FCG3A_CANLF
ID FCG3A_CANLF Reviewed; 249 AA.
AC E2RP87;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
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}; OrderedLocusNames=LOC478984;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
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 adapters 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}.
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DR EMBL; AAEX03018435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_536141.3; XM_536141.4.
DR SMR; E2RP87; -.
DR STRING; 9612.ENSCAFP00000019180; -.
DR PaxDb; E2RP87; -.
DR Ensembl; ENSCAFT00030038120; ENSCAFP00030033256; ENSCAFG00030020788.
DR Ensembl; ENSCAFT00040023409; ENSCAFP00040020309; ENSCAFG00040012704.
DR eggNOG; ENOG502RU1M; Eukaryota.
DR HOGENOM; CLU_023383_1_0_1; -.
DR InParanoid; E2RP87; -.
DR OMA; GDNSTQW; -.
DR OrthoDB; 866496at2759; -.
DR TreeFam; TF335097; -.
DR Proteomes; UP000002254; Chromosome 38.
DR Bgee; ENSCAFG00000013015; Expressed in cartilage tissue and 46 other tissues.
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 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..249
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000454788"
FT TOPO_DOM 21..206
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 24..104
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 119..172
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT SITE 220
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 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 47..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 127..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 249 AA; 28010 MW; D38330C25AE96DCF CRC64;
MWQLVSSTAL LLLVSAGTQA ADVPKAVVVL EPKWNRVLTM DSVTLKCQGD HLLRDNYTWL
HNGRPISNQI STYIIKNASI KNSGEYRCQT DQSKLSDPVQ LEVHTGWLLL QVPRLVFQEG
ELIQLKCHSW KNTPVRNVQY FQNGRGKKFF YNNSEYHIPA ATSEHNGSYF CRGIIGKKNE
SSEAVNIIIQ GSSLPSTSLL LSHWPQIPFS LVMALLFAVD TGLYFAVQRD LRSSMGNLKN
SKVIWSQGS
