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P12314 (FCGR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High affinity immunoglobulin gamma Fc receptor I

Short name=IgG Fc receptor I
Alternative name(s):
Fc-gamma RI
Short name=FcRI
Fc-gamma RIA
Short name=FcgammaRIa
CD_antigen=CD64
Gene names
Name:FCGR1A
Synonyms:FCG1, FCGR1, IGFR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses. Ref.9 Ref.10 Ref.11 Ref.12 Ref.19

Subunit structure

Interacts with FCERG1; forms a functional signaling complex. Interacts with FLNA; prevents FCGR1A degradation. Interacts with EPB41L2, LAT and PPL. Interacts with HCK and LYN. Ref.8 Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17

Subcellular location

Cell membrane; Single-pass type I membrane protein. Note: Stabilized at the cell membrane through interaction with FCER1G. Ref.9 Ref.14

Tissue specificity

Monocyte/macrophage specific.

Post-translational modification

Phosphorylated on serine residues By similarity.

Sequence similarities

Belongs to the immunoglobulin superfamily. FCGR1 family.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandIgG-binding protein
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

immune response

Traceable author statement PubMed 10879688. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

intracellular signal transduction

Traceable author statement PubMed 10879688. Source: GOC

phagocytosis, engulfment

Traceable author statement PubMed 10879688. Source: ProtInc

signal transduction

Traceable author statement PubMed 10879688. Source: ProtInc

   Cellular_componentclathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

early endosome membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.16. Source: BHF-UCL

   Molecular_functionreceptor signaling protein activity

Traceable author statement PubMed 10879688. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P12314-1)

Also known as: A;

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: P12314-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     333-374: HEKKVISSLQEDRHLEEELKCQEQKEEQLQEGVHRKEPQGAT → GQALEAPTQGCA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.6
Chain16 – 374359High affinity immunoglobulin gamma Fc receptor I
PRO_0000015139

Regions

Topological domain16 – 292277Extracellular Potential
Transmembrane293 – 31321Helical; Potential
Topological domain314 – 37461Cytoplasmic Potential
Domain22 – 10180Ig-like C2-type 1
Domain95 – 18490Ig-like C2-type 2
Domain190 – 27788Ig-like C2-type 3
Region312 – 33221Interaction with EPB41L2

Amino acid modifications

Glycosylation591N-linked (GlcNAc...) Ref.19
Glycosylation781N-linked (GlcNAc...) Ref.18 Ref.19
Glycosylation1521N-linked (GlcNAc...) Ref.19
Glycosylation1591N-linked (GlcNAc...) Ref.19
Glycosylation1631N-linked (GlcNAc...) Ref.19
Glycosylation1951N-linked (GlcNAc...) Ref.19
Glycosylation2401N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 85 Ref.19
Disulfide bond124 ↔ 168 Ref.19
Disulfide bond212 ↔ 260 Ref.19

Natural variations

Alternative sequence333 – 37442HEKKV…PQGAT → GQALEAPTQGCA in isoform 2.
VSP_002637
Natural variant1051L → P.
Corresponds to variant rs619322 [ dbSNP | Ensembl ].
VAR_019522

Experimental info

Mutagenesis3061N → D: Decreases cell membrane expression by 50% in absence of FCER1G. Ref.14
Mutagenesis3061N → G: Increases cell membrane expression in absence of FCER1G. Ref.14
Sequence conflict251T → S in CAA32537. Ref.1
Sequence conflict1151T → M in AAA58414. Ref.4
Sequence conflict1831V → QY in AAA58414. Ref.4
Sequence conflict2841Q → R in AAA58414. Ref.4
Sequence conflict3241D → N in AAA58414. Ref.4
Sequence conflict3381I → T Ref.1
Sequence conflict3381I → T Ref.2

Secondary structure

........................................................ 374
Helix Strand Turn

Details...

