FCG3A_HUMAN
ID FCG3A_HUMAN Reviewed; 254 AA.
AC P08637; A2N6W9; Q53FJ0; Q53FL6; Q5EBR4; Q65ZM6; Q6PIJ0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-A {ECO:0000303|PubMed:7836402};
DE Short=IgG Fc receptor III-A;
DE AltName: Full=CD16-II {ECO:0000303|PubMed:1825220, ECO:0000303|PubMed:2532305};
DE AltName: Full=CD16a antigen;
DE AltName: Full=Fc-gamma RIII-alpha;
DE Short=Fc-gamma RIII;
DE Short=Fc-gamma RIIIa;
DE Short=FcRIII;
DE Short=FcRIIIa;
DE Short=FcgammaRIIIA {ECO:0000303|PubMed:28126818};
DE AltName: Full=FcR-10;
DE AltName: Full=IgG Fc receptor III-2;
DE AltName: CD_antigen=CD16a {ECO:0000303|PubMed:25816339};
DE Flags: Precursor;
GN Name=FCGR3A {ECO:0000303|PubMed:23006327};
GN Synonyms=CD16A {ECO:0000303|PubMed:25816339}, FCG3, FCGR3, IGFR3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2526846; DOI=10.1084/jem.170.2.481;
RA Ravetch J.V., Perussia B.;
RT "Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer
RT cells and neutrophils. Cell type-specific expression of two genes that
RT differ in single nucleotide substitutions.";
RL J. Exp. Med. 170:481-497(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=16951347; DOI=10.4049/jimmunol.177.6.3848;
RA Rogers K.A., Scinicariello F., Attanasio R.;
RT "IgG Fc receptor III homologues in nonhuman primate species: genetic
RT characterization and ligand interactions.";
RL J. Immunol. 177:3848-3856(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-176.
RC TISSUE=Synovium;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-176.
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC TISSUE=Placenta;
RX PubMed=7836402; DOI=10.1074/jbc.270.3.1350;
RA Gessner J.E., Grussenmeyer T., Kolanus W., Schmidt R.E.;
RT "The human low affinity immunoglobulin G Fc receptor III-A and III-B genes.
RT Molecular characterization of the promoter regions.";
RL J. Biol. Chem. 270:1350-1361(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-254, AND VARIANT VAL-176.
RX PubMed=7700021; DOI=10.1038/ki.1994.462;
RA Morcos M., Hansch G.M., Schonermark M., Ellwanger S., Harle M.,
RA Heckl-Ostreicher B.;
RT "Human glomerular mesangial cells express CD16 and may be stimulated via
RT this receptor.";
RL Kidney Int. 46:1627-1634(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-254.
RC TISSUE=Lung;
RX PubMed=2525780; DOI=10.1073/pnas.86.13.5079;
RA Scallon B.J., Scigliano E., Freedman V.H., Miedel M.C., Pan Y.C.,
RA Unkeless J.C., Kochan J.P.;
RT "A human immunoglobulin G receptor exists in both polypeptide-anchored and
RT phosphatidylinositol-glycan-anchored forms.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5079-5083(1989).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH CD247, AND SUBCELLULAR LOCATION.
RX PubMed=2532305; DOI=10.1038/342803a0;
RA Lanier L.L., Yu G., Phillips J.H.;
RT "Co-association of CD3 zeta with a receptor (CD16) for IgG Fc on human
RT natural killer cells.";
RL Nature 342:803-805(1989).
RN [10]
RP FUNCTION, SUBUNIT, INTERACTION WITH CD247 AND FCER1G, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF PHE-203, AND VARIANT SER-203.
RX PubMed=1825220;
RA Lanier L.L., Yu G., Phillips J.H.;
RT "Analysis of Fc gamma RIII (CD16) membrane expression and association with
RT CD3 zeta and Fc epsilon RI-gamma by site-directed mutation.";
RL J. Immunol. 146:1571-1576(1991).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=9916693;
RA Warren H.S., Kinnear B.F.;
RT "Quantitative analysis of the effect of CD16 ligation on human NK cell
RT proliferation.";
RL J. Immunol. 162:735-742(1999).
RN [13]
RP FUNCTION.
RX PubMed=10318937; DOI=10.1073/pnas.96.10.5640;
RA Mandelboim O., Malik P., Davis D.M., Jo C.H., Boyson J.E., Strominger J.L.;
RT "Human CD16 as a lysis receptor mediating direct natural killer cell
RT cytotoxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5640-5644(1999).
