FCG3A_MOUSE
ID FCG3A_MOUSE Reviewed; 249 AA.
AC A0A0B4J1G0; Q3TC44; Q8R2R4; Q8R477;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 53.
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:0000303|PubMed:12389094};
DE AltName: Full=FcgammaRIV {ECO:0000303|PubMed:16039578};
DE AltName: CD_antigen=CD16a;
DE Flags: Precursor;
GN Name=Fcgr4 {ECO:0000303|PubMed:17558411, ECO:0000312|MGI:MGI:2179523};
GN Synonyms=Fcgr3a {ECO:0000303|PubMed:17558411};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAM19249.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAM19249.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAM19249.1};
RX PubMed=12389094; DOI=10.1007/s00251-002-0486-0;
RA Mechetina L.V., Najakshin A.M., Alabyev B.Y., Chikaev N.A., Taranin A.V.;
RT "Identification of CD16-2, a novel mouse receptor homologous to CD16/Fc
RT gamma RIII.";
RL Immunogenetics 54:463-468(2002).
RN [2] {ECO:0000312|EMBL:ABS89131.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NOD/LtJ {ECO:0000312|EMBL:ABS89131.1};
RX PubMed=18292508; DOI=10.4049/jimmunol.180.5.2863;
RA Xiu Y., Wong C.P., Bouaziz J.D., Hamaguchi Y., Wang Y., Pop S.M.,
RA Tisch R.M., Tedder T.F.;
RT "B lymphocyte depletion by CD20 monoclonal antibody prevents diabetes in
RT nonobese diabetic mice despite isotype-specific differences in Fc gamma R
RT effector functions.";
RL J. Immunol. 180:2863-2875(2008).
RN [3] {ECO:0000312|EMBL:BAE42113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD {ECO:0000312|EMBL:BAE42113.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE42113.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000312|EMBL:EDL39140.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000312|EMBL:AAH27310.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH27310.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH27310.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
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 [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FCER1G, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=16039578; DOI=10.1016/j.immuni.2005.05.010;
RA Nimmerjahn F., Bruhns P., Horiuchi K., Ravetch J.V.;
RT "FcgammaRIV: a novel FcR with distinct IgG subclass specificity.";
RL Immunity 23:41-51(2005).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FCERG, TISSUE SPECIFICITY, INDUCTION,
RP PHOSPHORYLATION AT TYR-235, AND MUTAGENESIS OF TYR-235.
RX PubMed=17558411; DOI=10.1038/ni1477;
RA Hirano M., Davis R.S., Fine W.D., Nakamura S., Shimizu K., Yagi H.,
RA Kato K., Stephan R.P., Cooper M.D.;
RT "IgEb immune complexes activate macrophages through FcgammaRIV binding.";
RL Nat. Immunol. 8:762-771(2007).
RN [10] {ECO:0000305}
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=18949059; DOI=10.1172/jci36452;
RA Mancardi D.A., Iannascoli B., Hoos S., England P., Daeron M., Bruhns P.;
RT "FcgammaRIV is a mouse IgE receptor that resembles macrophage FcepsilonRI
RT in humans and promotes IgE-induced lung inflammation.";
RL J. Clin. Invest. 118:3738-3750(2008).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=18097064; DOI=10.4049/jimmunol.180.1.618;
RA Jakus Z., Nemeth T., Verbeek J.S., Mocsai A.;
RT "Critical but overlapping role of FcgammaRIII and FcgammaRIV in activation
RT of murine neutrophils by immobilized immune complexes.";
RL J. Immunol. 180:618-629(2008).
RN [12] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19795417; DOI=10.1002/eji.200939884;
RA Syed S.N., Konrad S., Wiege K., Nieswandt B., Nimmerjahn F., Schmidt R.E.,
RA Gessner J.E.;
RT "Both FcgammaRIV and FcgammaRIII are essential receptors mediating type II
RT and type III autoimmune responses via FcRgamma-LAT-dependent generation of
RT C5a.";
RL Eur. J. Immunol. 39:3343-3356(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-235, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [14]
RP FUNCTION.
RX PubMed=24412922; DOI=10.1038/nm.3443;
RA DiLillo D.J., Tan G.S., Palese P., Ravetch J.V.;
RT "Broadly neutralizing hemagglutinin stalk-specific antibodies require
RT FcgammaR interactions for protection against influenza virus in vivo.";
RL Nat. Med. 20:143-151(2014).
