ID FCG3A_HUMAN Reviewed; 254 AA.
AC P08637; A2N6W9; Q53FJ0; Q53FL6; Q5EBR4; Q65ZM6; Q6PIJ0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 29-MAY-2013, entry version 150.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-A;
DE AltName: Full=CD16a antigen;
DE AltName: Full=Fc-gamma RIII-alpha;
DE Short=Fc-gamma RIII;
DE Short=Fc-gamma RIIIa;
DE Short=FcRIII;
DE Short=FcRIIIa;
DE AltName: Full=FcR-10;
DE AltName: Full=IgG Fc receptor III-2;
DE AltName: CD_antigen=CD16a;
DE Flags: Precursor;
GN Name=FCGR3A; Synonyms=CD16A, FCG3, FCGR3, IGFR3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2526846; DOI=10.1084/jem.170.2.481;
RA Ravetch J.V., Perussia B.;
RT "Alternative membrane forms of Fc gamma RIII(CD16) on human natural
RT killer cells and neutrophils. Cell type-specific expression of two
RT genes that differ in single nucleotide substitutions.";
RL J. Exp. Med. 170:481-497(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=16951347;
RA Rogers K.A., Scinicariello F., Attanasio R.;
RT "IgG Fc receptor III homologues in nonhuman primate species: genetic
RT characterization and ligand interactions.";
RL J. Immunol. 177:3848-3856(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-176.
RC TISSUE=Synovium;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-176.
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC TISSUE=Placenta;
RX PubMed=7836402; DOI=10.1074/jbc.270.3.1350;
RA Gessner J.E., Grussenmeyer T., Kolanus W., Schmidt R.E.;
RT "The human low affinity immunoglobulin G Fc receptor III-A and III-B
RT genes. Molecular characterization of the promoter regions.";
RL J. Biol. Chem. 270:1350-1361(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-254, AND VARIANT VAL-176.
RX PubMed=7700021; DOI=10.1038/ki.1994.462;
RA Morcos M., Hansch G.M., Schonermark M., Ellwanger S., Harle M.,
RA Heckl-Ostreicher B.;
RT "Human glomerular mesangial cells express CD16 and may be stimulated
RT via this receptor.";
RL Kidney Int. 46:1627-1634(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-254.
RC TISSUE=Lung;
RX PubMed=2525780; DOI=10.1073/pnas.86.13.5079;
RA Scallon B.J., Scigliano E., Freedman V.H., Miedel M.C., Pan Y.C.,
RA Unkeless J.C., Kochan J.P.;
RT "A human immunoglobulin G receptor exists in both polypeptide-anchored
RT and phosphatidylinositol-glycan-anchored forms.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5079-5083(1989).
RN [9]
RP VARIANTS ARG-66 AND HIS-66.
RX PubMed=8609432;
RA de Haas M., Koene H.R., Kleijer M., de Vries E., Simsek S.,
RA van Tol M.J.D., Roos D., von dem Borne A.E.G.K.;
RT "A triallelic Fc gamma receptor type IIIA polymorphism influences the
RT binding of human IgG by NK cell Fc gamma RIIIa.";
RL J. Immunol. 156:2948-2955(1996).
RN [10]
RP VARIANT VAL-176.
RX PubMed=9242542;
RA Koene H.R., Kleijer M., Algra J., Roos D., von dem Borne A.E.G.K.,
RA de Haas M.;
RT "Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by
RT natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-
RT 48L/R/H phenotype.";
RL Blood 90:1109-1114(1997).
RN [11]
RP VARIANT VAL-176.
RX PubMed=9276722; DOI=10.1172/JCI119616;
RA Wu J., Edberg J.C., Redecha P.B., Bansal V., Guyre P.M., Coleman K.,
RA Salmon J.E., Kimberly R.P.;
RT "A novel polymorphism of FcgammaRIIIa (CD16) alters receptor function
RT and predisposes to autoimmune disease.";
RL J. Clin. Invest. 100:1059-1070(1997).
CC -!- FUNCTION: Receptor for the Fc region of IgG. Binds complexed or
CC aggregated IgG and also monomeric IgG. Mediates antibody-dependent
CC cellular cytotoxicity (ADCC) and other antibody-dependent
CC responses, such as phagocytosis.
