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P08637

- FCG3A_HUMAN

UniProt

P08637 - FCG3A_HUMAN

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Protein

Low affinity immunoglobulin gamma Fc region receptor III-A

Gene

FCGR3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. immune response Source: ProtInc
  3. innate immune response Source: Reactome
  4. regulation of immune response Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

IgG-binding protein

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160274. FCGR activation.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Low affinity immunoglobulin gamma Fc region receptor III-A
Alternative name(s):
CD16a antigen
Fc-gamma RIII-alpha
Short name:
Fc-gamma RIII
Short name:
Fc-gamma RIIIa
Short name:
FcRIII
Short name:
FcRIIIa
FcR-10
IgG Fc receptor III-2
CD_antigen: CD16a
Gene namesi
Name:FCGR3A
Synonyms:CD16A, FCG3, FCGR3, IGFR3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3619. FCGR3A.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 208192ExtracellularSequence AnalysisAdd
BLAST
Transmembranei209 – 22921HelicalSequence AnalysisAdd
BLAST
Topological domaini230 – 25425CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency 20 (IMD20) [MIM:615707]: A rare autosomal recessive primary immunodeficiency characterized by functional deficiency of NK cells. Affected individuals typically present with severe herpes viral infections, particularly Epstein Barr virus (EBV), and human papillomavirus (HPV).
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661L → H in IMD20. 4 Publications
Corresponds to variant rs10127939 [ dbSNP | Ensembl ].
VAR_008800

Organism-specific databases

MIMi615707. phenotype.
PharmGKBiPA28065.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 254238Low affinity immunoglobulin gamma Fc region receptor III-APRO_0000015150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 89
Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi63 – 631N-linked (GlcNAc...)2 Publications
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi128 ↔ 172
Glycosylationi180 – 1801N-linked (GlcNAc...)2 Publications
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated. Contains high mannose- and complex-type oligosaccharides. Glycosylation at Asn-180 is mandatory for high affinity binding to the Fc and for discrimination between fucosylated and afucosylated IgG glycoforms.2 Publications
The soluble form is produced by a proteolytic cleavage.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08637.
PRIDEiP08637.

PTM databases

PhosphoSiteiP08637.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP08637.
CleanExiHS_FCGR3A.
ExpressionAtlasiP08637. baseline.
GenevestigatoriP08637.

Organism-specific databases

HPAiCAB032435.
HPA055431.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi108508. 8 interactions.
IntActiP08637. 3 interactions.
STRINGi9606.ENSP00000356946.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 336Combined sources
Beta strandi35 – 384Combined sources
Beta strandi43 – 475Combined sources
Beta strandi51 – 544Combined sources
Beta strandi60 – 656Combined sources
Beta strandi71 – 788Combined sources
Helixi81 – 833Combined sources
Beta strandi85 – 895Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi124 – 1307Combined sources
Helixi131 – 1333Combined sources
Beta strandi137 – 1437Combined sources
Beta strandi146 – 1538Combined sources
Beta strandi157 – 1615Combined sources
Helixi164 – 1663Combined sources
Beta strandi168 – 1769Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi186 – 1916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AY4X-ray2.20C21-193[»]
3SGJX-ray2.20C19-208[»]
3SGKX-ray2.40C19-208[»]
ProteinModelPortaliP08637.
SMRiP08637. Positions 24-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08637.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 10582Ig-like C2-type 1Add
BLAST
Domaini107 – 18983Ig-like C2-type 2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47725.
GeneTreeiENSGT00760000119130.
HOVERGENiHBG051602.
InParanoidiP08637.
KOiK06463.
PhylomeDBiP08637.

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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08637-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWQLLLPTAL LLLVSAGMRT EDLPKAVVFL EPQWYRVLEK DSVTLKCQGA
60 70 80 90 100
YSPEDNSTQW FHNESLISSQ ASSYFIDAAT VDDSGEYRCQ TNLSTLSDPV
110 120 130 140 150
QLEVHIGWLL LQAPRWVFKE EDPIHLRCHS WKNTALHKVT YLQNGKGRKY
160 170 180 190 200
FHHNSDFYIP KATLKDSGSY FCRGLFGSKN VSSETVNITI TQGLAVSTIS
210 220 230 240 250
SFFPPGYQVS FCLVMVLLFA VDTGLYFSVK TNIRSSTRDW KDHKFKWRKD

PQDK
Length:254
Mass (Da):29,089
Last modified:August 1, 1990 - v2
Checksum:iD38D178D32C67337
GO

Sequence cautioni

The sequence BAD96988.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortenedCurated
The sequence BAD97015.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortenedCurated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061I → V in BAD96988. 1 PublicationCurated
Sequence conflicti106 – 1061I → V in BAD97015. 1 PublicationCurated
Sequence conflicti195 – 1951A → S in AAH33678. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661L → H in IMD20. 4 Publications
Corresponds to variant rs10127939 [ dbSNP | Ensembl ].
VAR_008800
Natural varianti66 – 661L → R.1 Publication
Corresponds to variant rs10127939 [ dbSNP | Ensembl ].
VAR_008799
Natural varianti147 – 1471G → D.
Corresponds to variant rs443082 [ dbSNP | Ensembl ].
VAR_058398
Natural varianti158 – 1581Y → H.
Corresponds to variant rs396716 [ dbSNP | Ensembl ].
VAR_058399
Natural varianti176 – 1761F → V Shows a higher binding capacity of IgG1, IgG3 and IgG4. 5 Publications
Corresponds to variant rs396991 [ dbSNP | Ensembl ].
VAR_003960
Natural varianti203 – 2031F → S.
Corresponds to variant rs1042206 [ dbSNP | Ensembl ].
VAR_058400

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44266.1.
PIRiJL0107.
RefSeqiNP_000560.5. NM_000569.6.
NP_001121064.1. NM_001127592.1.
NP_001121065.1. NM_001127593.1.
NP_001121067.1. NM_001127595.1.
NP_001121068.1. NM_001127596.1.
UniGeneiHs.372679.