RN [14]
RP FUNCTION, AND INTERACTION WITH IGHG1.
RX PubMed=11711607; DOI=10.1128/jvi.75.24.12161-12168.2001;
RA Hezareh M., Hessell A.J., Jensen R.C., van de Winkel J.G., Parren P.W.;
RT "Effector function activities of a panel of mutants of a broadly
RT neutralizing antibody against human immunodeficiency virus type 1.";
RL J. Virol. 75:12161-12168(2001).
RN [15]
RP FUNCTION, INTERACTION WITH S100A4, PHOSPHORYLATION AT SER-236 AND THR-237,
RP AND MUTAGENESIS OF 249-LYS--LYS-254 AND 235-SER--THR-237.
RX PubMed=23024279; DOI=10.4049/jimmunol.1200704;
RA Li X., Baskin J.G., Mangan E.K., Su K., Gibson A.W., Ji C., Edberg J.C.,
RA Kimberly R.P.;
RT "The unique cytoplasmic domain of human FcgammaRIIIA regulates receptor-
RT mediated function.";
RL J. Immunol. 189:4284-4294(2012).
RN [16]
RP PTM, SITE, AND SUBCELLULAR LOCATION.
RX PubMed=24337742; DOI=10.4049/jimmunol.1301024;
RA Lajoie L., Congy-Jolivet N., Bolzec A., Gouilleux-Gruart V., Sicard E.,
RA Sung H.C., Peiretti F., Moreau T., Vie H., Clemenceau B., Thibault G.;
RT "ADAM17-mediated shedding of FcgammaRIIIA on human NK cells: identification
RT of the cleavage site and relationship with activation.";
RL J. Immunol. 192:741-751(2014).
RN [17]
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 [18]
RP FUNCTION.
RX PubMed=25786175; DOI=10.1016/j.immuni.2015.02.013;
RA Lee J., Zhang T., Hwang I., Kim A., Nitschke L., Kim M., Scott J.M.,
RA Kamimura Y., Lanier L.L., Kim S.;
RT "Epigenetic modification and antibody-dependent expansion of memory-like NK
RT cells in human cytomegalovirus-infected individuals.";
RL Immunity 42:431-442(2015).
RN [19]
RP FUNCTION, PTM, SITE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-197.
RX PubMed=25816339; DOI=10.1371/journal.pone.0121788;
RA Jing Y., Ni Z., Wu J., Higgins L., Markowski T.W., Kaufman D.S.,
RA Walcheck B.;
RT "Identification of an ADAM17 cleavage region in human CD16 (FcgammaRIII)
RT and the engineering of a non-cleavable version of the receptor in NK
RT cells.";
RL PLoS ONE 10:e0121788-e0121788(2015).
RN [20]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=27670158; DOI=10.1038/srep34310;
RA Yeap W.H., Wong K.L., Shimasaki N., Teo E.C., Quek J.K., Yong H.X.,
RA Diong C.P., Bertoletti A., Linn Y.C., Wong S.C.;
RT "CD16 is indispensable for antibody-dependent cellular cytotoxicity by
RT human monocytes.";
RL Sci. Rep. 6:34310-34310(2016).
RN [21]
RP FUNCTION, INTERACTION WITH CD247 AND FCER1G, SUBCELLULAR LOCATION, SITE,
RP AND MUTAGENESIS OF GLN-208; SER-210; PHE-211; CYS-212; PHE-219; ASP-222;
RP THR-223; TYR-226; PHE-227 AND SER-228.
RX PubMed=28652325; DOI=10.1073/pnas.1706483114;
RA Blazquez-Moreno A., Park S., Im W., Call M.J., Call M.E., Reyburn H.T.;
RT "Transmembrane features governing Fc receptor CD16A assembly with CD16A
RT signaling adaptor molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E5645-E5654(2017).
RN [22]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=28126818; DOI=10.1126/science.aai8128;
RA Wang T.T., Sewatanon J., Memoli M.J., Wrammert J., Bournazos S.,
RA Bhaumik S.K., Pinsky B.A., Chokephaibulkit K., Onlamoon N.,
RA Pattanapanyasat K., Taubenberger J.K., Ahmed R., Ravetch J.V.;
RT "IgG antibodies to dengue enhanced for FcgammaRIIIA binding determine
RT disease severity.";
RL Science 355:395-398(2017).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, PTM, AND MUTAGENESIS OF SER-197.
