FCGR2_RAT
ID FCGR2_RAT Reviewed; 285 AA.
AC Q63203;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor II;
DE AltName: Full=Fc-gamma RII;
DE Short=FcRII;
DE AltName: Full=IgG Fc receptor II beta;
DE AltName: CD_antigen=CD32;
DE Flags: Precursor;
GN Name=Fcgr2; Synonyms=Fcgr2b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8405417; DOI=10.1016/0014-5793(93)80302-b;
RA Bocek P., Pecht I.;
RT "Cloning and sequence of the cDNA coding for rat type II Fc gamma receptor
RT of mast cells.";
RL FEBS Lett. 331:86-90(1993).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds to the Fc region of immunoglobulins gamma. Low affinity
CC receptor. By binding to IgG it initiates cellular responses against
CC pathogens and soluble antigens.
CC -!- SUBUNIT: Interacts with FGR and LYN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- PTM: Phosphorylated by SRC-type Tyr-kinases such as LYN, BLK, FYN and
CC SYK. {ECO:0000250}.
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DR EMBL; X73371; CAA51788.1; -; mRNA.
DR PIR; S36903; S36903.
DR RefSeq; NP_786932.1; NM_175756.1.
DR AlphaFoldDB; Q63203; -.
DR SMR; Q63203; -.
DR BioGRID; 252829; 1.
DR GlyGen; Q63203; 6 sites.
DR iPTMnet; Q63203; -.
DR PhosphoSitePlus; Q63203; -.
DR GeneID; 289211; -.
DR KEGG; rno:289211; -.
DR UCSC; RGD:631331; rat.
DR CTD; 2213; -.
DR RGD; 631331; Fcgr2b.
DR VEuPathDB; HostDB:ENSRNOG00000046452; -.
DR InParanoid; Q63203; -.
DR PhylomeDB; Q63203; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-2029481; FCGR activation.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q63203; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000046452; Expressed in spleen and 19 other tissues.
DR ExpressionAtlas; Q63203; baseline and differential.
DR Genevisible; Q63203; RN.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0019864; F:IgG binding; IDA:RGD.
DR GO; GO:0019865; F:immunoglobulin binding; IDA:RGD.
DR GO; GO:0019772; F:low-affinity IgG receptor activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0006952; P:defense response; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0032456; P:endocytic recycling; IDA:RGD.
DR GO; GO:0160006; P:Fc receptor-mediated immune complex endocytosis; ISO:RGD.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; ISO:RGD.
DR GO; GO:0002434; P:immune complex clearance; IDA:RGD.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISO:RGD.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; ISO:RGD.
DR GO; GO:0050777; P:negative regulation of immune response; ISO:RGD.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:RGD.
DR GO; GO:0033030; P:negative regulation of neutrophil apoptotic process; IMP:RGD.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISO:RGD.
DR GO; GO:0001811; P:negative regulation of type I hypersensitivity; ISO:RGD.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:ARUK-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:1905898; P:positive regulation of response to endoplasmic reticulum stress; IMP:ARUK-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:RGD.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; ISO:RGD.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR Gene3D; 2.60.40.10; -; 2.
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 Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; IgG-binding protein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..285
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT II"
FT /id="PRO_0000015144"
FT TOPO_DOM 32..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..118
FT /note="Ig-like C2-type 1"
FT DOMAIN 119..201
FT /note="Ig-like C2-type 2"
FT MOTIF 262..267
FT /note="ITIM motif"
FT MOD_RES 264
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 281
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08101"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
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 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 140..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 285 AA; 32048 MW; 255540A584CFFA0A CRC64;
MDSNRTVVHV LSRTLYHMLL WTAVLNLVAE SHAGLPKAVV KLEPPWIQVL KEDTVTLMCE
GTHNTKNCST QWFHNGSSIW HQAQANYTFK ATVNDSGEYR CRMEETGISE PIHLGVISDW
LLLQTSQLVF EEGETITLRC HSWKNKQLTK VLLFQNGKPV RYYHQSSNFS IPKANHSHSG
NYYCKAYLGR TMHVSKPVTI TVQEPKSSSS LPVLTIVAAV AGIAVAAIVI ILVSLVYLKK
KQVPDTPSGL EEAEKNEVEN TITYSLLKHP EAPDEESDHD YQNHI