Sequences

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

Last modified July 19, 2004. Version 2.
Checksum: D33D59398CEEA699

FASTA37442,632
        10         20         30         40         50         60 
MWFLTTLLLW VPVDGQVDTT KAVITLQPPW VSVFQEETVT LHCEVLHLPG SSSTQWFLNG 

        70         80         90        100        110        120 
TATQTSTPSY RITSASVNDS GEYRCQRGLS GRSDPIQLEI HRGWLLLQVS SRVFTEGEPL 

       130        140        150        160        170        180 
ALRCHAWKDK LVYNVLYYRN GKAFKFFHWN SNLTILKTNI SHNGTYHCSG MGKHRYTSAG 

       190        200        210        220        230        240 
ISVTVKELFP APVLNASVTS PLLEGNLVTL SCETKLLLQR PGLQLYFSFY MGSKTLRGRN 

       250        260        270        280        290        300 
TSSEYQILTA RREDSGLYWC EAATEDGNVL KRSPELELQV LGLQLPTPVW FHVLFYLAVG 

       310        320        330        340        350        360 
IMFLVNTVLW VTIRKELKRK KKWDLEISLD SGHEKKVISS LQEDRHLEEE LKCQEQKEEQ 

       370 
LQEGVHRKEP QGAT 

« Hide

Isoform 2 (B) [UniParc].

Checksum: DDBE5DE64A66F6B8
Show »

FASTA34438,795

References

« Hide 'large scale' references
[1]"Nucleotide sequence of three cDNAs for the human high affinity Fc receptor (FcRI)."
Allen J.M., Seed B.
Nucleic Acids Res. 16:11824-11824(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Isolation and expression of functional high-affinity Fc receptor complementary DNAs."
Allen J.M., Seed B.
Science 243:378-381(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Novel Fc gamma receptor I family gene products in human mononuclear cells."
Porges A.J., Redecha P.B., Doebele R., Pan L.C., Salmon J.E., Kimberly R.P.
J. Clin. Invest. 90:2102-2109(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Blood.
[4]"Definition of interferon gamma-response elements in a novel human Fc gamma receptor gene (Fc gamma RIb) and characterization of the gene structure."
Benech P.D., Sastry K.N., Iyer R.R., Eichbaum Q.G., Raveh D.P., Ezekowitz R.A.
J. Exp. Med. 176:1115-1123(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[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. 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].
[6]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-30.
[7]"Three genes for the human high affinity Fc receptor for IgG (Fc gamma RI) encode four distinct transcription products."
Ernst L.K., van de Winkel J.G., Chiu I.M., Anderson C.L.
J. Biol. Chem. 267:15692-15700(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[8]"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn."
Wang A.V., Scholl P.R., Geha R.S.
J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCK AND LYN.
[9]"FcR gamma-chain is essential for both surface expression and function of human Fc gamma RI (CD64) in vivo."
van Vugt M.J., Heijnen I.A.F.M., Capel P.J.A., Park S.Y., Ra C., Saito T., Verbeek J.S., van de Winkel J.G.J.
Blood 87:3593-3599(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FCER1G, SUBCELLULAR LOCATION.
[10]"Molecular characterization of six variant Fcgamma receptor class I (CD64) transcripts."
Ernst L.K., Duchemin A.-M., Miller K.L., Anderson C.L.
Mol. Immunol. 35:943-954(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE SPLICING, GLYCOSYLATION.
[11]"The FcgammaRIa (CD64) ligand binding chain triggers major histocompatibility complex class II antigen presentation independently of its associated FcR gamma-chain."
van Vugt M.J., Kleijmeer M.J., Keler T., Zeelenberg I., van Dijk M.A., Leusen J.H.W., Geuze H.J., van de Winkel J.G.J.
Blood 94:808-817(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The cytoplasmic domain of human FcgammaRIa alters the functional properties of the FcgammaRI.gamma-chain receptor complex."
Edberg J.C., Yee A.M., Rakshit D.S., Chang D.J., Gokhale J.A., Indik Z.K., Schreiber A.D., Kimberly R.P.
J. Biol. Chem. 274:30328-30333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FCER1G.
[13]"The adapter protein LAT enhances fcgamma receptor-mediated signal transduction in myeloid cells."
Tridandapani S., Lyden T.W., Smith J.L., Carter J.E., Coggeshall K.M., Anderson C.L.
J. Biol. Chem. 275:20480-20487(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT.
[14]"Fcgamma receptor transmembrane domains: role in cell surface expression, gamma chain interaction, and phagocytosis."
Kim M.-K., Huang Z.-Y., Hwang P.-H., Jones B.A., Sato N., Hunter S., Kim-Han T.-H., Worth R.G., Indik Z.K., Schreiber A.D.
Blood 101:4479-4484(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-306, SUBCELLULAR LOCATION.
[15]"Direct interaction between FcgammaRI (CD64) and periplakin controls receptor endocytosis and ligand binding capacity."
Beekman J.M., Bakema J.E., van de Winkel J.G.J., Leusen J.H.W.
Proc. Natl. Acad. Sci. U.S.A. 101:10392-10397(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPL.
[16]"Filamin A stabilizes FcgammaRI surface expression and prevents its lysosomal routing."
Beekman J.M., van der Poel C.E., van der Linden J.A., van den Berg D.L.C., van den Berghe P.V.E., van de Winkel J.G.J., Leusen J.H.W.
J. Immunol. 180:3938-3945(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLNA.
[17]"Protein 4.1G binds to a unique motif within the FcgammaRI cytoplasmic tail."
Beekman J.M., Bakema J.E., van der Poel C.E., van der Linden J.A., van de Winkel J.G.J., Leusen J.H.W.
Mol. Immunol. 45:2069-2075(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPB41L2.
[18]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
Tissue: Liver.
[19]"Crystal structure of Fcgamma receptor I and its implication in high affinity gamma-immunoglobulin binding."
Lu J., Ellsworth J.L., Hamacher N., Oak S.W., Sun P.D.
J. Biol. Chem. 286:40608-40613(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 21-282, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-59; ASN-78; ASN-152; ASN-159; ASN-163 AND ASN-195.
+Additional computationally mapped references.

