FCGR1_HUMAN
ID FCGR1_HUMAN Reviewed; 374 AA.
AC P12314; P12315; Q5QNW7; Q92495; Q92663;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=High affinity immunoglobulin gamma Fc receptor I;
DE Short=IgG Fc receptor I;
DE AltName: Full=Fc-gamma RI;
DE Short=FcRI;
DE AltName: Full=Fc-gamma RIA;
DE Short=FcgammaRIa;
DE AltName: CD_antigen=CD64;
DE Flags: Precursor;
GN Name=FCGR1A; Synonyms=FCG1, FCGR1, IGFR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=2974947; DOI=10.1093/nar/16.24.11824;
RA Allen J.M., Seed B.;
RT "Nucleotide sequence of three cDNAs for the human high affinity Fc receptor
RT (FcRI).";
RL Nucleic Acids Res. 16:11824-11824(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2911749; DOI=10.1126/science.2911749;
RA Allen J.M., Seed B.;
RT "Isolation and expression of functional high-affinity Fc receptor
RT complementary DNAs.";
RL Science 243:378-381(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=1430234; DOI=10.1172/jci116094;
RA Porges A.J., Redecha P.B., Doebele R., Pan L.C., Salmon J.E.,
RA Kimberly R.P.;
RT "Novel Fc gamma receptor I family gene products in human mononuclear
RT cells.";
RL J. Clin. Invest. 90:2102-2109(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=1402657; DOI=10.1084/jem.176.4.1115;
RA Benech P.D., Sastry K.N., Iyer R.R., Eichbaum Q.G., Raveh D.P.,
RA Ezekowitz R.A.;
RT "Definition of interferon gamma-response elements in a novel human Fc gamma
RT receptor gene (Fc gamma RIb) and characterization of the gene structure.";
RL J. Exp. Med. 176:1115-1123(1992).
RN [5]
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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 [6]
RP PROTEIN SEQUENCE OF 16-30.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP ALTERNATIVE SPLICING.
RX PubMed=1379234; DOI=10.1016/s0021-9258(19)49591-4;
RA Ernst L.K., van de Winkel J.G., Chiu I.M., Anderson C.L.;
RT "Three genes for the human high affinity Fc receptor for IgG (Fc gamma RI)
RT encode four distinct transcription products.";
RL J. Biol. Chem. 267:15692-15700(1992).
RN [8]
RP INTERACTION WITH HCK AND LYN.
RX PubMed=8064233; DOI=10.1084/jem.180.3.1165;
RA Wang A.V., Scholl P.R., Geha R.S.;
RT "Physical and functional association of the high affinity immunoglobulin G
RT receptor (Fc gamma RI) with the kinases Hck and Lyn.";
RL J. Exp. Med. 180:1165-1170(1994).
RN [9]
RP FUNCTION, INTERACTION WITH FCER1G, AND SUBCELLULAR LOCATION.
RX PubMed=8611682;
RA van Vugt M.J., Heijnen I.A.F.M., Capel P.J.A., Park S.Y., Ra C., Saito T.,
RA Verbeek J.S., van de Winkel J.G.J.;
RT "FcR gamma-chain is essential for both surface expression and function of
RT human Fc gamma RI (CD64) in vivo.";
RL Blood 87:3593-3599(1996).
RN [10]
RP FUNCTION, ALTERNATIVE SPLICING, AND GLYCOSYLATION.
RX PubMed=9881690; DOI=10.1016/s0161-5890(98)00079-0;
RA Ernst L.K., Duchemin A.-M., Miller K.L., Anderson C.L.;
RT "Molecular characterization of six variant Fcgamma receptor class I (CD64)
RT transcripts.";
RL Mol. Immunol. 35:943-954(1998).
RN [11]
RP FUNCTION.
RX PubMed=10397749;
RA van Vugt M.J., Kleijmeer M.J., Keler T., Zeelenberg I., van Dijk M.A.,
RA Leusen J.H.W., Geuze H.J., van de Winkel J.G.J.;
RT "The FcgammaRIa (CD64) ligand binding chain triggers major
RT histocompatibility complex class II antigen presentation independently of
RT its associated FcR gamma-chain.";
RL Blood 94:808-817(1999).
RN [12]
RP FUNCTION, AND INTERACTION WITH FCER1G.
RX PubMed=10514529; DOI=10.1074/jbc.274.42.30328;
RA Edberg J.C., Yee A.M., Rakshit D.S., Chang D.J., Gokhale J.A., Indik Z.K.,
RA Schreiber A.D., Kimberly R.P.;
RT "The cytoplasmic domain of human FcgammaRIa alters the functional
RT properties of the FcgammaRI.gamma-chain receptor complex.";
RL J. Biol. Chem. 274:30328-30333(1999).
RN [13]
RP INTERACTION WITH LAT.
RX PubMed=10781611; DOI=10.1074/jbc.m909462199;
RA Tridandapani S., Lyden T.W., Smith J.L., Carter J.E., Coggeshall K.M.,
RA Anderson C.L.;
RT "The adapter protein LAT enhances fcgamma receptor-mediated signal
RT transduction in myeloid cells.";
RL J. Biol. Chem. 275:20480-20487(2000).
RN [14]
RP FUNCTION, AND INTERACTION WITH IGHG1.
RX PubMed=11711607; DOI=10.1128/jvi.75.24.12161-12168.2001;
RA Hezareh M., Hessell A.J., Jensen R.C., van de Winkel J.G., Parren P.W.;
RT "Effector function activities of a panel of mutants of a broadly
RT neutralizing antibody against human immunodeficiency virus type 1.";
RL J. Virol. 75:12161-12168(2001).
RN [15]
RP MUTAGENESIS OF ASN-306, AND SUBCELLULAR LOCATION.
RX PubMed=12756162; DOI=10.1182/blood.v101.11.4479;
RA Kim M.-K., Huang Z.-Y., Hwang P.-H., Jones B.A., Sato N., Hunter S.,
RA Kim-Han T.-H., Worth R.G., Indik Z.K., Schreiber A.D.;
RT "Fcgamma receptor transmembrane domains: role in cell surface expression,
RT gamma chain interaction, and phagocytosis.";
RL Blood 101:4479-4484(2003).
RN [16]
RP INTERACTION WITH PPL.
RX PubMed=15229321; DOI=10.1073/pnas.0401217101;
RA Beekman J.M., Bakema J.E., van de Winkel J.G.J., Leusen J.H.W.;
RT "Direct interaction between FcgammaRI (CD64) and periplakin controls
RT receptor endocytosis and ligand binding capacity.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10392-10397(2004).
RN [17]
RP INTERACTION WITH FLNA.
RX PubMed=18322202; DOI=10.4049/jimmunol.180.6.3938;
RA Beekman J.M., van der Poel C.E., van der Linden J.A., van den Berg D.L.C.,
RA van den Berghe P.V.E., van de Winkel J.G.J., Leusen J.H.W.;
RT "Filamin A stabilizes FcgammaRI surface expression and prevents its
RT lysosomal routing.";
RL J. Immunol. 180:3938-3945(2008).
RN [18]
RP INTERACTION WITH EPB41L2.
RX PubMed=18023480; DOI=10.1016/j.molimm.2007.10.024;
RA Beekman J.M., Bakema J.E., van der Poel C.E., van der Linden J.A.,
RA van de Winkel J.G.J., Leusen J.H.W.;
RT "Protein 4.1G binds to a unique motif within the FcgammaRI cytoplasmic
RT tail.";
RL Mol. Immunol. 45:2069-2075(2008).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 21-282, FUNCTION, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-59; ASN-78; ASN-152; ASN-159; ASN-163 AND
RP ASN-195.
RX PubMed=21965667; DOI=10.1074/jbc.m111.257550;
RA Lu J., Ellsworth J.L., Hamacher N., Oak S.W., Sun P.D.;
RT "Crystal structure of Fcgamma receptor I and its implication in high
RT affinity gamma-immunoglobulin binding.";
RL J. Biol. Chem. 286:40608-40613(2011).
