FCG3A_RABIT
ID FCG3A_RABIT Reviewed; 253 AA.
AC G1TR84;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 3.
DT 03-AUG-2022, entry version 56.
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=FcgammaRIIIA {ECO:0000303|PubMed:34485821};
DE AltName: CD_antigen=CD16a;
DE Flags: Precursor;
GN Name=FCGR3A {ECO:0000250|UniProtKB:P08637};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke;
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2]
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 [3]
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) (By similarity). Optimally activated upon binding of
CC clustered antigen-IgG complexes displayed on cell surfaces, triggers
CC lysis of antibody-coated cells, a process known as antibody-dependent
CC cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus
CC avoiding inappropriate effector cell activation in the absence of
CC antigenic trigger. Mediates IgG effector functions on natural killer
CC (NK) cells. Binds antigen-IgG complexes generated upon infection and
CC triggers NK cell-dependent cytokine production and degranulation to
CC limit viral load and propagation (By similarity). Fc-binding subunit
CC that associates with FCER1G adapter to form functional signaling
CC complexes. Following the engagement of antigen-IgG complexes, triggers
CC phosphorylation of immunoreceptor tyrosine-based activation motif
CC (ITAM)-containing adapters with subsequent activation of
CC phosphatidylinositol 3-kinase signaling and sustained elevation of
CC intracellular calcium that ultimately drive NK cell activation (By
CC similarity). Mediates enhanced ADCC in response to afucosylated IgGs
CC (PubMed:34485821). {ECO:0000250|UniProtKB:A0A0B4J1G0,
CC ECO:0000250|UniProtKB:P08637, ECO:0000250|UniProtKB:Q28942,
CC 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:P08637}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08637};
CC Single-pass membrane protein {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAGW02000249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002715293.1; XM_002715247.3.
DR STRING; 9986.ENSOCUP00000019538; -.
DR Ensembl; ENSOCUT00000024322; ENSOCUP00000019538; ENSOCUG00000024349.
DR GeneID; 100337909; -.
DR KEGG; ocu:100337909; -.
DR eggNOG; ENOG502RU1M; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_1_0_1; -.
DR InParanoid; G1TR84; -.
DR OrthoDB; 866496at2759; -.
DR TreeFam; TF335097; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000024349; Expressed in blood and 20 other tissues.
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 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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; IgG-binding protein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..253
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-A"
FT /evidence="ECO:0000255"
FT /id="PRO_5023820611"
FT TOPO_DOM 21..207
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 24..90
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 99..189
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT SITE 221
FT /note="Important for receptor turnover"
FT /evidence="ECO:0000250|UniProtKB:P08637"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 47..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 128..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 253 AA; 27902 MW; F17684F6B0F6C55B CRC64;
MGQPLPPVAL LLLVSASSRA ADVPKALVLL DPPWASVLKD DHVTLKCQGL HPAGDNTTQW
LHNGSLLSSQ APAYTITAAR AEDGGEYRCQ TGLSSLSDPV QLHVHLGWLV LQAPRWVFQE
GEPIQLRCHS WKNNKLHKVT YLQNGRGLRY FHQNSDLHIP EATRNHSGSY FCRGLIGHHN
MSSETVTITV QGPANPVISS SVLPWHQIAF CLVMGLLLAA DTGLYFSVQR DLRSSQRARK
EHTLGWSLGS QDK