Web resources

FCGR1Abase

FCGR1A mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14356 mRNA. Translation: CAA32537.1.
X14355 mRNA. Translation: CAA32536.1.
L03418 mRNA. Translation: AAA36049.1.
M91555 expand/collapse EMBL AC list , M91550, M91551, M91552, M91553, M91554 Genomic DNA. Translation: AAA58414.1.
AL591493 Genomic DNA. Translation: CAI12557.1.
PIRA39878.
A41357.
RefSeqNP_000557.1. NM_000566.3.
UniGeneHs.77424.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RJDX-ray2.65A21-282[»]
ProteinModelPortalP12314.
SMRP12314. Positions 21-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108503. 5 interactions.
IntActP12314. 1 interaction.
MINTMINT-1538623.
STRING9606.ENSP00000358165.

Chemistry

BindingDBP12314.
ChEMBLCHEMBL5349.
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.
DB00992. Methyl aminolevulinate.
DB00075. Muromonab.
DB00108. Natalizumab.
DB00110. Palivizumab.
DB00707. Porfimer.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.

PTM databases

PhosphoSiteP12314.

Polymorphism databases

DMDM50403717.

Proteomic databases

PaxDbP12314.
PRIDEP12314.

Protocols and materials databases

DNASU2209.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369168; ENSP00000358165; ENSG00000150337. [P12314-1]
ENST00000580698; ENSP00000462402; ENSG00000266332. [P12314-1]
GeneID2209.
KEGGhsa:2209.
UCSCuc001esp.4. human. [P12314-1]

Organism-specific databases

CTD2209.
GeneCardsGC01P149754.
H-InvDBHIX0000999.
HGNCHGNC:3613. FCGR1A.
MIM146760. gene.
neXtProtNX_P12314.
PharmGKBPA28060.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277652.
HOGENOMHOG000251632.
HOVERGENHBG051602.
InParanoidP12314.
KOK06498.
OMARNSEFTI.
PhylomeDBP12314.
TreeFamTF335097.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP12314.

Gene expression databases

BgeeP12314.
CleanExHS_FCGR1A.
GenevestigatorP12314.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PfamPF00047. ig. 1 hit.
[Graphical view]
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFCGR1A.
GenomeRNAi2209.
NextBio8947.
PROP12314.
SOURCESearch...

Entry information

Entry nameFCGR1_HUMAN
AccessionPrimary (citable) accession number: P12314
Secondary accession number(s): P12315 expand/collapse secondary AC list , Q5QNW7, Q92495, Q92663
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 152 of the entry and version 2 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