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O75015

- FCG3B_HUMAN

UniProt

O75015 - FCG3B_HUMAN

Protein

Low affinity immunoglobulin gamma Fc region receptor III-B

Gene

FCGR3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    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.

    GO - Biological processi

    1. immune response Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    IgG-binding protein

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:FCGR3B
    Synonyms:CD16B, FCG3, FCGR3, IGFR3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3620. FCGR3B.

    Subcellular locationi

    Cell membrane; Lipid-anchorGPI-anchor. Secreted
    Note: Secreted after cleavage.

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProt
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti855. Hashimoto struma.
    536. Systemic lupus erythematosus.
    PharmGKBiPA28066.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 200184Low affinity immunoglobulin gamma Fc region receptor III-BPRO_0000015151Add
    BLAST
    Propeptidei201 – 23333Removed in mature formSequence AnalysisPRO_0000015152Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi47 ↔ 89
    Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi128 ↔ 172
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Lipidationi200 – 2001GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

    Glycosylated. Glycosylation plays an inhibitory role in the interaction with IgG3.
    The soluble form is produced by a proteolytic cleavage.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiO75015.
    PRIDEiO75015.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO75015.
    BgeeiO75015.
    CleanExiHS_FCGR3B.
    GenevestigatoriO75015.

    Interactioni

    Subunit structurei

    Monomer. Interacts with INPP5D/SHIP1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiO75015. 1 interaction.
    STRINGi9606.ENSP00000294800.

    Structurei

    Secondary structure

    1
    233
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 326
    Beta strandi35 – 384
    Beta strandi43 – 486
    Beta strandi59 – 624
    Beta strandi65 – 706
    Beta strandi72 – 787
    Helixi81 – 833
    Beta strandi85 – 906
    Beta strandi92 – 943
    Beta strandi100 – 1056
    Beta strandi107 – 1126
    Beta strandi116 – 1194
    Beta strandi120 – 1223
    Beta strandi124 – 1307
    Helixi131 – 1333
    Beta strandi137 – 1437
    Beta strandi146 – 1538
    Beta strandi157 – 1615
    Helixi164 – 1663
    Beta strandi168 – 1769
    Beta strandi179 – 1824
    Beta strandi186 – 1916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E4JX-ray2.50A18-193[»]
    1E4KX-ray3.20C18-193[»]
    1FNLX-ray1.80A19-192[»]
    1T83X-ray3.00C19-194[»]
    1T89X-ray3.50C19-194[»]
    ProteinModelPortaliO75015.
    SMRiO75015. Positions 23-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75015.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 9657Ig-like C2-type 1Add
    BLAST
    Domaini121 – 17959Ig-like C2-type 2Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG47725.
    HOGENOMiHOG000251632.
    HOVERGENiHBG051602.
    InParanoidiO75015.
    KOiK06463.
    OrthoDBiEOG7SXW4Z.
    PhylomeDBiO75015.
    TreeFamiTF335097.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view]
    SMARTiSM00409. IG. 2 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O75015-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWQLLLPTAL LLLVSAGMRT EDLPKAVVFL EPQWYSVLEK DSVTLKCQGA    50
    YSPEDNSTQW FHNESLISSQ ASSYFIDAAT VNDSGEYRCQ TNLSTLSDPV 100
    QLEVHIGWLL LQAPRWVFKE EDPIHLRCHS WKNTALHKVT YLQNGKDRKY 150
    FHHNSDFHIP KATLKDSGSY FCRGLVGSKN VSSETVNITI TQGLAVSTIS 200
    SFSPPGYQVS FCLVMVLLFA VDTGLYFSVK TNI 233
    Length:233
    Mass (Da):26,216
    Last modified:November 1, 1999 - v2
    Checksum:i7AB5159432761726
    GO

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361S → R in allele FCGR3B*01.
    VAR_003956
    Natural varianti65 – 651S → N in allele FCGR3B*01. 1 Publication
    Corresponds to variant rs448740 [ dbSNP | Ensembl ].
    VAR_003963
    Natural varianti78 – 781A → D in allele SH. 1 Publication
    Corresponds to variant rs5030738 [ dbSNP | Ensembl ].
    VAR_008802
    Natural varianti82 – 821N → D in allele FCGR3B*01.
    VAR_003957
    Natural varianti106 – 1061I → V in allele FCGR3B*01.
    VAR_003964

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41433.1.
    PIRiJU0284.
    RefSeqiNP_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.
    UniGeneiHs.372679.
    Hs.694258.
    Hs.736230.

    Genome annotation databases

    EnsembliENST00000294800; ENSP00000294800; ENSG00000162747.
    ENST00000367964; ENSP00000356941; ENSG00000162747.
    GeneIDi2215.
    KEGGihsa:2215.
    UCSCiuc021pdo.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS41433.1.
    PIRi JU0284.
    RefSeqi NP_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.
    UniGenei Hs.372679.
    Hs.694258.
    Hs.736230.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E4J X-ray 2.50 A 18-193 [» ]
    1E4K X-ray 3.20 C 18-193 [» ]
    1FNL X-ray 1.80 A 19-192 [» ]
    1T83 X-ray 3.00 C 19-194 [» ]
    1T89 X-ray 3.50 C 19-194 [» ]
    ProteinModelPortali O75015.
    SMRi O75015. Positions 23-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O75015. 1 interaction.
    STRINGi 9606.ENSP00000294800.

    Chemistry

    BindingDBi O75015.
    ChEMBLi CHEMBL5842.
    DrugBanki DB00054. 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

    MEROPSi I43.001.

    Proteomic databases

    PaxDbi O75015.
    PRIDEi O75015.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000294800 ; ENSP00000294800 ; ENSG00000162747 .
    ENST00000367964 ; ENSP00000356941 ; ENSG00000162747 .
    GeneIDi 2215.
    KEGGi hsa:2215.
    UCSCi uc021pdo.1. human.

    Organism-specific databases

    CTDi 2215.
    GeneCardsi GC01M161592.
    H-InvDB HIX0056770.
    HGNCi HGNC:3620. FCGR3B.
    MIMi 610665. gene.
    neXtProti NX_O75015.
    Orphaneti 855. Hashimoto struma.
    536. Systemic lupus erythematosus.
    PharmGKBi PA28066.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47725.
    HOGENOMi HOG000251632.
    HOVERGENi HBG051602.
    InParanoidi O75015.
    KOi K06463.
    OrthoDBi EOG7SXW4Z.
    PhylomeDBi O75015.
    TreeFami TF335097.

    Miscellaneous databases

    EvolutionaryTracei O75015.
    GeneWikii FCGR3B.
    GenomeRNAii 2215.
    NextBioi 8985.
    PROi O75015.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75015.
    Bgeei O75015.
    CleanExi HS_FCGR3B.
    Genevestigatori O75015.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view ]
    SMARTi SM00409. IG. 2 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiFCG3B_HUMAN
    AccessioniPrimary (citable) accession number: O75015
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3