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P12318 (FCG2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low affinity immunoglobulin gamma Fc region receptor II-a

Short name=IgG Fc receptor II-a
Alternative name(s):
CDw32
Fc-gamma RII-a
Short name=Fc-gamma-RIIa
Short name=FcRII-a
CD_antigen=CD32
Gene names
Name:FCGR2A
Synonyms:CD32, FCG2, FCGR2A1, IGFR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Promotes phagocytosis of opsonized antigens. Ref.15

Subunit structure

Interacts with INPP5D/SHIP1 and INPPL1/SHIP2, regulating its function. Interacts with APCS and FGR. Interacts with HCK. Ref.9 Ref.10 Ref.12

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.15.

Tissue specificity

Found on monocytes, neutrophils and eosinophil platelets.

Post-translational modification

Phosphorylated by SRC-type Tyr-kinases such as LYN, BLK, FYN, HCK and SYK. Ref.10 Ref.11

Sequence similarities

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Sequence caution

The sequence AAA35932.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P12318-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P12318-2)

The sequence of this isoform differs from the canonical sequence as follows:
     35-35: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.8
Chain34 – 317284Low affinity immunoglobulin gamma Fc region receptor II-a
PRO_0000015145

Regions

Topological domain34 – 217184Extracellular Potential
Transmembrane218 – 24023Helical; Potential
Topological domain241 – 31777Cytoplasmic Potential
Domain39 – 11880Ig-like C2-type 1
Domain122 – 20483Ig-like C2-type 2

Amino acid modifications

Modified residue2881Phosphotyrosine; by SRC-type Tyr-kinases Ref.11
Modified residue3041Phosphotyrosine; by SRC-type Tyr-kinases Ref.11
Glycosylation971N-linked (GlcNAc...) Ref.8
Glycosylation1781N-linked (GlcNAc...) Ref.8
Disulfide bond62 ↔ 104 Ref.14 Ref.15
Disulfide bond143 ↔ 187 Ref.14 Ref.15

Natural variations

Alternative sequence351Missing in isoform 2.
VSP_036865
Natural variant631Q → R.
Corresponds to variant rs9427398 [ dbSNP | Ensembl ].
VAR_054857
Natural variant1401M → V.
Corresponds to variant rs4986941 [ dbSNP | Ensembl ].
VAR_054858
Natural variant1671H → R May be associated with susceptibility to lupus nephritis; does not efficiently recognize IgG2. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.16
Corresponds to variant rs1801274 [ dbSNP | Ensembl ].
VAR_003955
Natural variant2181I → V. Ref.4
Corresponds to variant rs17851834 [ dbSNP | Ensembl ].
VAR_054859

Experimental info

Sequence conflict21T → A in AAA35827. Ref.2

Secondary structure

........................................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 13, 2007. Version 4.
Checksum: 07F73F3BB282DFF6

FASTA31735,001
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 3B4B813ECF6DCFCD
Show »

FASTA31634,930

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-167.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-167.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 2), VARIANTS ARG-167 AND VAL-218.
Tissue: Lung and Testis.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-317 (ISOFORM 1), VARIANT ARG-167.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-317 (ISOFORM 1), VARIANT ARG-167.
[7]"Identification of multiple isoforms of the low-affinity human IgG Fc receptor."
Seki T.
Immunogenetics 30:5-12(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-317 (ISOFORM 1).
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION AT ASN-97 AND ASN-178, CRYSTALLIZATION.
[9]"Association of immunoglobulin G Fc receptor II with Src-like protein-tyrosine kinase Fgr in neutrophils."
Hamada F., Aoki M., Akiyama T., Toyoshima K.
Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGR.
[10]"Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells."
Ghazizadeh S., Bolen J.B., Fleit H.B.
J. Biol. Chem. 269:8878-8884(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCK, PHOSPHORYLATION.
[11]"In vivo and in vitro specificity of protein tyrosine kinases for immunoglobulin G receptor (FcgammaRII) phosphorylation."
Bewarder N., Weinrich V., Budde P., Hartmann D., Flaswinkel H., Reth M., Frey J.
Mol. Cell. Biol. 16:4735-4743(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-288 AND TYR-304.
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INPPL1.
[13]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 37-207.
[14]"Molecular basis for immune complex recognition: a comparison of Fc-receptor structures."
Sondermann P., Kaiser J., Jacob U.
J. Mol. Biol. 309:737-749(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 37-208, DISULFIDE BONDS.
[15]"Structural recognition and functional activation of FcgammaR by innate pentraxins."
Lu J., Marnell L.L., Marjon K.D., Mold C., Du Clos T.W., Sun P.D.
Nature 456:989-992(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 37-207 IN COMPLEX WITH APCS, SUBCELLULAR LOCATION, FUNCTION, DISULFIDE BONDS.
[16]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-167.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00644 mRNA. Translation: CAA68672.1.
M31932 mRNA. Translation: AAA35827.1.
AL590385 Genomic DNA. No translation available.
BC019931 mRNA. Translation: AAH19931.1.
BC020823 mRNA. Translation: AAH20823.1.
J03619 mRNA. Translation: AAA35932.1. Different initiation.
PIRJL0118.
RefSeqNP_001129691.1. NM_001136219.1.
NP_067674.2. NM_021642.3.
UniGeneHs.352642.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCGX-ray2.00A34-207[»]
1H9VX-ray3.00A37-208[»]
3D5OX-ray2.80F37-207[»]
3RY4X-ray1.50A37-206[»]
3RY5X-ray2.30A37-206[»]
3RY6X-ray3.80C40-206[»]
ProteinModelPortalP12318.
SMRP12318. Positions 37-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108506. 10 interactions.
IntActP12318. 2 interactions.
MINTMINT-8013486.
STRING9606.ENSP00000271450.

Chemistry

BindingDBP12318.
ChEMBLCHEMBL5841.
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.

PTM databases

PhosphoSiteP12318.

Polymorphism databases

DMDM160332371.

Proteomic databases

PaxDbP12318.
PRIDEP12318.

Protocols and materials databases

DNASU2212.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271450; ENSP00000271450; ENSG00000143226. [P12318-1]
ENST00000367972; ENSP00000356949; ENSG00000143226. [P12318-2]
GeneID2212.
KEGGhsa:2212.
UCSCuc001gam.3. human. [P12318-2]
uc001gan.3. human. [P12318-1]

Organism-specific databases

CTD2212.
GeneCardsGC01P161475.
H-InvDBHIX0018571.
HGNCHGNC:3616. FCGR2A.
HPAHPA010718.
HPA014730.
MIM146790. gene.
neXtProtNX_P12318.
PharmGKBPA28063.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG25177.
HOGENOMHOG000251632.
HOVERGENHBG051602.
InParanoidP12318.
KOK06472.
OMADLEPPWI.
OrthoDBEOG708W0N.
PhylomeDBP12318.
TreeFamTF335097.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP12318.
BgeeP12318.
CleanExHS_FCGR2A.
GenevestigatorP12318.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFCGR2A. human.
EvolutionaryTraceP12318.
GeneWikiFCGR2A.
GenomeRNAi2212.
NextBio8961.
PROP12318.
SOURCESearch...

Entry information

Entry nameFCG2A_HUMAN
AccessionPrimary (citable) accession number: P12318
Secondary accession number(s): Q8WUN1, Q8WW64
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 162 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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

Human cell differentiation molecules

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