Reviewed, UniProtKB/Swiss-Prot P12318 (FCG2A_HUMAN)

Names and origin

Protein names

Recommended name:
    Low affinity immunoglobulin gamma Fc region receptor II-a
      Short name=IgG Fc receptor II-a
Alternative name(s):
    Fc-gamma RII-a
    Fc-gamma-RIIa
      Short name=FcRII-a
    CDw32
    CD_antigen=CD32

Gene names

Name:	FCGR2A
Synonyms:	CD32, FCG2, FCGR2A1, IGFR2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	317 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	Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens.
Subunit structure	Interacts with INPP5D/SHIP1 and INPPL1/SHIP2, regulating its function.
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Tissue specificity	Found on monocytes, neutrophils and eosinophil platelets.
Sequence similarities	Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Ligand	IgG-binding protein
Molecular function	Receptor
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	plasma membrane Non-traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRP	P02741	1	EBI-1395970,EBI-1395983

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 33

33

Chain

34 – 317

284

Low affinity immunoglobulin gamma Fc region receptor II-a

Regions

Topological domain

34 – 217

184

Extracellular Potential

Transmembrane

218 – 240

23

Potential

Topological domain

241 – 317

77

Cytoplasmic Potential

Domain

39 – 118

80

Ig-like C2-type 1

Domain

122 – 204

83

Ig-like C2-type 2

Amino acid modifications

Modified residue

288

1

Phosphotyrosine

Glycosylation

97

1

N-linked (GlcNAc...)

Glycosylation

178

1

N-linked (GlcNAc...)

Disulfide bond

62 ↔ 104

Disulfide bond

143 ↔ 187

Natural variations

Natural variant

167

1

H → R May be associated with susceptibility to lupus nephritis; does not efficiently recognize IgG2. dbSNP rs1801274.

Experimental info

Sequence conflict

2

1

T → A in AAA35827. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

317

Helix Strand Turn

Details...