RN [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=25824719; DOI=10.1038/ncomms7637;
RA Negishi-Koga T., Gober H.J., Sumiya E., Komatsu N., Okamoto K., Sawa S.,
RA Suematsu A., Suda T., Sato K., Takai T., Takayanagi H.;
RT "Immune complexes regulate bone metabolism through FcRgamma signalling.";
RL Nat. Commun. 6:6637-6637(2015).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28389502; DOI=10.1084/jem.20160951;
RA Lehmann C.H.K., Baranska A., Heidkamp G.F., Heger L., Neubert K.,
RA Luehr J.J., Hoffmann A., Reimer K.C., Brueckner C., Beck S., Seeling M.,
RA Kiessling M., Soulat D., Krug A.B., Ravetch J.V., Leusen J.H.W.,
RA Nimmerjahn F., Dudziak D.;
RT "DC subset-specific induction of T cell responses upon antigen uptake via
RT Fcgamma receptors in vivo.";
RL J. Exp. Med. 214:1509-1528(2017).
RN [17]
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) (PubMed:16039578). Binds with intermediate affinity to both
CC IgG2a and IgG2b (PubMed:16039578, PubMed:17558411, PubMed:19795417).
CC Can bind to IgG2a and IgG2b monomers (PubMed:18949059). Does not
CC display binding to IgG1 or IgG3 (PubMed:16039578). Recognizes
CC neutralizing virus-specific IgGs displayed on the cell surface of
CC infected cells and triggers antibody-dependent cellular cytotoxicity
CC (ADCC). Confers protection to lethal influenza virus infection
CC (PubMed:24412922). On splenic dendritic cells, uptakes antigen immune
CC complexes and efficiently divert them into MHC class I and II antigen
CC presentation pathways to provide for superior priming of CD4-positive
CC and CD8-positive T cell immune responses (PubMed:28389502). Mediates
CC neutrophil activation by IgG complexes redundantly with FCGR2A
CC (PubMed:18097064). Plays a role in promoting bone resorption by
CC enhancing osteoclast differentiation following binding to IgG2a
CC (PubMed:25824719). Also acts as a receptor for the Fc region of
CC immunoglobulin epsilon (IgE) (PubMed:17558411, PubMed:18949059). Binds
CC with low affinity to both the a and b allotypes of IgE
CC (PubMed:18949059). Has also been shown to bind to IgE allotype a only
CC but not to allotype b (PubMed:17558411). Binds aggregated IgE but not
CC the monomeric form and bound monomeric IgG is readily displaced by IgE
CC complexes (PubMed:18949059). Binding to IgE promotes macrophage-
CC mediated phagocytosis, antigen presentation to T cells, production of
CC pro-inflammatory cytokines and the late phase of cutaneous allergic
CC reactions (PubMed:17558411, PubMed:18949059). Mediates enhanced ADCC in
CC response to afucosylated IgGs (PubMed:34485821).
CC {ECO:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411,
CC ECO:0000269|PubMed:18097064, ECO:0000269|PubMed:18949059,
CC ECO:0000269|PubMed:19795417, ECO:0000269|PubMed:24412922,
CC ECO:0000269|PubMed:25824719, ECO:0000269|PubMed:28389502,
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:0000269|PubMed:16039578, ECO:0000269|PubMed:17558411}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16039578,
CC ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:28389502}; Single-pass
CC type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected on myeloid cells, peripheral blood
CC monocytes, splenic and bone marrow dendritic cells, and thioglycollate-
CC elicited macrophages and neutrophils but absent from lymphoid
CC populations with no expression observed on T cells, B cells, NK cells
CC or other granulocytes (at protein level) (PubMed:16039578,
CC PubMed:19795417). Expressed in peripheral blood leukocytes, spleen,
CC liver, thymus and small intestine (PubMed:12389094, PubMed:17558411).
CC Expressed in splenic dendritic cell subsets (at protein level).
CC {ECO:0000269|PubMed:12389094, ECO:0000269|PubMed:16039578,
CC ECO:0000269|PubMed:17558411, ECO:0000269|PubMed:19795417,
CC ECO:0000269|PubMed:28389502}.