CC -!- SUBUNIT: Exists as a heterooligomeric receptor complex with Fc
CC epsilon receptor I gamma subunit and / or the CD3 zeta subunit.
CC Interacts with INPP5D/SHIP1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential). Secreted. Note=Exists also as a soluble
CC receptor.
CC -!- TISSUE SPECIFICITY: Expressed on natural killer cells,
CC macrophages, subpopulation of T-cells, immature thymocytes and
CC placental trophoblasts.
CC -!- PTM: Glycosylated. Contains high mannose- and complex-type
CC oligosaccharides.
CC -!- PTM: The soluble form is produced by a proteolytic cleavage.
CC -!- MISCELLANEOUS: Encoded by one of two nearly indentical genes:
CC FCGR3A (Shown here) and FCGR3B which are expressed in a tissue-
CC specific manner. The Phe-203 in III-A determines the transmembrane
CC domains whereas the 'Ser-203' in III-B determines the GPI-
CC anchoring.
CC -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD96988.1; Type=Erroneous initiation;
CC Sequence=BAD97015.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=FCGR3Abase; Note=FCGR3A mutation db;
CC URL="http://bioinf.uta.fi/FCGR3Abase/";
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/FCGR3A";
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DR EMBL; X52645; CAA36870.1; -; mRNA.
DR EMBL; AK223268; BAD96988.1; ALT_INIT; mRNA.
DR EMBL; AK223295; BAD97015.1; ALT_INIT; mRNA.
DR EMBL; AL590385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017865; AAH17865.1; -; mRNA.
DR EMBL; BC033678; AAH33678.1; -; mRNA.
DR EMBL; Z46222; CAA86295.1; -; Genomic_DNA.
DR EMBL; S76824; AAB33925.2; -; mRNA.
DR EMBL; M24853; AAA53506.1; -; mRNA.
DR IPI; IPI00218834; -.
DR PIR; JL0107; JL0107.
DR RefSeq; NP_000560.5; NM_000569.6.
DR RefSeq; NP_001121064.1; NM_001127592.1.
DR RefSeq; NP_001121065.1; NM_001127593.1.
DR RefSeq; NP_001121067.1; NM_001127595.1.
DR RefSeq; NP_001121068.1; NM_001127596.1.
DR UniGene; Hs.372679; -.
DR PDB; 3AY4; X-ray; 2.20 A; C=21-193.
DR PDB; 3SGJ; X-ray; 2.20 A; C=19-208.
DR PDB; 3SGK; X-ray; 2.40 A; C=19-208.
DR PDBsum; 3AY4; -.
DR PDBsum; 3SGJ; -.
DR PDBsum; 3SGK; -.
DR ProteinModelPortal; P08637; -.
DR IntAct; P08637; 2.
DR STRING; 9606.ENSP00000356946; -.
DR MEROPS; I43.001; -.
DR PhosphoSite; P08637; -.
DR DMDM; 119876; -.
DR PaxDb; P08637; -.
DR PRIDE; P08637; -.
DR DNASU; 2214; -.
DR Ensembl; ENST00000367967; ENSP00000356944; ENSG00000203747.
DR Ensembl; ENST00000436743; ENSP00000416607; ENSG00000203747.
DR Ensembl; ENST00000540048; ENSP00000444971; ENSG00000203747.
DR GeneID; 2214; -.
DR KEGG; hsa:2214; -.
DR UCSC; uc001gar.3; human.
DR CTD; 2214; -.
DR GeneCards; GC01M161511; -.
DR HGNC; HGNC:3619; FCGR3A.
DR HPA; CAB032435; -.
DR MIM; 146740; gene.
DR neXtProt; NX_P08637; -.
DR PharmGKB; PA28065; -.
DR eggNOG; NOG47725; -.
DR HOVERGEN; HBG051602; -.
DR InParanoid; P08637; -.
DR KO; K06463; -.
DR OrthoDB; EOG4ZS94D; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; FCGR3A; human.
DR DrugBank; DB00054; Abciximab.
DR DrugBank; DB00051; Adalimumab.
DR DrugBank; DB00092; Alefacept.