Beta strand

42 – 47

6

Beta strand

50 – 53

4

Beta strand

57 – 64

8

Beta strand

68 – 71

4

Beta strand

73 – 77

5

Beta strand

80 – 82

3

Beta strand

87 – 93

7

Helix

96 – 98

3

Beta strand

100 – 106

7

Beta strand

115 – 120

6

Beta strand

122 – 127

6

Beta strand

131 – 133

3

Beta strand

139 – 145

7

Helix

146 – 148

3

Beta strand

151 – 158

8

Beta strand

161 – 168

8

Beta strand

171 – 176

6

Helix

179 – 181

3

Beta strand

183 – 191

9

Beta strand

194 – 197

4

Beta strand

201 – 205

5

Sequences

	Sequence		Length	Mass (Da)
	P12318-1 [UniParc]. Last modified November 13, 2007. Version 4. Checksum: 07F73F3BB282DFF6	FASTA	317	35,001
	10 20 30 40 50 60 MTMETQMSQN VCPRNLWLLQ PLTVLLLLAS ADSQAAAPPK AVLKLEPPWI NVLQEDSVTL 70 80 90 100 110 120 TCQGARSPES DSIQWFHNGN LIPTHTQPSY RFKANNNDSG EYTCQTGQTS LSDPVHLTVL 130 140 150 160 170 180 SEWLVLQTPH LEFQEGETIM LRCHSWKDKP LVKVTFFQNG KSQKFSHLDP TFSIPQANHS 190 200 210 220 230 240 HSGDYHCTGN IGYTLFSSKP VTITVQVPSM GSSSPMGIIV AVVIATAVAA IVAAVVALIY 250 260 270 280 290 300 CRKKRISANS TDPVKAAQFE PPGRQMIAIR KRQLEETNND YETADGGYMT LNPRAPTDDD 310 KNIYLTLPPN DHVNSNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of human IgG FcRII(CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes." Brooks D.G., Qiu W.Q., Luster A.D., Ravetch J.V. J. Exp. Med. 170:1369-1385(1989) [PubMed: 2529342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-167.
[2]	"Isolation and expression of cDNA clones encoding a human receptor for IgG (Fc gamma RII)." Stuart S.G., Trounstine M.L., Vaux D.J.T., Koch T., Martens C.L., Moore K.W. J. Exp. Med. 166:1668-1684(1987) [PubMed: 2824655] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-167.
[3]	"Molecular cloning of a human immunoglobulin G Fc receptor." Hibbs M.L., Bonadonna L., Scott B.M., McKenzie I.F.C., Hogarth P.M. Proc. Natl. Acad. Sci. U.S.A. 85:2240-2244(1988) [PubMed: 2965389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-167.
[4]	"Isolation of cDNAs for two distinct human Fc receptors by ligand affinity cloning." Stengelin S., Stamenkovic I., Seed B. EMBO J. 7:1053-1059(1988) [PubMed: 3402431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[5]	"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].
[6]	"Identification of multiple isoforms of the low-affinity human IgG Fc receptor." Seki T. Immunogenetics 30:5-12(1989) [PubMed: 2526077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 6-317.
[7]	"Biochemical analysis and crystallisation of Fc gamma RIIa, the low affinity receptor for IgG." Powell M.S., Barton P.A., Emmanouilidis D., Wines B.D., Neumann G.M., Peitersz G.A., Maxwell K.F., Garrett T.P., Hogarth P.M. Immunol. Lett. 68:17-23(1999) [PubMed: 10397151] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION AT ASN-97 AND ASN-178, CRYSTALLIZATION.
[8]	"SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling." Pengal R.A., Ganesan L.P., Fang H., Marsh C.B., Anderson C.L., Tridandapani S. J. Biol. Chem. 278:22657-22663(2003) [PubMed: 12690104] [Abstract] Cited for: INTERACTION WITH INPPL1.
[9]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-288, MASS SPECTROMETRY.
[10]	"Crystal structure of the human leukocyte Fc receptor, Fc gammaRIIa." Maxwell K.F., Powell M.S., Hulett M.D., Barton P.A., McKenzie I.F., Garrett T.P., Hogarth P.M. Nat. Struct. Biol. 6:437-442(1999) [PubMed: 10331870] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 37-207.
[11]	"Fc gamma RIIA alleles are heritable risk factors for lupus nephritis in African Americans." Salmon J.E., Millard S., Schachter L.A., Arnett F.C., Ginzler E.M., Gourley M.F., Ramsey-Goldman R., Peterson M.G.E., Kimberly R.P. J. Clin. Invest. 97:1348-1354(1996) [PubMed: 8636449] [Abstract] Cited for: VARIANT ARG-167.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M31932 mRNA. Translation: AAA35827.1.
Y00644 mRNA. Translation: CAA68672.1.
J03619 mRNA. Translation: AAA35932.1. Different initiation.
AL590385 Genomic DNA. No translation available.

PIR

JL0118.

UniGene

Hs.352642

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FCG	X-ray	2.00	A	34-207	[»]
1H9V	X-ray	3.00	A	37-208	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P12318.

PTM databases

PhosphoSite

P12318.

Genome annotation databases

Ensembl

ENSG00000143226. Homo sapiens. [Contig view]

NMPDR

fig|9606.3.peg.2491.

Organism-specific databases

H-InvDB

HIX0018571.

HGNC

HGNC:3616. FCGR2A.

HPA

HPA010718.

MIM

146790. gene.

PharmGKB

PA28063.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P12318.

HOVERGEN

P12318.

Gene expression databases

ArrayExpress

P12318.

CleanEx

HS_FCGR2A.

GermOnline

ENSG00000143226. 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. 2 hits.
[Graphical view]

ProDom

P12318.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

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.

SOURCE

Search...

ProtoNet

Search...

Entry information

Entry name

FCG2A_HUMAN

Accession

Primary (citable) accession number: P12318

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	November 13, 2007
Last modified:	September 2, 2008
This is version 104 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)