RX PubMed=29967280; DOI=10.1083/jcb.201712085;
RA Srpan K., Ambrose A., Karampatzakis A., Saeed M., Cartwright A.N.R.,
RA Guldevall K., De Matos G.D.S.C., Oenfelt B., Davis D.M.;
RT "Shedding of CD16 disassembles the NK cell immune synapse and boosts serial
RT engagement of target cells.";
RL J. Cell Biol. 217:3267-3283(2018).
RN [24]
RP MISCELLANEOUS.
RX PubMed=31244843; DOI=10.3389/fimmu.2019.01297;
RA Lejeune J., Brachet G., Watier H.;
RT "Evolutionary Story of the Low/Medium-Affinity IgG Fc Receptor Gene
RT Cluster.";
RL Front. Immunol. 10:1297-1297(2019).
RN [25]
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).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-193 IN COMPLEX WITH IGHG1,
RP FUNCTION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-63 AND ASN-180.
RX PubMed=22023369; DOI=10.1111/j.1365-2443.2011.01552.x;
RA Mizushima T., Yagi H., Takemoto E., Shibata-Koyama M., Isoda Y., Iida S.,
RA Masuda K., Satoh M., Kato K.;
RT "Structural basis for improved efficacy of therapeutic antibodies on
RT defucosylation of their Fc glycans.";
RL Genes Cells 16:1071-1080(2011).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-208 IN COMPLEX WITH IGHG1,
RP FUNCTION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-63 AND ASN-180.
RX PubMed=21768335; DOI=10.1073/pnas.1108455108;
RA Ferrara C., Grau S., Jager C., Sondermann P., Brunker P., Waldhauer I.,
RA Hennig M., Ruf A., Rufer A.C., Stihle M., Umana P., Benz J.;
RT "Unique carbohydrate-carbohydrate interactions are required for high
RT affinity binding between FcgammaRIII and antibodies lacking core fucose.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12669-12674(2011).
RN [28]
RP INVOLVEMENT IN IMD20, VARIANT IMD20 HIS-66, VARIANT ARG-66, FUNCTION, AND
RP SUBUNIT.
RX PubMed=8609432;
RA de Haas M., Koene H.R., Kleijer M., de Vries E., Simsek S., van Tol M.J.D.,
RA Roos D., von dem Borne A.E.G.K.;
RT "A triallelic Fc gamma receptor type IIIA polymorphism influences the
RT binding of human IgG by NK cell Fc gamma RIIIa.";
RL J. Immunol. 156:2948-2955(1996).
RN [29]
RP VARIANT VAL-176, FUNCTION, AND SUBUNIT.
RX PubMed=9242542;
RA Koene H.R., Kleijer M., Algra J., Roos D., von dem Borne A.E.G.K.,
RA de Haas M.;
RT "Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by natural
RT killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-48L/R/H
RT phenotype.";
RL Blood 90:1109-1114(1997).
RN [30]
RP VARIANT VAL-176.
RX PubMed=9276722; DOI=10.1172/jci119616;
RA Wu J., Edberg J.C., Redecha P.B., Bansal V., Guyre P.M., Coleman K.,
RA Salmon J.E., Kimberly R.P.;
RT "A novel polymorphism of FcgammaRIIIa (CD16) alters receptor function and
RT predisposes to autoimmune disease.";
RL J. Clin. Invest. 100:1059-1070(1997).
RN [31]
RP INVOLVEMENT IN IMD20, AND VARIANT IMD20 HIS-66.
RX PubMed=8874200;
RA de Vries E., Koene H.R., Vossen J.M., Gratama J.W., von dem Borne A.E.,
RA Waaijer J.L., Haraldsson A., de Haas M., van Tol M.J.;
RT "Identification of an unusual Fc gamma receptor IIIa (CD16) on natural
RT killer cells in a patient with recurrent infections.";
RL Blood 88:3022-3027(1996).
RN [32]
RP VARIANT IMD20 HIS-66.
RX PubMed=8608639; DOI=10.1111/j.1365-2249.1996.tb08295.x;
RA Jawahar S., Moody C., Chan M., Finberg R., Geha R., Chatila T.;
RT "Natural Killer (NK) cell deficiency associated with an epitope-deficient
RT Fc receptor type IIIA (CD16-II).";
RL Clin. Exp. Immunol. 103:408-413(1996).
