FCGR2_CAVPO
ID FCGR2_CAVPO Reviewed; 341 AA.
AC Q60513; Q60498; Q60511; Q60512;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
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: Full=Fc-gamma-1/gamma-2 receptor;
DE AltName: CD_antigen=CD32;
DE Flags: Precursor;
GN Name=FCGR2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2R-B1).
RX PubMed=1692213; DOI=10.1016/0006-291x(90)92375-a;
RA Tominaga M., Sakata A., Ohmura T., Yamashita T., Koyama J., Onoue K.;
RT "The structure and expression of the guinea pig Fc receptor for IgG1 and
RT IgG2 (Fc gamma 1/gamma 2R).";
RL Biochem. Biophys. Res. Commun. 168:683-689(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2R-B1; 2R-B2 AND 2R-B3).
RC STRAIN=JY-1;
RX PubMed=8345193;
RA Yamashita T., Shinohara K., Yamashita Y.;
RT "Expression cloning of complementary DNA encoding three distinct isoforms
RT of guinea pig Fc receptor for IgG1 and IgG2.";
RL J. Immunol. 151:2014-2023(1993).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2R-B3;
CC IsoId=Q60513-1; Sequence=Displayed;
CC Name=2R-B1;
CC IsoId=Q60513-2; Sequence=VSP_002639;
CC Name=2R-B2;
CC IsoId=Q60513-3; Sequence=VSP_002638;
CC -!- TISSUE SPECIFICITY: Macrophages and polymorphonuclear leukocytes
CC express preferentially isoform 2R-B1. B-lymphocytes express isoform 2R-
CC B1, isoform 2R-B2 and isoform 2R-B3.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37036.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D13693; BAA02852.1; -; mRNA.
DR EMBL; D13692; BAA02851.1; -; mRNA.
DR EMBL; D13691; BAA02850.1; -; mRNA.
DR EMBL; M35272; AAA37036.1; ALT_INIT; mRNA.
DR RefSeq; NP_001166520.1; NM_001173049.1. [Q60513-1]
DR AlphaFoldDB; Q60513; -.
DR SMR; Q60513; -.
DR STRING; 10141.ENSCPOP00000002698; -.
DR MEROPS; I43.001; -.
DR GeneID; 100192391; -.
DR KEGG; cpoc:100192391; -.
DR CTD; 2213; -.
DR eggNOG; ENOG502SVEW; Eukaryota.
DR InParanoid; Q60513; -.
DR OrthoDB; 1246375at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW IgG-binding protein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..341
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT II"
FT /id="PRO_0000015142"
FT TOPO_DOM 43..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 131..213
FT /note="Ig-like C2-type 2"
FT REGION 255..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 318..323
FT /note="ITIM motif"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250"
FT MOD_RES 337
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08101"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 257..301
FT /note="GNPEHREMGETLPEDPGEYSVVFGGSMMSCPGLPDGLEPARTDLS -> A
FT (in isoform 2R-B1)"
FT /evidence="ECO:0000303|PubMed:1692213,
FT ECO:0000303|PubMed:8345193"
FT /id="VSP_002639"
FT VAR_SEQ 273..301
FT /note="GEYSVVFGGSMMSCPGLPDGLEPARTDLS -> A (in isoform 2R-
FT B2)"
FT /evidence="ECO:0000303|PubMed:8345193"
FT /id="VSP_002638"
FT CONFLICT 114
FT /note="Q -> QVLPSYRFTAKGNDSGEYRCQ (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 37091 MW; 5137E3271D443B84 CRC64;
MAIPSFLPVL GTKSHRADYK PLQTLSHMLL WITVLFLAPV AGTSADPPKA VVRLEPPWIQ
VLRGDRVTLT CEGAPSPGNH STQWLHNGRL IPTQVLPSYR FTAKGNDSGE YRCQAGGTSL
SDPVRLDVIS DWLVLQTSQL IFQEGDVIVL RCHSWNNWPL AKVTFYHNGV AKKYFSISKN
FSIPQANHSH SGAYNCTGLI GRTSHTSPPV TITVQGPKSS DSSMVVIIVA AVIGIATAAI
VVAVVAIICL KKKQPPGNPE HREMGETLPE DPGEYSVVFG GSMMSCPGLP DGLEPARTDL
SNLSDPEEVA KSEVENTITY SLLKHPEAQD DDTEHDYQNH I