CC -!- INDUCTION: By lipopolysaccharide, interferon beta and IFNG.
CC {ECO:0000269|PubMed:17558411}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16039578,
CC ECO:0000269|PubMed:18949059}.
CC -!- PTM: Phosphorylated following receptor ligation.
CC {ECO:0000269|PubMed:17558411}.
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; AF499613; AAM19249.1; -; mRNA.
DR EMBL; EU050648; ABS89131.1; -; mRNA.
DR EMBL; AK170920; BAE42113.1; -; mRNA.
DR EMBL; AC115959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39140.1; -; Genomic_DNA.
DR EMBL; BC027310; AAH27310.1; -; mRNA.
DR CCDS; CCDS15476.1; -.
DR RefSeq; NP_653142.2; NM_144559.2.
DR AlphaFoldDB; A0A0B4J1G0; -.
DR SMR; A0A0B4J1G0; -.
DR STRING; 10090.ENSMUSP00000077873; -.
DR GlyGen; A0A0B4J1G0; 3 sites.
DR iPTMnet; A0A0B4J1G0; -.
DR PhosphoSitePlus; A0A0B4J1G0; -.
DR PaxDb; A0A0B4J1G0; -.
DR ProteomicsDB; 271732; -.
DR DNASU; 246256; -.
DR Ensembl; ENSMUST00000078825; ENSMUSP00000077873; ENSMUSG00000059089.
DR GeneID; 246256; -.
DR KEGG; mmu:246256; -.
DR UCSC; uc007dmw.2; mouse.
DR CTD; 246256; -.
DR MGI; MGI:2179523; Fcgr4.
DR VEuPathDB; HostDB:ENSMUSG00000059089; -.
DR eggNOG; ENOG502RU1M; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_1_0_1; -.
DR OMA; GDNSTQW; -.
DR OrthoDB; 866496at2759; -.
DR PhylomeDB; A0A0B4J1G0; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2029481; FCGR activation.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR BioGRID-ORCS; 246256; 1 hit in 75 CRISPR screens.
DR PRO; PR:A0A0B4J1G0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; A0A0B4J1G0; protein.
DR Bgee; ENSMUSG00000059089; Expressed in granulocyte and 35 other tissues.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0033001; C:Fc-gamma receptor III complex; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0034235; F:GPI anchor binding; ISO:MGI.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0019767; F:IgE receptor activity; IDA:UniProtKB.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0019770; F:IgG receptor activity; IDA:UniProtKB.
DR GO; GO:0140375; F:immune receptor activity; ISO:MGI.
DR GO; GO:0019772; F:low-affinity IgG receptor activity; ISO:MGI.
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:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0002468; P:dendritic cell antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0160006; P:Fc receptor-mediated immune complex endocytosis; IDA:UniProtKB.
DR GO; GO:0042119; P:neutrophil activation; IMP:UniProtKB.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:UniProtKB.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
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 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; IgE-binding protein;
KW IgG-binding protein; Immunity; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW 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_5008204824"
FT TOPO_DOM 21..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 22..102
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 119..188
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT SITE 217
FT /note="Important for receptor turnover"
FT /evidence="ECO:0000250|UniProtKB:P08637"
FT MOD_RES 235
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17558411,
FT ECO:0007744|PubMed:19144319"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
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 46..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 127..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 235
FT /note="Y->W: Abolishes receptor ligation-induced
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:17558411"
FT CONFLICT 57
FT /note="I -> T (in Ref. 2; ABS89131 and 3; BAE42113)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="L -> S (in Ref. 6; AAH27310)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="L -> P (in Ref. 1; AAM19249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 28398 MW; 99BBA7992862E80C CRC64;
MWQLLLPTAL VLTAFSGIQA GLQKAVVNLD PKWVRVLEED SVTLRCQGTF SPEDNSIKWF
HNESLIPHQD ANYVIQSARV KDSGMYRCQT ALSTISDPVQ LEVHMGWLLL QTTKWLFQEG
DPIHLRCHSW QNRPVRKVTY LQNGKGKKYF HENSELLIPK ATHNDSGSYF CRGLIGHNNK
SSASFRISLG DPGSPSMFPP WHQITFCLLI GLLFAIDTVL YFSVRRGLQS PVADYEEPKI
QWSKEPQDK