RN [33]
RP VARIANT IMD20 HIS-66, FUNCTION, INTERACTION WITH CD2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23006327; DOI=10.1172/jci64837;
RA Grier J.T., Forbes L.R., Monaco-Shawver L., Oshinsky J., Atkinson T.P.,
RA Moody C., Pandey R., Campbell K.S., Orange J.S.;
RT "Human immunodeficiency-causing mutation defines CD16 in spontaneous NK
RT cell cytotoxicity.";
RL J. Clin. Invest. 122:3769-3780(2012).
CC -!- FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin
CC gamma (IgG). Optimally activated upon binding of clustered antigen-IgG
CC complexes displayed on cell surfaces, triggers lysis of antibody-coated
CC cells, a process known as antibody-dependent cellular cytotoxicity
CC (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate
CC effector cell activation in the absence of antigenic trigger
CC (PubMed:24412922, PubMed:25786175, PubMed:21768335, PubMed:22023369,
CC PubMed:8609432, PubMed:9242542, PubMed:25816339, PubMed:11711607,
CC PubMed:28652325). 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. Involved in the generation of memory-
CC like adaptive NK cells capable to produce high amounts of IFNG and to
CC efficiently eliminate virus-infected cells via ADCC (PubMed:25786175,
CC PubMed:24412922). Regulates NK cell survival and proliferation, in
CC particular by preventing NK cell progenitor apoptosis (PubMed:9916693,
CC PubMed:29967280). Fc-binding subunit that associates with CD247 and/or
CC FCER1G adapters to form functional signaling complexes. Following the
CC engagement of antigen-IgG complexes, triggers phosphorylation of
CC immunoreceptor tyrosine-based activation motif (ITAM)-containing
CC adapters with subsequent activation of phosphatidylinositol 3-kinase
CC signaling and sustained elevation of intracellular calcium that
CC ultimately drive NK cell activation. The ITAM-dependent signaling
CC coupled to receptor phosphorylation by PKC mediates robust
CC intracellular calcium flux that leads to production of pro-inflammatory
CC cytokines, whereas in the absence of receptor phosphorylation it mainly
CC activates phosphatidylinositol 3-kinase signaling leading to cell
CC degranulation (PubMed:2532305, PubMed:1825220, PubMed:23024279).
CC Costimulates NK cells and trigger lysis of target cells independently
CC of IgG binding (PubMed:23006327, PubMed:10318937). Mediates the
CC antitumor activities of therapeutic antibodies. Upon ligation on
CC monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells
CC (PubMed:27670158). Mediates enhanced ADCC in response to afucosylated
CC IgGs (PubMed:34485821). {ECO:0000269|PubMed:10318937,
CC ECO:0000269|PubMed:11711607, ECO:0000269|PubMed:1825220,
CC ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:22023369,
CC ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:23024279,
CC ECO:0000269|PubMed:24412922, ECO:0000269|PubMed:2532305,
CC ECO:0000269|PubMed:25786175, ECO:0000269|PubMed:25816339,
CC ECO:0000269|PubMed:27670158, ECO:0000269|PubMed:29967280,
CC ECO:0000269|PubMed:34485821, ECO:0000269|PubMed:8609432,
CC ECO:0000269|PubMed:9242542, ECO:0000269|PubMed:9916693}.
CC -!- FUNCTION: (Microbial infection) Involved in Dengue virus pathogenesis
CC via antibody-dependent enhancement (ADE) mechanism. Secondary infection
CC with Dengue virus triggers elevated levels of afucosylated non-
CC neutralizing IgG1s with reactivity to viral envelope/E protein. Viral
CC antigen-IgG1 complexes bind with high affinity to FCGR3A, facilitating
CC virus entry in myeloid cells and subsequent viral replication.
CC {ECO:0000269|PubMed:28126818}.
