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Reviewed, UniProtKB/Swiss-Prot P08637 (FCG3A_HUMAN)

Last modified November 24, 2009. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · 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 III-A
Alternative name(s):
    IgG Fc receptor III-2
    Fc-gamma RIII-alpha
      Short name=Fc-gamma RIIIa
      Short name=FcRIIIa
      Short name=Fc-gamma RIII
      Short name=FcRIII
    FcR-10
    CD16a antigen
    CD_antigen=CD16a
Gene names
Name: FCGR3A
Synonyms: CD16A, FCG3, FCGR3, IGFR3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Receptor for the Fc region of IgG. Binds complexed or aggregated IgG and also monomeric IgG. Mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis.

Subunit structure

Exists as a heterooligomeric receptor complex with Fc epsilon receptor I gamma subunit and / or the CD3 zeta subunit. Interacts with INPP5D/SHIP1 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein Potential. Secreted. Note: Exists also as a soluble receptor.

Tissue specificity

Expressed on natural killer cells, macrophages, subpopulation of T-cells, immature thymocytes and placental trophoblasts.

Post-translational modification

Glycosylated. Contains high mannose- and complex-type oligosaccharides.

The soluble form is produced by a proteolytic cleavage.

Polymorphism

Variant Val-157 shows a higher binding capacity of IgG1, IgG3 and IgG4 compared with variant Phe-157. Alleles Leu-66 and Phe-157, and alleles His-66 / Arg-66 and Val-157 are in linkage desequilibrium.

Miscellaneous

Encoded by one of two nearly indentical genes: FCGR3A (Shown here) and FCGR3B which are expressed in a tissue-specific manner. The Phe-203 in III-A determines the transmembrane domains whereas the 'Ser-203' in III-B 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
Transmembrane
   LigandIgG-binding protein
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processimmune response

Traceable author statement. Source: ProtInc

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from Experiment. Source: Reactome

   Molecular functionIgG binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 254238Low affinity immunoglobulin gamma Fc region receptor III-A
PRO_0000015150

Regions

Topological domain17 – 208192Extracellular Potential
Transmembrane209 – 22921 Potential
Topological domain230 – 25425Cytoplasmic Potential
Domain24 – 10582Ig-like C2-type 1
Domain107 – 18983Ig-like C2-type 2

Amino acid modifications

Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 89 By similarity
Disulfide bond128 ↔ 172 By similarity

Natural variations

Natural variant661L → H
VAR_008800
Natural variant661L → R: dbSNP rs10127939. Ref.9
VAR_008799
Natural variant1471G → D: dbSNP rs443082.
VAR_058398
Natural variant1571F → V
VAR_008801
Natural variant1581Y → H: dbSNP rs396716.
VAR_058399
Natural variant1761F → V: dbSNP rs396991. Ref.3 Ref.5 Ref.7 Ref.11
VAR_003960
Natural variant2031F → S: dbSNP rs1042206.
VAR_058400

Experimental info

Sequence conflict1061I → V in BAD96988. Ref.3
Sequence conflict1061I → V in BAD97015. Ref.3
Sequence conflict1951A → S in AAH33678. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P08637-1 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: D38D178D32C67337

FASTA25429,089
        10         20         30         40         50         60 
MWQLLLPTAL LLLVSAGMRT EDLPKAVVFL EPQWYRVLEK DSVTLKCQGA YSPEDNSTQW 

        70         80         90        100        110        120 
FHNESLISSQ ASSYFIDAAT VDDSGEYRCQ TNLSTLSDPV QLEVHIGWLL LQAPRWVFKE 

       130        140        150        160        170        180 
EDPIHLRCHS WKNTALHKVT YLQNGKGRKY FHHNSDFYIP KATLKDSGSY FCRGLFGSKN 

       190        200        210        220        230        240 
VSSETVNITI TQGLAVSTIS SFFPPGYQVS FCLVMVLLFA VDTGLYFSVK TNIRSSTRDW 