DR DrugBank; DB00087; Alemtuzumab.
DR DrugBank; DB00074; Basiliximab.
DR DrugBank; DB00112; Bevacizumab.
DR DrugBank; DB00002; Cetuximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00095; Efalizumab.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00056; Gemtuzumab ozogamicin.
DR DrugBank; DB00078; Ibritumomab.
DR DrugBank; DB00028; Immune globulin.
DR DrugBank; DB00075; Muromonab.
DR DrugBank; DB00108; Natalizumab.
DR DrugBank; DB00110; Palivizumab.
DR DrugBank; DB00073; Rituximab.
DR DrugBank; DB00081; Tositumomab.
DR DrugBank; DB00072; Trastuzumab.
DR EvolutionaryTrace; P08637; -.
DR GenomeRNAi; 2214; -.
DR NextBio; 8979; -.
DR ArrayExpress; P08637; -.
DR Bgee; P08637; -.
DR CleanEx; HS_FCGR3A; -.
DR Genevestigator; P08637; -.
DR GermOnline; ENSG00000203747; Homo sapiens.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR SMART; SM00409; IG; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond;
KW Glycoprotein; IgG-binding protein; Immunoglobulin domain; Membrane;
KW Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 16 Potential.
FT CHAIN 17 254 Low affinity immunoglobulin gamma Fc
FT region receptor III-A.
FT /FTId=PRO_0000015150.
FT TOPO_DOM 17 208 Extracellular (Potential).
FT TRANSMEM 209 229 Helical; (Potential).
FT TOPO_DOM 230 254 Cytoplasmic (Potential).
FT DOMAIN 24 105 Ig-like C2-type 1.
FT DOMAIN 107 189 Ig-like C2-type 2.
FT CARBOHYD 56 56 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 63 63 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 92 92 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 180 180 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 187 187 N-linked (GlcNAc...) (Potential).
FT DISULFID 47 89 By similarity.
FT DISULFID 128 172 By similarity.
FT VARIANT 66 66 L -> H.
FT /FTId=VAR_008800.
FT VARIANT 66 66 L -> R (in dbSNP:rs10127939).
FT /FTId=VAR_008799.
FT VARIANT 147 147 G -> D (in dbSNP:rs443082).
FT /FTId=VAR_058398.
FT VARIANT 158 158 Y -> H (in dbSNP:rs396716).
FT /FTId=VAR_058399.
FT VARIANT 176 176 F -> V (shows a higher binding capacity
FT of IgG1, IgG3 and IgG4; dbSNP:rs396991).
FT /FTId=VAR_003960.
FT VARIANT 203 203 F -> S (in dbSNP:rs1042206).
FT /FTId=VAR_058400.
FT CONFLICT 106 106 I -> V (in Ref. 3; BAD96988/BAD97015).
FT CONFLICT 195 195 A -> S (in Ref. 5; AAH33678).
FT STRAND 28 33
FT STRAND 35 38
FT STRAND 43 47
FT STRAND 51 54
FT STRAND 60 65
FT STRAND 71 78
FT HELIX 81 83
FT STRAND 85 89
FT STRAND 100 105
FT STRAND 107 112
FT STRAND 116 119
FT STRAND 124 130
FT HELIX 131 133
FT STRAND 137 143
FT STRAND 146 153
FT STRAND 157 161
FT HELIX 164 166
FT STRAND 168 176
FT STRAND 179 182
FT STRAND 186 191
SQ SEQUENCE 254 AA; 29089 MW; D38D178D32C67337 CRC64;
MWQLLLPTAL LLLVSAGMRT EDLPKAVVFL EPQWYRVLEK DSVTLKCQGA YSPEDNSTQW
FHNESLISSQ ASSYFIDAAT VDDSGEYRCQ TNLSTLSDPV QLEVHIGWLL LQAPRWVFKE
EDPIHLRCHS WKNTALHKVT YLQNGKGRKY FHHNSDFYIP KATLKDSGSY FCRGLFGSKN
VSSETVNITI TQGLAVSTIS SFFPPGYQVS FCLVMVLLFA VDTGLYFSVK TNIRSSTRDW
KDHKFKWRKD PQDK
//