CC -!- SUBUNIT: Forms a heterooligomeric complex with ITAM-containing
CC signaling subunits, either a homodimer of CD247, a homodimer of FCER1G
CC or a heterodimer of CD247 and FCER1G (PubMed:2532305, PubMed:1825220,
CC PubMed:28652325). Interacts (via transmembrane domain) with signaling
CC subunits; this interaction is a prerequisite for receptor complex
CC expression on the cell surface and intracellular signal transduction
CC (PubMed:2532305, PubMed:1825220, PubMed:28652325). Binds the Fc region
CC of antigen-complexed IgG with a preference for IgG1 and IgG3 isotypes
CC (PubMed:22023369, PubMed:21768335, PubMed:8609432, PubMed:9242542,
CC PubMed:11711607). Interacts with CD2; this interaction is involved in
CC NK cell activation and cytotoxicity (PubMed:23006327). Interacts with
CC S100A4; this interaction inhibits PKC-dependent phosphorylation of
CC FCGR3A (PubMed:23024279). {ECO:0000269|PubMed:11711607,
CC ECO:0000269|PubMed:1825220, ECO:0000269|PubMed:21768335,
CC ECO:0000269|PubMed:22023369, ECO:0000269|PubMed:23006327,
CC ECO:0000269|PubMed:23024279, ECO:0000269|PubMed:2532305,
CC ECO:0000269|PubMed:8609432, ECO:0000269|PubMed:9242542}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1825220,
CC ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:24337742,
CC ECO:0000269|PubMed:2532305, ECO:0000269|PubMed:28652325,
CC ECO:0000269|PubMed:29967280}; Single-pass type I membrane protein
CC {ECO:0000255}. Secreted {ECO:0000269|PubMed:25816339,
CC ECO:0000269|PubMed:29967280}. Note=Exists also as a soluble receptor.
CC {ECO:0000269|PubMed:25816339, ECO:0000269|PubMed:29967280}.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer cells (at protein
CC level) (PubMed:2526846). Expressed in a subset of circulating monocytes
CC (at protein level) (PubMed:27670158). {ECO:0000269|PubMed:2526846,
CC ECO:0000269|PubMed:27670158}.
CC -!- INDUCTION: Up-regulated in a monocyte subset upon exposure to IL10,
CC TGFB and MCSF. {ECO:0000269|PubMed:27670158}.
CC -!- PTM: Glycosylated. Contains high mannose- and complex-type
CC oligosaccharides. Glycosylation at Asn-180 is mandatory for high
CC affinity binding to the Fc and for discrimination between fucosylated
CC and afucosylated IgG glycoforms. {ECO:0000269|PubMed:21768335,
CC ECO:0000269|PubMed:22023369}.
CC -!- PTM: Undergoes rapid ectodomain shedding upon NK cell stimulation. The
CC soluble form is produced by a proteolytic cleavage mediated by ADAM17.
CC Repeated stimulation causes receptor shedding, a mechanism that allows
CC for increased NK cell motility and detachment from opsonized target
CC cells while avoiding activation-induced NK cell apoptosis.
CC {ECO:0000269|PubMed:24337742, ECO:0000269|PubMed:25816339,
CC ECO:0000269|PubMed:29967280}.
CC -!- PTM: Phosphorylated at RSSTR motif by PKC. The relevant physiological
CC PKCs might be PRKCI, PRKCG, PRKCE, PRKCH and PRKCQ.
CC {ECO:0000269|PubMed:23024279}.
CC -!- DISEASE: Immunodeficiency 20 (IMD20) [MIM:615707]: A rare autosomal
CC recessive primary immunodeficiency characterized by functional
CC deficiency of NK cells. Affected individuals typically present with
CC severe herpes viral infections, particularly Epstein Barr virus (EBV),
CC and human papillomavirus (HPV). {ECO:0000269|PubMed:23006327,
CC ECO:0000269|PubMed:8608639, ECO:0000269|PubMed:8609432,
CC ECO:0000269|PubMed:8874200}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Encoded by one of two nearly indentical genes: FCGR3A
CC (shown here) and FCGR3B which are expressed in a tissue-specific
CC manner. The Phe-203 in III-A determines the transmembrane domains
CC whereas the 'Ser-203' in III-B determines the GPI-anchoring.
CC -!- MISCELLANEOUS: FCGR3A in mammals is the true ortholog of FCGR4 in
CC rodents. The FCGR2A-HSPA6-FCGR4-FCGR2B module was duplicated in great
CC apes through non-allelic homologous recombination, giving rise to two
CC FCGR4-type genes and to FCGR2C, a hybrid gene combining FCGR2A and
CC FCGR2B. While FCGR3A kept the original FCGR4 functionality, FCGR3B
CC rapidly evolved and acquired specific features coding for a GPI-
CC anchored receptor. {ECO:0000269|PubMed:31244843}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD96988.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD97015.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=FCGR3Abase; Note=FCGR3A mutation db;
CC URL="http://structure.bmc.lu.se/idbase/FCGR3Abase/";
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DR EMBL; X52645; CAA36870.1; -; mRNA.
