FCG3A_CRIGR
ID FCG3A_CRIGR Reviewed; 275 AA.
AC P0DTI4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-A {ECO:0000250|UniProtKB:P08637};
DE Short=IgG Fc receptor III-A;
DE AltName: Full=CD16-2 {ECO:0000250|UniProtKB:A0A0B4J1G0};
DE AltName: Full=FcgammaRIV {ECO:0000303|PubMed:34485821};
DE AltName: CD_antigen=CD16a;
DE Flags: Precursor;
GN Name=FCGR3A {ECO:0000250|UniProtKB:P08637};
GN Synonyms=FCGR4 {ECO:0000303|PubMed:34485821};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29704459; DOI=10.1002/bit.26722;
RA Rupp O., MacDonald M.L., Li S., Dhiman H., Polson S., Griep S., Heffner K.,
RA Hernandez I., Brinkrolf K., Jadhav V., Samoudi M., Hao H., Kingham B.,
RA Goesmann A., Betenbaugh M.J., Lewis N.E., Borth N., Lee K.H.;
RT "A reference genome of the Chinese hamster based on a hybrid assembly
RT strategy.";
RL Biotechnol. Bioeng. 115:2087-2100(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=32410221; DOI=10.1002/bit.27432;
RA Hilliard W., MacDonald M.L., Lee K.H.;
RT "Chromosome-scale scaffolds for the Chinese hamster reference genome
RT assembly to facilitate the study of the CHO epigenome.";
RL Biotechnol. Bioeng. 117:2331-2339(2020).
RN [3]
RP NOMENCLATURE.
RX PubMed=7955033;
RA Conrad D., Cooper M., Fridman W.H., Kinet J.P., Ravetch J.;
RT "Nomenclature of Fc receptors. IUIS/WHO Subcommittee on Nomenclature of Fc
RT receptors.";
RL Bull. World Health Organ. 72:809-810(1994).
RN [4]
RP FUNCTION.
RX PubMed=34485821; DOI=10.1093/abt/tbab016;
RA Mao C., Near R., Zhong X., Gao W.;
RT "Cross-species higher sensitivities of FcgammaRIIIA/FcgammaRIV to
RT afucosylated IgG for enhanced ADCC.";
RL Antib Ther 4:159-170(2021).
CC -!- FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin
CC gamma (IgG). Binds with intermediate affinity to both IgG2a and IgG2b.
CC Can bind to IgG2a and IgG2b monomers. Does not display binding to IgG1
CC or IgG3 (By similarity). Recognizes neutralizing virus-specific IgGs
CC displayed on the cell surface of infected cells and triggers antibody-
CC dependent cellular cytotoxicity (ADCC). Confers protection to lethal
CC influenza virus infection (By similarity). On splenic dendritic cells,
CC uptakes antigen immune complexes and efficiently divert them into MHC
CC class I and II antigen presentation pathways to provide for superior
CC priming of CD4-positive and CD8-positive T cell immune responses (By
CC similarity). Mediates neutrophil activation by IgG complexes
CC redundantly with FCGR2A (By similarity). Plays a role in promoting bone
CC resorption by enhancing osteoclast differentiation following binding to
CC IgG2a (By similarity). Also acts as a receptor for the Fc region of
CC immunoglobulin epsilon (IgE). Binds with low affinity to both the a and
CC b allotypes of IgE. Has also been shown to bind to IgE allotype a only
CC but not to allotype b. Binds aggregated IgE but not the monomeric form
CC and bound monomeric IgG is readily displaced by IgE complexes. Binding
CC to IgE promotes macrophage-mediated phagocytosis, antigen presentation
CC to T cells, production of pro-inflammatory cytokines and the late phase
CC of cutaneous allergic reactions (By similarity). Mediates enhanced ADCC
CC in response to afucosylated IgGs (PubMed:34485821).
CC {ECO:0000250|UniProtKB:A0A0B4J1G0, ECO:0000269|PubMed:34485821}.
CC -!- SUBUNIT: Forms a heterooligomeric complex with ITAM-containing
CC signaling subunits FCER1G. Interacts (via transmembrane domain) with
CC signaling subunits; this interaction is a prerequisite for receptor
CC complex expression on the cell surface and intracellular signal
CC transduction. Binds the Fc region of antigen-complexed IgG.
CC {ECO:0000250|UniProtKB:A0A0B4J1G0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0A0B4J1G0};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:A0A0B4J1G0}.
CC -!- PTM: Phosphorylated following receptor ligation.
CC {ECO:0000250|UniProtKB:A0A0B4J1G0}.
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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:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; 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 InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; IgE-binding protein;
KW IgG-binding protein; Immunity; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..275
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-A"
FT /id="PRO_0000454796"
FT TOPO_DOM 24..207
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 28..92
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 101..192
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 237..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A0A0B4J1G0"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 49..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 131..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 275 AA; 31183 MW; 2C6BD1C6AE335A62 CRC64;
MSVWTSRKAA EDNDTSLSSG IRAGLQKAVV TLHPEWVRVL QDDSVTLRCQ GTYPPGDNST
KWFHNGSLTL QQDANYLIGS AKVKDSGEYT CQTALSMLSD PVNLEVHIGW LLLQTTQRPV
FREGDPIRLN CHSWRNTPVY KVTYLQNGKG KKYFHKNSEL HIPNATQNHS GSYFCRGIIG
RNNKSSETLR ITVGDLTSPS TFPPWHQITF CLLIGLLFTI DTVMYFSVQK GLRRSTADYE
EPEVHWSKEP ENKTISEEKQ SFRSSRANSE TPENR