       250 
KDHKFKWRKD PQDK 

« 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: 2526846] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"IgG Fc receptor III homologues in nonhuman primate species: genetic characterization and ligand interactions."
Rogers K.A., Scinicariello F., Attanasio R.
J. Immunol. 177:3848-3856(2006) [PubMed: 16951347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-176.
Tissue: Synovium.
[4]"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].
[5]"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], VARIANT VAL-176.
Tissue: Lung.
[6]"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 1-39.
Tissue: Placenta.
[7]"Human glomerular mesangial cells express CD16 and may be stimulated via this receptor."
Morcos M., Hansch G.M., Schonermark M., Ellwanger S., Harle M., Heckl-Ostreicher B.
Kidney Int. 46:1627-1634(1994) [PubMed: 7700021] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-254, VARIANT VAL-176.
[8]"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] OF 31-254.
Tissue: Lung.
[9]"A triallelic Fc gamma receptor type IIIA polymorphism influences the binding of human IgG by NK cell Fc gamma RIIIa."
de Haas M., Koene H.R., Kleijer M., de Vries E., Simsek S., van Tol M.J.D., Roos D., von dem Borne A.E.G.K.
J. Immunol. 156:2948-2955(1996) [PubMed: 8609432] [Abstract]
Cited for: VARIANTS ARG-66 AND HIS-66.
[10]"Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-48L/R/H phenotype."
Koene H.R., Kleijer M., Algra J., Roos D., von dem Borne A.E.G.K., de Haas M.
Blood 90:1109-1114(1997) [PubMed: 9242542] [Abstract]
Cited for: VARIANT VAL-157.
[11]"A novel polymorphism of FcgammaRIIIa (CD16) alters receptor function and predisposes to autoimmune disease."
Wu J., Edberg J.C., Redecha P.B., Bansal V., Guyre P.M., Coleman K., Salmon J.E., Kimberly R.P.
J. Clin. Invest. 100:1059-1070(1997) [PubMed: 9276722] [Abstract]
Cited for: VARIANT VAL-176.
+Additional computationally mapped references.

Web resources

FCGR3Abase

FCGR3A mutation db

GeneReviews

Cross-references

Sequence databases

X52645 mRNA. Translation: CAA36870.1.
AK223268 mRNA. Translation: BAD96988.1. Different initiation.
AK223295 mRNA. Translation: BAD97015.1. Different initiation.
AL590385 Genomic DNA. No translation available.
BC017865 mRNA. Translation: AAH17865.1.
BC033678 mRNA. Translation: AAH33678.1.
Z46222 Genomic DNA. Translation: CAA86295.1.
S76824 mRNA. Translation: AAB33925.2.
M24853 mRNA. Translation: AAA53506.1.
IPIIPI00218834.
PIRJL0107.
RefSeqNP_000560.5.
NP_001121064.1.
NP_001121065.1.
NP_001121067.1.
NP_001121068.1.
UniGeneHs.372679

3D structure databases

SMRP08637. Positions 21-193.
ModBaseSearch...

Protein-protein interaction databases

STRINGP08637.

Proteomic databases

PRIDEP08637.

Genome annotation databases

EnsemblENST00000367967; ENSP00000356944; ENSG00000203747; Homo sapiens. [Genome view]
ENST00000367969; ENSP00000356946; ENSG00000203747; Homo sapiens. [Genome view]
ENST00000436743; ENSP00000416607; ENSG00000203747; Homo sapiens. [Genome view]
GeneID2214.
KEGGhsa:2214.
UCSCuc001gat.2. human.

Organism-specific databases

CTD2214.
GeneCardsGC01M159778.
H-InvDBHIX0001248.
HGNCHGNC:3619. FCGR3A.
MIM146740. gene.
PharmGKBPA28065.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP08637.
OrthoDBEOG9642XB

Enzyme and pathway databases

ReactomeREACT_6900. Signaling in Immune system.

Gene expression databases

BgeeP08637.
CleanExHS_FCGR3A.
GenevestigatorP08637.
GermOnlineENSG00000203747. Homo sapiens.

Family and domain databases

InterProIPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
PfamPF00047. ig. 2 hits.
[Graphical view]
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

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.
NextBio8979.
SOURCESearch...

Entry information

Entry nameFCG3A_HUMAN
AccessionPrimary (citable) accession number: P08637
Secondary accession number(s): A2N6W9 expand/collapse secondary AC list , Q53FJ0, Q53FL6, Q5EBR4, Q65ZM6, Q6PIJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: November 24, 2009
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human cell differentiation molecules

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

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents