FCGR1_MOUSE
ID FCGR1_MOUSE Reviewed; 404 AA.
AC P26151;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 181.
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: CD_antigen=CD64;
DE Flags: Precursor;
GN Name=Fcgr1; Synonyms=Fcg1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2136886;
RA Sears D.W., Osman N., Tate B., McKenzie I.F.C., Hogarth P.M.;
RT "Molecular cloning and expression of the mouse high affinity Fc receptor
RT for IgG.";
RL J. Immunol. 144:371-378(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1531670;
RA Osman N., Kozak C.A., McKenzie I.F.C., Hogarth P.M.;
RT "Structure and mapping of the gene encoding mouse high affinity Fc gamma RI
RT and chromosomal location of the human Fc gamma RI gene.";
RL J. Immunol. 148:1570-1575(1992).
RN [3]
RP GLYCOSYLATION, AND PHOSPHORYLATION.
RX PubMed=8478020;
RA Quilliam A.L., Osman N., McKenzie I.F.C., Hogarth P.M.;
RT "Biochemical characterization of murine Fc gamma RI.";
RL Immunology 78:358-363(1993).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11911823; DOI=10.1016/s1074-7613(02)00287-x;
RA Barnes N., Gavin A.L., Tan P.S., Mottram P., Koentgen F., Hogarth P.M.;
RT "FcgammaRI-deficient mice show multiple alterations to inflammatory and
RT immune responses.";
RL Immunity 16:379-389(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11911824; DOI=10.1016/s1074-7613(02)00294-7;
RA Ioan-Facsinay A., de Kimpe S.J., Hellwig S.M.M., van Lent P.L.,
RA Hofhuis F.M.A., van Ojik H.H., Sedlik C., da Silveira S.A., Gerber J.,
RA de Jong Y.F., Roozendaal R., Aarden L.A., van den Berg W.B., Saito T.,
RA Mosser D., Amigorena S., Izui S., van Ommen G.-J.B., van Vugt M.,
RA van de Winkel J.G.J., Verbeek J.S.;
RT "FcgammaRI (CD64) contributes substantially to severity of arthritis,
RT hypersensitivity responses, and protection from bacterial infection.";
RL Immunity 16:391-402(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-368, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: High affinity receptor for the Fc region of immunoglobulins
CC gamma. Functions in both innate and adaptive immune responses.
CC {ECO:0000269|PubMed:11911823, ECO:0000269|PubMed:11911824}.
CC -!- SUBUNIT: Interacts with FCERG1; forms a functional signaling complex
CC (By similarity). Interacts with FLNA; prevents FCGR1A degradation (By
CC similarity). Interacts with EPB41L2, LAT and PPL. Interacts with HCK
CC and LYN (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Note=Stabilized at the cell membrane through interaction with
CC FCER1G. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Macrophage-specific.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8478020}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:8478020}.
CC -!- DISRUPTION PHENOTYPE: According to PubMed:11911823, mice display
CC altered endocytosis of monomeric IgG and impaired antibody-dependent
CC killing of cells by macrophage. Antigen presentation is also affected
CC and those mice develop only reduced inflammatory responses. An
CC increased in IgG responses is also detected associated with an
CC increased number of antibody-forming cells. PubMed:11911824, also
CC reported that a variety of IgG2a-immune complex-dependent immune
CC functions like protection against bacterial infection were impaired.
CC {ECO:0000269|PubMed:11911823, ECO:0000269|PubMed:11911824}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. FCGR1 family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M31314; AAA40056.1; -; mRNA.
DR CCDS; CCDS17639.1; -.
DR PIR; A46480; A46480.
DR RefSeq; NP_034316.1; NM_010186.5.
DR AlphaFoldDB; P26151; -.
DR SMR; P26151; -.
DR BioGRID; 199618; 2.
DR IntAct; P26151; 1.
DR MINT; P26151; -.
DR STRING; 10090.ENSMUSP00000029748; -.
DR GlyGen; P26151; 5 sites.
DR iPTMnet; P26151; -.
DR PhosphoSitePlus; P26151; -.
DR jPOST; P26151; -.
DR MaxQB; P26151; -.
DR PaxDb; P26151; -.
DR PeptideAtlas; P26151; -.
DR PRIDE; P26151; -.
DR ProteomicsDB; 271684; -.
DR DNASU; 14129; -.
DR Ensembl; ENSMUST00000029748; ENSMUSP00000029748; ENSMUSG00000015947.
DR GeneID; 14129; -.
DR KEGG; mmu:14129; -.
DR UCSC; uc008qmr.1; mouse.
DR CTD; 14129; -.
DR MGI; MGI:95498; Fcgr1.
DR VEuPathDB; HostDB:ENSMUSG00000015947; -.
DR eggNOG; ENOG502S1XR; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_3_0_1; -.
DR InParanoid; P26151; -.
DR OMA; EYHIARA; -.
DR OrthoDB; 866496at2759; -.
DR PhylomeDB; P26151; -.
DR TreeFam; TF335097; -.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-2029481; FCGR activation.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR BioGRID-ORCS; 14129; 4 hits in 73 CRISPR screens.
DR PRO; PR:P26151; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P26151; protein.
DR Bgee; ENSMUSG00000015947; Expressed in stroma of bone marrow and 123 other tissues.
DR ExpressionAtlas; P26151; baseline and differential.
DR Genevisible; P26151; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019771; F:high-affinity IgG receptor activity; ISO:MGI.
DR GO; GO:0019864; F:IgG binding; IDA:MGI.
DR GO; GO:0019770; F:IgG receptor activity; IMP:MGI.
DR GO; GO:0031774; F:leukotriene receptor binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IMP:MGI.
DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; IMP:MGI.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IMP:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:MGI.
DR GO; GO:0006910; P:phagocytosis, recognition; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:MGI.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IMP:MGI.
DR GO; GO:0001805; P:positive regulation of type III hypersensitivity; IMP:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
DR GO; GO:0050776; P:regulation of immune response; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
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; 2.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; IgG-binding protein; Immunity;
KW Immunoglobulin domain; Innate immunity; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..404
FT /note="High affinity immunoglobulin gamma Fc receptor I"
FT /id="PRO_0000015140"
FT TOPO_DOM 25..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..111
FT /note="Ig-like C2-type 1"
FT DOMAIN 117..194
FT /note="Ig-like C2-type 2"
FT DOMAIN 201..286
FT /note="Ig-like C2-type 3"
FT REGION 321..342
FT /note="Interaction with EPB41L2"
FT /evidence="ECO:0000250"
FT REGION 346..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 134..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 221..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 404 AA; 44888 MW; 1C4F0033842767E7 CRC64;
MILTSFGDDM WLLTTLLLWV PVGGEVVNAT KAVITLQPPW VSIFQKENVT LWCEGPHLPG
DSSTQWFING TAVQISTPSY SIPEASFQDS GEYRCQIGSS MPSDPVQLQI HNDWLLLQAS
RRVLTEGEPL ALRCHGWKNK LVYNVVFYRN GKSFQFSSDS EVAILKTNLS HSGIYHCSGT
GRHRYTSAGV SITVKELFTT PVLRASVSSP FPEGSLVTLN CETNLLLQRP GLQLHFSFYV
GSKILEYRNT SSEYHIARAE REDAGFYWCE VATEDSSVLK RSPELELQVL GPQSSAPVWF
HILFYLSVGI MFSLNTVLYV KIHRLQREKK YNLEVPLVSE QGKKANSFQQ VRSDGVYEEV
TATASQTTPK EAPDGPRSSV GDCGPEQPEP LPPSDSTGAQ TSQS
