Reviewed, UniProtKB/Swiss-Prot O75015 (FCG3B_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	233 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 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal
Ligand	IgG-binding protein
Molecular function	Receptor
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	immune response Traceable author statement. Source: ProtInc
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	IgG binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Potential

Chain

17 – 200

184

Low affinity immunoglobulin gamma Fc region receptor III-B

PRO_0000015151

Propeptide

201 – 233

33

Removed in mature form Potential

PRO_0000015152

Regions

Domain

40 – 96

57

Ig-like C2-type 1

Domain

121 – 179

59

Ig-like C2-type 2

Amino acid modifications

Lipidation

200

1

GPI-anchor amidated serine Potential

Glycosylation

56

1

N-linked (GlcNAc...) Potential

Glycosylation

63

1

N-linked (GlcNAc...) Potential

Glycosylation

82

1

N-linked (GlcNAc...) Potential

Glycosylation

92

1

N-linked (GlcNAc...) Potential

Glycosylation

180

1

N-linked (GlcNAc...) Potential

Glycosylation

187

1

N-linked (GlcNAc...) Potential

Disulfide bond

47 ↔ 89

Disulfide bond

128 ↔ 172

Natural variations

Natural variant

36

1

S → R in allele FCGR3B*01.

VAR_003956

Natural variant

65

1

S → N in allele FCGR3B*01. dbSNP rs448740.

VAR_003963

Natural variant

78

1

A → D in allele SH. dbSNP rs5030738.

VAR_008802

Natural variant

82

1

N → D in allele FCGR3B*01.

VAR_003957

Natural variant

106

1

I → V in allele FCGR3B*01.

VAR_003964

Secondary structure

1

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233

Helix Strand Turn

Details...

Beta strand

27 – 32

6

Beta strand

35 – 38

4

Beta strand

43 – 48

6

Beta strand

59 – 62

4

Beta strand

65 – 70

6

Beta strand

72 – 78

7

Helix

81 – 83

3

Beta strand

85 – 90

6

Beta strand

92 – 94

3

Beta strand

100 – 105

6

Beta strand

107 – 112

6

Beta strand

116 – 119

4

Beta strand

124 – 130

7

Beta strand

137 – 143

7

Beta strand

146 – 153

8

Beta strand

157 – 161

5

Helix

164 – 166

3

Beta strand

168 – 176

9

Beta strand

179 – 182

4

Beta strand

186 – 191

6

Sequences

	Sequence		Length	Mass (Da)
	O75015-1 [UniParc]. Last modified November 1, 1999. Version 2. Checksum: 7AB5159432761726	FASTA	233	26,216
	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

References

	« Hide 'large scale' referencesShow '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: 2526846] [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: 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 [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: 16710414] [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: 7836402] [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: 10917521] [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: 11021536] [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: 9028335] [Abstract] Cited for: VARIANT SH ASP-78.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00023858.

PIR

JU0284.

RefSeq

NP_000561.3.

UniGene

Hs.694258

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

O75015.

Proteomic databases

PRIDE

O75015.

Genome annotation databases

Ensembl

ENST00000294800; ENSP00000294800; ENSG00000162747; Homo sapiens. [Genome view]
ENST00000367964; ENSP00000356941; ENSG00000162747; Homo sapiens. [Genome view]

GeneID

2215.

KEGG

hsa:2215.

UCSC

uc009wul.1. human.

Organism-specific databases

CTD

2215.

GeneCards

GC01M159859.

H-InvDB

HIX0056770.

HGNC

HGNC:3620. FCGR3B.

MIM

610665. gene.

Orphanet

855. Hashimoto struma.

PharmGKB

PA28066.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG282721.

HOVERGEN

O75015.

InParanoid

O75015.

Gene expression databases

ArrayExpress

O75015.

Bgee

O75015.

CleanEx

HS_FCGR3B.

Genevestigator

O75015.

GermOnline

ENSG00000162747. Homo sapiens.

Family and domain databases

InterPro

IPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 2 hits.

Pfam

PF00047. ig. 2 hits.
[Graphical view]

SMART

SM00409. IG. 2 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

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.

NextBio

8985.

SOURCE

Search...

Entry information

Entry name

FCG3B_HUMAN

Accession

Primary (citable) accession number: O75015

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	December 15, 2009
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.