CC -!- FUNCTION: High affinity receptor for the Fc region of immunoglobulins
CC gamma. Functions in both innate and adaptive immune responses. Mediates
CC IgG effector functions on monocytes triggering antibody-dependent
CC cellular cytotoxicity (ADCC) of virus-infected cells.
CC {ECO:0000269|PubMed:10397749, ECO:0000269|PubMed:10514529,
CC ECO:0000269|PubMed:11711607, ECO:0000269|PubMed:21965667,
CC ECO:0000269|PubMed:8611682, ECO:0000269|PubMed:9881690}.
CC -!- SUBUNIT: Interacts with IGHG1 (PubMed:11711607). Interacts with FCERG1;
CC forms a functional signaling complex. Interacts with FLNA; prevents
CC FCGR1A degradation. Interacts with EPB41L2, LAT and PPL. Interacts with
CC HCK and LYN. {ECO:0000269|PubMed:10514529, ECO:0000269|PubMed:10781611,
CC ECO:0000269|PubMed:11711607, ECO:0000269|PubMed:15229321,
CC ECO:0000269|PubMed:18023480, ECO:0000269|PubMed:18322202,
CC ECO:0000269|PubMed:8064233, ECO:0000269|PubMed:8611682}.
CC -!- INTERACTION:
CC P12314; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-2869867, EBI-10827839;
CC P12314; P07306: ASGR1; NbExp=3; IntAct=EBI-2869867, EBI-1172335;
CC P12314; Q13323: BIK; NbExp=3; IntAct=EBI-2869867, EBI-700794;
CC P12314; O95393: BMP10; NbExp=3; IntAct=EBI-2869867, EBI-3922513;
CC P12314; Q86VB7: CD163; NbExp=3; IntAct=EBI-2869867, EBI-2808455;
CC P12314; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-2869867, EBI-12256978;
CC P12314; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-2869867, EBI-11989440;
CC P12314; O43491: EPB41L2; NbExp=3; IntAct=EBI-2869867, EBI-1052044;
CC P12314; Q92520: FAM3C; NbExp=3; IntAct=EBI-2869867, EBI-2876774;
CC P12314; P30273: FCER1G; NbExp=2; IntAct=EBI-2869867, EBI-515289;
CC P12314; P01857: IGHG1; NbExp=2; IntAct=EBI-2869867, EBI-356114;
CC P12314; O43736: ITM2A; NbExp=3; IntAct=EBI-2869867, EBI-2431769;
CC P12314; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2869867, EBI-10266796;
CC P12314; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-2869867, EBI-2820517;
CC P12314; Q13021: MALL; NbExp=3; IntAct=EBI-2869867, EBI-750078;
CC P12314; Q92982: NINJ1; NbExp=3; IntAct=EBI-2869867, EBI-2802124;
CC P12314; Q8IZ57: NRSN1; NbExp=3; IntAct=EBI-2869867, EBI-10264528;
CC P12314; Q9NS64: RPRM; NbExp=3; IntAct=EBI-2869867, EBI-1052363;
CC P12314; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-2869867, EBI-12003398;
CC P12314; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-2869867, EBI-12195249;
CC P12314; O00526: UPK2; NbExp=3; IntAct=EBI-2869867, EBI-10179682;
CC P12314; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-2869867, EBI-12190699;
CC P12314; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-2869867, EBI-723716;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12756162,
CC ECO:0000269|PubMed:8611682}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12756162, ECO:0000269|PubMed:8611682}.
CC Note=Stabilized at the cell membrane through interaction with FCER1G.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=P12314-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=P12314-2; Sequence=VSP_002637;
CC -!- TISSUE SPECIFICITY: Monocyte/macrophage specific.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. FCGR1 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=FCGR1Abase; Note=FCGR1A mutation db;
CC URL="http://structure.bmc.lu.se/idbase/FCGR1Abase/";
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DR EMBL; X14356; CAA32537.1; -; mRNA.
DR EMBL; X14355; CAA32536.1; -; mRNA.
DR EMBL; L03418; AAA36049.1; -; mRNA.
