,044
        10         20         30         40         50         60 
MGILSFLPVL ATESDWADCK SPQPWGHMLL WTAVLFLAPV AGTPAAPPKA VLKLEPQWIN 

        70         80         90        100        110        120 
VLQEDSVTLT CRGTHSPESD SIQWFHNGNL IPTHTQPSYR FKANNNDSGE YTCQTGQTSL 

       130        140        150        160        170        180 
SDPVHLTVLS EWLVLQTPHL EFQEGETIVL RCHSWKDKPL VKVTFFQNGK SKKFSRSDPN 

       190        200        210        220        230        240 
FSIPQANHSH SGDYHCTGNI GYTLYSSKPV TITVQAPSSS PMGIIVAVVT GIAVAAIVAA 

       250        260        270        280        290        300 
VVALIYCRKK RISALPGYPE CREMGETLPE KPANPTNPDE ADKVGAENTI TYSLLMHPDA 

       310 
LEEPDDQNRI 

« Hide

Isoform IIB2 [UniParc].

Checksum: 3B76609541B30962
Show »

29131,944
Isoform IIB3 [UniParc].

Checksum: B84833348A175687
Show »

30333,450

References

« Hide 'large scale' references
[1]"Fc-gamma-RIIb nucleotide sequences in SLE and non-SLE humans in vivo derived lymphocytes."
Ng S., Sinclair N.R.S., Anderson C., Bell D.A., Cairns E.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1 AND IIB2).
Tissue: Lymphocyte.
[2]"Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in macrophages, lymphocytes and IgG-transporting placental epithelium."
Stuart S.G., Simister N.E., Clarkson S.B., Kacinski B.M., Shapiro M., Mellman I.
EMBO J. 8:3657-3666(1989) [PubMed: 2531080] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
Tissue: Placenta.
[3]"Structure and expression of human IgG FcRII(CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes."
Brooks D.G., Qiu W.Q., Luster A.D., Ravetch J.V.
J. Exp. Med. 170:1369-1385(1989) [PubMed: 2529342] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1; IIB2 AND IIB3), VARIANT PHE-205.
[4]"Distribution, inducibility and biological function of the cloned and expressed human beta Fc receptor II."
Engelhardt W., Geerds C., Frey J.
Eur. J. Immunol. 20:1367-1377(1990) [PubMed: 2142460] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
Tissue: Placenta.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIB2).
[6]"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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIB1).
Tissue: Skin.
[8]"Fc gamma receptor gene polymorphisms in Japanese patients with systemic lupus erythematosus: contribution of FCGR2B to genetic susceptibility."
Kyogoku C., Dijstelbloem H.M., Tsuchiya N., Hatta Y., Kato H., Yamaguchi A., Fukazawa T., Jansen M.D., Hashimoto H., van de Winkel J.G.J., Kallenberg C.G.M., Tokunaga K.
Arthritis Rheum. 46:1242-1254(2002) [PubMed: 12115230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-253, VARIANT THR-232.
[9]"Measles virus nucleoprotein induces cell-proliferation arrest and apoptosis through NTAIL-NR and NCORE-FcgammaRIIB1 interactions, respectively."
Laine D., Bourhis J.-M., Longhi S., Flacher M., Cassard L., Canard B., Sautes-Fridman C., Rabourdin-Combe C., Valentin H.
J. Gen. Virol. 86:1771-1784(2005) [PubMed: 15914856] [Abstract]
Cited for: INTERACTION WITH MEASLES VIRUS N PROTEIN.
[10]"Crystal structure of the soluble form of the human fcgamma-receptor IIb: a new member of the immunoglobulin superfamily at 1.7 A resolution."
Sondermann P., Huber R., Jacob U.
EMBO J. 18:1095-1103(1999) [PubMed: 10064577] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 46-217, DISULFIDE BONDS.
[11]"Interaction of a human Fc gamma RIIb1 (CD32) isoform with murine and human IgG subclasses."
Warmerdam P.A., van den Herik-Oudijk I.E., Parren P.W., Westerdaal N.A., van de Winkel J.G., Capel P.J.
Int. Immunol. 5:239-247(1993) [PubMed: 8466861] [Abstract]
Cited for: VARIANT ASP-258.
+Additional computationally mapped references.

Cross-references

Sequence databases

U87560 mRNA. Translation: AAD00627.1.
U87561 mRNA. Translation: AAD00628.1.
U87562 mRNA. Translation: AAD00629.1.
U87563 mRNA. Translation: AAD00630.1.
U87564 mRNA. Translation: AAD00631.1.
U87565 mRNA. Translation: AAD00632.1.
U87566 mRNA. Translation: AAD00633.1.
U87567 mRNA. Translation: AAD00634.1.
U87568 mRNA. Translation: AAD00635.1.
U87569 mRNA. Translation: AAD00636.1.
U87570 mRNA. Translation: AAD00637.1.
U87571 mRNA. Translation: AAD00638.1.
U87572 mRNA. Translation: AAD00639.1.
U87573 mRNA. Translation: AAD00640.1.
U87574 mRNA. Translation: AAD00641.1.
U87575 mRNA. Translation: AAD00642.1.
U87576 mRNA. Translation: AAD00643.1.