DR EMBL; AK223268; BAD96988.1; ALT_INIT; mRNA.
DR EMBL; AK223295; BAD97015.1; ALT_INIT; mRNA.
DR EMBL; AL590385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017865; AAH17865.1; -; mRNA.
DR EMBL; BC033678; AAH33678.1; -; mRNA.
DR EMBL; Z46222; CAA86295.1; -; Genomic_DNA.
DR EMBL; S76824; AAB33925.2; -; mRNA.
DR EMBL; M24853; AAA53506.1; -; mRNA.
DR CCDS; CCDS1232.2; -.
DR CCDS; CCDS44266.1; -.
DR PIR; JL0107; JL0107.
DR RefSeq; NP_000560.6; NM_000569.7.
DR RefSeq; NP_001121064.2; NM_001127592.2.
DR RefSeq; NP_001121065.1; NM_001127593.1.
DR RefSeq; NP_001121067.1; NM_001127595.1.
DR RefSeq; NP_001121068.1; NM_001127596.1.
DR RefSeq; NP_001316049.1; NM_001329120.1.
DR PDB; 3AY4; X-ray; 2.20 A; C=21-193.
DR PDB; 3SGJ; X-ray; 2.20 A; C=19-208.
DR PDB; 3SGK; X-ray; 2.40 A; C=19-208.
DR PDB; 3WN5; X-ray; 2.78 A; C/F=18-208.
DR PDB; 5BW7; X-ray; 3.00 A; C=21-193.
DR PDB; 5D6D; X-ray; 3.13 A; C=14-205.
DR PDB; 5ML9; X-ray; 2.35 A; A=19-193.
DR PDB; 5MN2; X-ray; 2.35 A; A/B=19-193.
DR PDB; 5VU0; X-ray; 2.26 A; C=22-192.
DR PDB; 5XJE; X-ray; 2.40 A; C=21-193.
DR PDB; 5XJF; X-ray; 2.50 A; C=21-193.
DR PDB; 5YC5; X-ray; 2.71 A; C=19-193.
DR PDB; 7SEG; X-ray; 2.16 A; C/D=16-193.
DR PDBsum; 3AY4; -.
DR PDBsum; 3SGJ; -.
DR PDBsum; 3SGK; -.
DR PDBsum; 3WN5; -.
DR PDBsum; 5BW7; -.
DR PDBsum; 5D6D; -.
DR PDBsum; 5ML9; -.
DR PDBsum; 5MN2; -.
DR PDBsum; 5VU0; -.
DR PDBsum; 5XJE; -.
DR PDBsum; 5XJF; -.
DR PDBsum; 5YC5; -.
DR PDBsum; 7SEG; -.
DR AlphaFoldDB; P08637; -.
DR SMR; P08637; -.
DR BioGRID; 108508; 32.
DR IntAct; P08637; 7.
DR STRING; 9606.ENSP00000356946; -.
DR ChEMBL; CHEMBL3856162; -.
DR DrugBank; DB00092; Alefacept.
DR DrugBank; DB00087; Alemtuzumab.
DR DrugBank; DB16695; Amivantamab.
DR DrugBank; DB12023; Benralizumab.
DR DrugBank; DB00112; Bevacizumab.
DR DrugBank; DB06607; Catumaxomab.
DR DrugBank; DB00002; Cetuximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00056; Gemtuzumab ozogamicin.
DR DrugBank; DB00028; Human immunoglobulin G.
DR DrugBank; DB00110; Palivizumab.
DR DrugBank; DB11767; Sarilumab.
DR GuidetoPHARMACOLOGY; 3017; -.
DR TCDB; 8.A.23.2.6; the basigin (basigin) family.
DR GlyGen; P08637; 6 sites.
DR iPTMnet; P08637; -.
DR PhosphoSitePlus; P08637; -.
DR BioMuta; FCGR3A; -.
DR DMDM; 119876; -.
DR jPOST; P08637; -.
DR MassIVE; P08637; -.
DR PaxDb; P08637; -.
DR PeptideAtlas; P08637; -.
DR PRIDE; P08637; -.
DR ProteomicsDB; 52146; -.
DR TopDownProteomics; P08637; -.
DR ABCD; P08637; 6 sequenced antibodies.
DR Antibodypedia; 20512; 2671 antibodies from 48 providers.
DR DNASU; 2214; -.