DR EMBL; M91555; AAA58414.1; -; Genomic_DNA.
DR EMBL; M91550; AAA58414.1; JOINED; Genomic_DNA.
DR EMBL; M91551; AAA58414.1; JOINED; Genomic_DNA.
DR EMBL; M91552; AAA58414.1; JOINED; Genomic_DNA.
DR EMBL; M91553; AAA58414.1; JOINED; Genomic_DNA.
DR EMBL; M91554; AAA58414.1; JOINED; Genomic_DNA.
DR EMBL; AL591493; CAI12557.1; -; Genomic_DNA.
DR CCDS; CCDS933.1; -. [P12314-1]
DR PIR; A39878; A39878.
DR PIR; A41357; A41357.
DR RefSeq; NP_000557.1; NM_000566.3. [P12314-1]
DR PDB; 3RJD; X-ray; 2.65 A; A=21-282.
DR PDB; 4W4O; X-ray; 1.80 A; C=16-289.
DR PDB; 4X4M; X-ray; 3.48 A; E/F=21-289.
DR PDB; 4ZNE; X-ray; 2.42 A; A=16-282.
DR PDBsum; 3RJD; -.
DR PDBsum; 4W4O; -.
DR PDBsum; 4X4M; -.
DR PDBsum; 4ZNE; -.
DR AlphaFoldDB; P12314; -.
DR SMR; P12314; -.
DR BioGRID; 108503; 48.
DR CORUM; P12314; -.
DR IntAct; P12314; 38.
DR MINT; P12314; -.
DR STRING; 9606.ENSP00000358165; -.
DR BindingDB; P12314; -.
DR ChEMBL; CHEMBL5349; -.
DR DrugBank; DB00087; Alemtuzumab.
DR DrugBank; DB00289; Atomoxetine.
DR DrugBank; DB00112; Bevacizumab.
DR DrugBank; DB06607; Catumaxomab.
DR DrugBank; DB00002; Cetuximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00056; Gemtuzumab ozogamicin.
DR DrugBank; DB00028; Human immunoglobulin G.
DR DrugBank; DB00108; Natalizumab.
DR DrugBank; DB00110; Palivizumab.
DR DrugBank; DB00707; Porfimer sodium.
DR DrugBank; DB11767; Sarilumab.
DR DrugBank; DB14962; Trastuzumab deruxtecan.
DR GlyGen; P12314; 7 sites.
DR iPTMnet; P12314; -.
DR PhosphoSitePlus; P12314; -.
DR BioMuta; FCGR1A; -.
DR DMDM; 50403717; -.
DR EPD; P12314; -.
DR jPOST; P12314; -.
DR MassIVE; P12314; -.
DR PaxDb; P12314; -.
DR PeptideAtlas; P12314; -.
DR PRIDE; P12314; -.
DR ProteomicsDB; 52847; -. [P12314-1]
DR ProteomicsDB; 52848; -. [P12314-2]
DR ABCD; P12314; 13 sequenced antibodies.
DR Antibodypedia; 20257; 1669 antibodies from 40 providers.
DR DNASU; 2209; -.
DR Ensembl; ENST00000369168.5; ENSP00000358165.4; ENSG00000150337.14. [P12314-1]
DR GeneID; 2209; -.
DR KEGG; hsa:2209; -.
DR MANE-Select; ENST00000369168.5; ENSP00000358165.4; NM_000566.4; NP_000557.1.
DR UCSC; uc001esp.5; human. [P12314-1]
DR CTD; 2209; -.
DR DisGeNET; 2209; -.
DR GeneCards; FCGR1A; -.
DR HGNC; HGNC:3613; FCGR1A.
DR HPA; ENSG00000150337; Tissue enhanced (epididymis, lymphoid tissue).
DR MIM; 146760; gene.
DR neXtProt; NX_P12314; -.
DR OpenTargets; ENSG00000150337; -.
DR PharmGKB; PA28060; -.
DR VEuPathDB; HostDB:ENSG00000150337; -.
DR eggNOG; ENOG502S1XR; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_3_0_1; -.
DR InParanoid; P12314; -.
