FCGR2_BOVIN
ID FCGR2_BOVIN Reviewed; 296 AA.
AC Q28110;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor II;
DE Short=IgG Fc receptor II;
DE AltName: Full=Fc-gamma RII;
DE Short=FcRII;
DE AltName: CD_antigen=CD32;
DE Flags: Precursor;
GN Name=FCGR2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8188320; DOI=10.1007/bf00176160;
RA Zhang G., Young J.R., Tregaskes C.R., Howard C.J.;
RT "Cattle Fc gamma RII: molecular cloning and ligand specificity.";
RL Immunogenetics 39:423-427(1994).
CC -!- FUNCTION: Binds to the Fc region of immunoglobulins gamma. Low affinity
CC receptor.
CC -!- SUBUNIT: Interacts with FGR and LYN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Higher expression is found in macrophages than in
CC neutrophils.
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; X75671; CAA53367.1; -; mRNA.
DR PIR; I46021; I46021.
DR RefSeq; NP_776964.1; NM_174539.2.
DR AlphaFoldDB; Q28110; -.
DR SMR; Q28110; -.
DR STRING; 9913.ENSBTAP00000045494; -.
DR PeptideAtlas; Q28110; -.
DR PRIDE; Q28110; -.
DR GeneID; 282229; -.
DR KEGG; bta:282229; -.
DR CTD; 2213; -.
DR InParanoid; Q28110; -.
DR OrthoDB; 1246375at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
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 2: Evidence at transcript 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..42
FT /evidence="ECO:0000255"
FT CHAIN 43..296
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT II"
FT /id="PRO_0000015141"
FT TOPO_DOM 43..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..129
FT /note="Ig-like C2-type 1"
FT DOMAIN 130..212
FT /note="Ig-like C2-type 2"
FT MOTIF 273..278
FT /note="ITIM motif"
FT MOD_RES 275
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63203"
FT MOD_RES 292
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08101"
FT CARBOHYD 79
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 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 151..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 296 AA; 33020 MW; A61A40A611F71ED5 CRC64;
MGIPSFLAFP AARRNRAHCT PWHPWGHMLL WTALLFLAPV SGKPDLPKAV VTIQPAWINV
LREDHVTLTC QGTSFSAGNL TTWFHNGSSI HTQKQPSYSF RAGSNDSGSY RCQREQTSLS
DPVHLDVISD WLLLQTPSLV FQEGEPIMLR CHSWRNQPLN KITFYQDRKS KIFSYQRTNF
SIPRANLSHS GQYHCTAFIG KMLHSSQPVN ITVQESSSSG PSSMTAVAIG TCFAAVAIVA
AIITWFRLRR KPISAGLTDA ENDAARTEAE NTVTYSLLSH PDVAEEDSES DYQKRL
