ID   FCG2A_PANTR             Reviewed;         316 AA.
AC   Q8SPV8;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Low affinity immunoglobulin gamma Fc region receptor II-a;
DE            Short=IgG Fc receptor II-a;
DE   AltName: Full=Fc-gamma RII-a;
DE            Short=Fc-gamma-RIIa;
DE            Short=FcRII-a;
DE   AltName: CD_antigen=CD32;
DE   Flags: Precursor;
GN   Name=FCGR2A;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RA   Presta L.G., Namenuk A.K.;
RT   "Non-human primate Fc receptors and methods of use.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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. Promotes phagocytosis of opsonized
CC       antigens (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with INPP5D/SHIP1 and INPPL1/SHIP2, regulating its
CC       function. Interacts with APCS and FGR. Interacts with HCK (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Phosphorylated by SRC-type Tyr-kinases such as HCK, LYN, BLK, FYN
CC       and SYK. {ECO:0000250}.
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DR   EMBL; AF485819; AAL92102.1; -; mRNA.
DR   RefSeq; NP_001009077.1; NM_001009077.1.
DR   AlphaFoldDB; Q8SPV8; -.
DR   SMR; Q8SPV8; -.
DR   STRING; 9598.ENSPTRP00000040980; -.
DR   PaxDb; Q8SPV8; -.
DR   GeneID; 450194; -.
DR   KEGG; ptr:450194; -.
DR   CTD; 2212; -.
DR   eggNOG; ENOG502SVEW; Eukaryota.
DR   InParanoid; Q8SPV8; -.
DR   OrthoDB; 1246375at2759; -.
DR   Proteomes; UP000002277; 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:0002376; P:immune system process; IEA:UniProtKB-KW.
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   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF13895; Ig_2; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 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; Immunity;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..316
FT                   /note="Low affinity immunoglobulin gamma Fc region receptor
FT                   II-a"
FT                   /id="PRO_0000015146"
FT   TOPO_DOM        36..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..316
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          38..117
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          121..203
FT                   /note="Ig-like C2-type 2"
FT   MOD_RES         287
FT                   /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT                   /evidence="ECO:0000250|UniProtKB:P12318"
FT   MOD_RES         303
FT                   /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT                   /evidence="ECO:0000250|UniProtKB:P12318"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        142..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   316 AA;  34782 MW;  AC8BF945B0859D35 CRC64;
     MAMETQMSQN VCPRNLWLLQ PLTVLLLLAS ADSQAAPPKA VLKLEPPWIN VLQEDSVTLT
     CRGARSPESD SIQWFHNGNL IPTHTQPSYR FKANNNDSGE YTCQTGQTSL SDPVHLTVLS
     EWLVLQTPHL EFQEGETIVL RCHSWKDKPL VKVTFFQNGK SQKFSHLDPN LSIPQANHSH
     SGDYHCTGNI GYTLFSSKPV TITVQAPSVG SSSPVGIIVA VVIATAVAAI VAAVVALIYC
     RKKRISANST DPVKAAQFEP PGRQMIAIRK RQLEETNNDY ETADGGYMTL NPRAPTDDDK
     NIYLTLPPND HVNSNN