DR Ensembl; ENST00000367967.7; ENSP00000356944.3; ENSG00000203747.12.
DR Ensembl; ENST00000436743.6; ENSP00000416607.1; ENSG00000203747.12.
DR Ensembl; ENST00000443193.6; ENSP00000392047.2; ENSG00000203747.12.
DR GeneID; 2214; -.
DR KEGG; hsa:2214; -.
DR MANE-Select; ENST00000443193.6; ENSP00000392047.2; NM_000569.8; NP_000560.7.
DR UCSC; uc001gat.5; human.
DR CTD; 2214; -.
DR DisGeNET; 2214; -.
DR GeneCards; FCGR3A; -.
DR HGNC; HGNC:3619; FCGR3A.
DR HPA; ENSG00000203747; Tissue enhanced (lung, lymphoid tissue).
DR MalaCards; FCGR3A; -.
DR MIM; 146740; gene.
DR MIM; 615707; phenotype.
DR neXtProt; NX_P08637; -.
DR OpenTargets; ENSG00000203747; -.
DR Orphanet; 437552; Autosomal recessive primary immunodeficiency with defective spontaneous natural killer cell cytotoxicity.
DR PharmGKB; PA28065; -.
DR VEuPathDB; HostDB:ENSG00000203747; -.
DR eggNOG; ENOG502RU1M; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_1_0_1; -.
DR InParanoid; P08637; -.
DR OMA; GDNSTQW; -.
DR OrthoDB; 866496at2759; -.
DR PhylomeDB; P08637; -.
DR PathwayCommons; P08637; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-2029481; FCGR activation.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; P08637; -.
DR SIGNOR; P08637; -.
DR BioGRID-ORCS; 2214; 12 hits in 998 CRISPR screens.
DR ChiTaRS; FCGR3A; human.
DR EvolutionaryTrace; P08637; -.
DR GeneWiki; FCGR3A; -.
DR GenomeRNAi; 2214; -.
DR Pharos; P08637; Tclin.
DR PRO; PR:P08637; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P08637; protein.
DR Bgee; ENSG00000203747; Expressed in granulocyte and 98 other tissues.
DR ExpressionAtlas; P08637; baseline and differential.
DR Genevisible; P08637; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0033001; C:Fc-gamma receptor III complex; IDA:UniProtKB.
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:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0140375; F:immune receptor activity; IDA:UniProtKB.
DR GO; GO:0019772; F:low-affinity IgG receptor activity; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IDA:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0038094; P:Fc-gamma receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0042116; P:macrophage activation; IDA:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; IDA:UniProtKB.
DR GO; GO:0043320; P:natural killer cell degranulation; IDA:UniProtKB.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein;
KW IgG-binding protein; Immunity; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..254
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-A"
FT /id="PRO_0000015150"
FT TOPO_DOM 17..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 107..189
FT /note="Ig-like C2-type 2"
FT SITE 195..196
FT /note="Cleavage; by ADAM17"
FT /evidence="ECO:0000269|PubMed:24337742,
FT ECO:0000269|PubMed:25816339"
FT SITE 222
FT /note="Important for receptor turnover"
FT /evidence="ECO:0000269|PubMed:28652325"
FT MOD_RES 236
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000305|PubMed:23024279"
FT MOD_RES 237
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000305|PubMed:23024279"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21768335,
FT ECO:0000269|PubMed:22023369"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21768335,
FT ECO:0000269|PubMed:22023369"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..89
FT /evidence="ECO:0000269|PubMed:21768335,
FT ECO:0000269|PubMed:22023369, ECO:0007744|PDB:3AY4,
FT ECO:0007744|PDB:3SGJ, ECO:0007744|PDB:3SGK"
FT DISULFID 128..172
FT /evidence="ECO:0000269|PubMed:21768335,
FT ECO:0000269|PubMed:22023369, ECO:0007744|PDB:3AY4,
FT ECO:0007744|PDB:3SGJ, ECO:0007744|PDB:3SGK"
FT VARIANT 66
FT /note="L -> H (in IMD20; loss of interaction with CD2;
FT dbSNP:rs10127939)"
FT /evidence="ECO:0000269|PubMed:23006327,
FT ECO:0000269|PubMed:8608639, ECO:0000269|PubMed:8609432,
FT ECO:0000269|PubMed:8874200"
FT /id="VAR_008800"
FT VARIANT 66
FT /note="L -> R (in dbSNP:rs10127939)"
FT /evidence="ECO:0000269|PubMed:8609432"
FT /id="VAR_008799"
FT VARIANT 147
FT /note="G -> D (in dbSNP:rs443082)"
FT /id="VAR_058398"
FT VARIANT 158
FT /note="Y -> H (in dbSNP:rs396716)"
FT /id="VAR_058399"
FT VARIANT 176
FT /note="F -> V (shows a higher binding capacity for IgG1,
FT IgG3 and IgG4; dbSNP:rs396991)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7700021, ECO:0000269|PubMed:9242542,
FT ECO:0000269|PubMed:9276722, ECO:0000269|Ref.3"
FT /id="VAR_003960"
FT VARIANT 203
FT /note="F -> S (enables membrane anchoring via
FT glycosylphosphatidylinositol; disrupts transmembrane
FT anchoring; dbSNP:rs1042206)"
FT /evidence="ECO:0000269|PubMed:1825220"
FT /id="VAR_058400"
FT MUTAGEN 197
FT /note="S->P: Impairs receptor shedding. Impairs the
FT detachment of NK cells from opsonized target cells upon
FT sequential activation."
