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   02-SEP-2026, entry version 197.
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; DOI=10.4049/jimmunol.148.5.1570;
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; 5.
DR   FunCoup; P26151; 608.
DR   IntAct; P26151; 1.
DR   MINT; P26151; -.
DR   STRING; 10090.ENSMUSP00000029748; -.
DR   GlyCosmos; P26151; 5 sites, No reported glycans.
DR   GlyGen; P26151; 5 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P26151; -.
DR   PhosphoSitePlus; P26151; -.
DR   jPOST; P26151; -.
DR   PaxDb; 10090-ENSMUSP00000029748; -.
DR   PeptideAtlas; P26151; -.
DR   ProteomicsDB; 271684; -.
DR   DNASU; 14129; -.
DR   Ensembl; ENSMUST00000029748.8; ENSMUSP00000029748.4; ENSMUSG00000015947.11.
DR   GeneID; 14129; -.
DR   KEGG; mmu:14129; -.
DR   UCSC; uc008qmr.1; mouse.
DR   AGR; MGI:95498; -.
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; VWFHILF; -.
DR   OrthoDB; 9950534at2759; -.
DR   PhylomeDB; P26151; -.
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 78 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 125 other cell types or tissues.
DR   ExpressionAtlas; P26151; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:GO_Central.
DR   GO; GO:0019771; F:high-affinity IgG receptor activity; ISO:GO_Central.
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: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: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:GO_Central.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IBA:GO_Central.
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   CDD; cd05752; Ig1_FcgammaR_like; 1.
DR   CDD; cd05753; Ig2_FcgammaR_like; 1.
DR   FunFam; 2.60.40.10:FF:000651; Fc receptor like 1; 1.
DR   FunFam; 2.60.40.10:FF:000217; High affinity immunoglobulin gamma Fc receptor I; 1.
DR   FunFam; 2.60.40.10:FF:000356; Low affinity immunoglobulin gamma Fc region receptor III-A; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR050488; Ig_Fc_receptor.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin_dom.
DR   PANTHER; PTHR11481:SF11; HIGH AFFINITY IMMUNOGLOBULIN GAMMA FC RECEPTOR I-RELATED; 1.
DR   PANTHER; PTHR11481; IMMUNOGLOBULIN FC RECEPTOR; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13895; Ig_2; 2.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 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        394..404
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
//