DR OMA; PPWVNVF; -.
DR PhylomeDB; P12314; -.
DR TreeFam; TF335097; -.
DR PathwayCommons; P12314; -.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-2029481; FCGR activation.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR SignaLink; P12314; -.
DR SIGNOR; P12314; -.
DR BioGRID-ORCS; 2209; 97 hits in 685 CRISPR screens.
DR GeneWiki; FCGR1A; -.
DR GenomeRNAi; 2209; -.
DR Pharos; P12314; Tclin.
DR PRO; PR:P12314; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P12314; protein.
DR Bgee; ENSG00000150337; Expressed in monocyte and 102 other tissues.
DR ExpressionAtlas; P12314; baseline and differential.
DR Genevisible; P12314; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0019771; F:high-affinity IgG receptor activity; IDA:UniProtKB.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IDA:UniProtKB.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; TAS:ProtInc.
DR GO; GO:0006910; P:phagocytosis, recognition; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:ARUK-UCL.
DR GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IEA:Ensembl.
DR GO; GO:0001805; P:positive regulation of type III hypersensitivity; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW IgG-binding protein; Immunity; Immunoglobulin domain; Innate immunity;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 16..374
FT /note="High affinity immunoglobulin gamma Fc receptor I"
FT /id="PRO_0000015139"
FT TOPO_DOM 16..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..101
FT /note="Ig-like C2-type 1"
FT DOMAIN 95..184
FT /note="Ig-like C2-type 2"
FT DOMAIN 190..277
FT /note="Ig-like C2-type 3"
FT REGION 312..332
FT /note="Interaction with EPB41L2"
FT /evidence="ECO:0000269|PubMed:18023480"
FT REGION 352..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21965667"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:21965667"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21965667"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21965667"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21965667"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21965667"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21965667"
FT DISULFID 124..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21965667"
FT DISULFID 212..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21965667"
FT VAR_SEQ 333..374
FT /note="HEKKVISSLQEDRHLEEELKCQEQKEEQLQEGVHRKEPQGAT -> GQALEA
FT PTQGCA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2974947"
FT /id="VSP_002637"
FT VARIANT 105
FT /note="L -> P (in dbSNP:rs619322)"
FT /id="VAR_019522"
FT MUTAGEN 306
FT /note="N->D: Decreases cell membrane expression by 50% in
FT absence of FCER1G."
FT /evidence="ECO:0000269|PubMed:12756162"
FT MUTAGEN 306
FT /note="N->G: Increases cell membrane expression in absence
FT of FCER1G."
FT /evidence="ECO:0000269|PubMed:12756162"
FT CONFLICT 25
FT /note="T -> S (in Ref. 1; CAA32537)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="T -> M (in Ref. 4; AAA58414)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="V -> QY (in Ref. 4; AAA58414)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Q -> R (in Ref. 4; AAA58414)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="D -> N (in Ref. 4; AAA58414)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="I -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:4W4O"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4X4M"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4W4O"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:4W4O"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 164..177
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:4W4O"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:4W4O"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:4W4O"
SQ SEQUENCE 374 AA; 42632 MW; D33D59398CEEA699 CRC64;
MWFLTTLLLW VPVDGQVDTT KAVITLQPPW VSVFQEETVT LHCEVLHLPG SSSTQWFLNG
TATQTSTPSY RITSASVNDS GEYRCQRGLS GRSDPIQLEI HRGWLLLQVS SRVFTEGEPL
ALRCHAWKDK LVYNVLYYRN GKAFKFFHWN SNLTILKTNI SHNGTYHCSG MGKHRYTSAG
ISVTVKELFP APVLNASVTS PLLEGNLVTL SCETKLLLQR PGLQLYFSFY MGSKTLRGRN
TSSEYQILTA RREDSGLYWC EAATEDGNVL KRSPELELQV LGLQLPTPVW FHVLFYLAVG
IMFLVNTVLW VTIRKELKRK KKWDLEISLD SGHEKKVISS LQEDRHLEEE LKCQEQKEEQ
LQEGVHRKEP QGAT