Genome annotation databases

EnsembliENST00000367967; ENSP00000356944; ENSG00000203747.
ENST00000436743; ENSP00000416607; ENSG00000203747.
ENST00000443193; ENSP00000392047; ENSG00000203747.
GeneIDi2214.
KEGGihsa:2214.
UCSCiuc001gar.3. human.

Polymorphism databases

DMDMi119876.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

FCGR3Abase

FCGR3A mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS44266.1.
PIRi JL0107.
RefSeqi NP_000560.5. NM_000569.6.
NP_001121064.1. NM_001127592.1.
NP_001121065.1. NM_001127593.1.
NP_001121067.1. NM_001127595.1.
NP_001121068.1. NM_001127596.1.
UniGenei Hs.372679.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AY4 X-ray 2.20 C 21-193 [» ]
3SGJ X-ray 2.20 C 19-208 [» ]
3SGK X-ray 2.40 C 19-208 [» ]
ProteinModelPortali P08637.
SMRi P08637. Positions 24-231.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108508. 8 interactions.
IntActi P08637. 3 interactions.
STRINGi 9606.ENSP00000356946.

Chemistry

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. Intravenous Immunoglobulin.
DB00075. Muromonab.
DB00108. Natalizumab.
DB00110. Palivizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei P08637.

Polymorphism databases

DMDMi 119876.

Proteomic databases

PaxDbi P08637.
PRIDEi P08637.

Protocols and materials databases

DNASUi 2214.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367967 ; ENSP00000356944 ; ENSG00000203747 .
ENST00000436743 ; ENSP00000416607 ; ENSG00000203747 .
ENST00000443193 ; ENSP00000392047 ; ENSG00000203747 .
GeneIDi 2214.
KEGGi hsa:2214.
UCSCi uc001gar.3. human.

Organism-specific databases

CTDi 2214.
GeneCardsi GC01M161511.
HGNCi HGNC:3619. FCGR3A.
HPAi CAB032435.
HPA055431.
MIMi 146740. gene.
615707. phenotype.
neXtProti NX_P08637.
PharmGKBi PA28065.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47725.
GeneTreei ENSGT00760000119130.
HOVERGENi HBG051602.
InParanoidi P08637.
KOi K06463.
PhylomeDBi P08637.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160274. FCGR activation.

Miscellaneous databases

ChiTaRSi FCGR3A. human.
EvolutionaryTracei P08637.
GeneWikii FCGR3A.
GenomeRNAii 2214.
NextBioi 8979.
PROi P08637.
SOURCEi Search...

Gene expression databases

Bgeei P08637.
CleanExi HS_FCGR3A.
ExpressionAtlasi P08637. baseline.
Genevestigatori P08637.

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. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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].
  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] [Europe PMC] [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.
    , 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].
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-254.
    Tissue: Lung.
  9. "Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans."
    Mizushima T., Yagi H., Takemoto E., Shibata-Koyama M., Isoda Y., Iida S., Masuda K., Satoh M., Kato K.
    Genes Cells 16:1071-1080(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-193 IN COMPLEX WITH IGHG1, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-63 AND ASN-180.
  10. "Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose."
    Ferrara C., Grau S., Jager C., Sondermann P., Brunker P., Waldhauer I., Hennig M., Ruf A., Rufer A.C., Stihle M., Umana P., Benz J.
    Proc. Natl. Acad. Sci. U.S.A. 108:12669-12674(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-208 IN COMPLEX WITH IGHG1, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-63 AND ASN-180.
  11. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT IMD20 HIS-66, VARIANT ARG-66.
  12. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-176.
  13. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-176.
  14. "Identification of an unusual Fc gamma receptor IIIa (CD16) on natural killer cells in a patient with recurrent infections."
    de Vries E., Koene H.R., Vossen J.M., Gratama J.W., von dem Borne A.E., Waaijer J.L., Haraldsson A., de Haas M., van Tol M.J.
    Blood 88:3022-3027(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: RP VARIANT IMD20 HIS-66.
  15. "Natural Killer (NK) cell deficiency associated with an epitope-deficient Fc receptor type IIIA (CD16-II)."
    Jawahar S., Moody C., Chan M., Finberg R., Geha R., Chatila T.
    Clin. Exp. Immunol. 103:408-413(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: RP VARIANT IMD20 HIS-66.
  16. "Human immunodeficiency-causing mutation defines CD16 in spontaneous NK cell cytotoxicity."
    Grier J.T., Forbes L.R., Monaco-Shawver L., Oshinsky J., Atkinson T.P., Moody C., Pandey R., Campbell K.S., Orange J.S.
    J. Clin. Invest. 122:3769-3780(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: RP VARIANT IMD20 HIS-66.

Entry informationi

Entry nameiFCG3A_HUMAN
AccessioniPrimary (citable) accession number: P08637
Secondary accession number(s): A2N6W9
, Q53FJ0, Q53FL6, Q5EBR4, Q65ZM6, Q6PIJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: November 26, 2014
This is version 166 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 (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.

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

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