Reviewed,
UniProtKB/Swiss-Prot P31994 (FCG2B_HUMAN)
Last modified
July 22, 2008.
Version 104.
History...
Clusters with 100%,
90%,
50% identity |
Documents (8) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 310 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| 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 process | Host-virus interaction |
| Cellular component | Cell membrane Membrane |
| Coding sequence diversity | Alternative splicing Chromosomal rearrangement Polymorphism |
| Disease | Proto-oncogene |
| Domain | Immunoglobulin domain Repeat Signal Transmembrane |
| Ligand | IgG-binding protein |
| Molecular function | Receptor |
| PTM | Glycoprotein |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | immune response Ref.4 Traceable author statement. Source: ProtInc signal transduction Ref.4Traceable author statement. Source: ProtInc |
| Cellular component | plasma membrane Non-traceable author statement. Source: ProtInc |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
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 key | Position(s) | Length | Description | Graphical view | |||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 42 | 42 | Potential | ||||||||||||||||||||||||||||||||||||||||||
| Chain | 43 – 310 | 268 | Low affinity immunoglobulin gamma Fc region receptor II-b | ||||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||
| Topological domain | 43 – 217 | 175 | Extracellular Potential | ||||||||||||||||||||||||||||||||||||||||||
| Transmembrane | 218 – 240 | 23 | Potential | ||||||||||||||||||||||||||||||||||||||||||
| Topological domain | 241 – 310 | 70 | Cytoplasmic Potential | ||||||||||||||||||||||||||||||||||||||||||
| Domain | 48 – 127 | 80 | Ig-like C2-type 1 | ||||||||||||||||||||||||||||||||||||||||||
| Domain | 131 – 213 | 83 | Ig-like C2-type 2 | ||||||||||||||||||||||||||||||||||||||||||
| Motif | 290 – 295 | 6 | ITIM motif | ||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 106 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 180 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 187 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 71 ↔ 113 | ||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 152 ↔ 196 | ||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 39 – 45 | 7 | Missing in isoform IIB3. | ||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 254 – 272 | 19 | Missing in isoform IIB2. | ||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 205 | 1 | Y → F: dbSNP rs17416919. | ||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 232 | 1 | I → T | ||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 258 | 1 | Y → D | ||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 46 | 1 | Missing in AAD00637, AAD00638, AAD00639 and AAD00644. Ref.1 | ||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 178 | 1 | D → I in CAA35644 and CAA35645. Ref.2 | ||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 230 | 1 | T → I in CAA35644 and CAA35645. Ref.2 | ||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 242 | 1 | V → G in CAA35644 and CAA35645. Ref.2 | ||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 275 | 1 | P → S Ref.2 | ||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 51 – 56 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 62 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 66 – 72 | 7 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 83 – 86 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 96 – 102 | 7 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 105 – 107 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 109 – 114 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 124 – 129 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 131 – 136 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 140 – 142 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 148 – 154 | 7 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 155 – 157 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 161 – 167 | 7 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 170 – 177 | 8 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 180 – 183 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 188 – 190 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 192 – 200 | 9 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 203 – 206 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 210 – 214 | 5 | |||||||||||||||||||||||||||||||||||||||||||
Sequences
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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. 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. | |

Clusters with