FT /evidence="ECO:0000269|PubMed:25816339,
FT ECO:0000269|PubMed:29967280"
FT MUTAGEN 203
FT /note="F->P: Disrupts transmembrane anchoring."
FT /evidence="ECO:0000269|PubMed:1825220"
FT MUTAGEN 203
FT /note="F->T,Y,N,E,A,D,K: Enables membrane anchoring via
FT glycosylphosphatidylinositol. Disrupts transmembrane
FT anchoring."
FT /evidence="ECO:0000269|PubMed:1825220"
FT MUTAGEN 203
FT /note="F->V,I,L: Enables only transmembrane anchoring."
FT /evidence="ECO:0000269|PubMed:1825220"
FT MUTAGEN 208
FT /note="Q->A: Decreases the association with either CD247 or
FT FCER1G."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 210
FT /note="S->A: Has no effect on complex association with
FT CD247 or FCER1G. Decreases cell surface expression; when
FT associated with A-211 and A-212."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 211
FT /note="F->A: Decreases the association with either CD247 or
FT FCER1G. Decreases cell surface expression; when associated
FT with A-210 and A-212."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 212
FT /note="C->A: Has no effect on complex formation with CD247
FT or FCER1G. Decreases cell surface expression; when
FT associated with A-210 and A-211."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 219
FT /note="F->A: Decreases the association with either CD247 or
FT FCER1G. Decreases cell surface expression."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 222
FT /note="D->A: Decreases the association with either CD247 or
FT FCER1G. Strongly increases cell surface expression."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 222
FT /note="D->E,K: Strongly decreases complex formation with
FT CD247 or FCER1G."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 222
FT /note="D->N: Has little effect on complex formation with
FT CD247 or FCER1G."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 223
FT /note="T->A: Decreases the association with either CD247 or
FT FCER1G. Decreases cell surface expression."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 226
FT /note="Y->A: Decreases the association with either CD247 or
FT FCER1G. Decreases cell surface expression; when associated
FT with A-227 and A-228."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 227
FT /note="F->A: Decreases the association with either CD247 or
FT FCER1G. Decreases cell surface expression; when associated
FT with A-226 and A-228."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 228
FT /note="S->A: Has little effect on complex formation with
FT CD247 or FCER1G. Decreases cell surface expression; when
FT associated with A-226 and A-227."
FT /evidence="ECO:0000269|PubMed:28652325"
FT MUTAGEN 235..237
FT /note="SST->AAA: Loss of PKC-dependent phosphorylation.
FT Abolishes pro-inflammatory cytokine production while
FT enhancing cell degranulation."
FT /evidence="ECO:0000269|PubMed:23024279"
FT MUTAGEN 249..254
FT /note="Missing: Impairs the interaction with S100A4."
FT /evidence="ECO:0000269|PubMed:23024279"
FT CONFLICT 106
FT /note="I -> V (in Ref. 3; BAD96988/BAD97015)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> S (in Ref. 5; AAH33678)"
FT /evidence="ECO:0000305"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3SGJ"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3SGJ"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:7SEG"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:7SEG"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:7SEG"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:7SEG"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:7SEG"
SQ SEQUENCE 254 AA; 29089 MW; D38D178D32C67337 CRC64;
MWQLLLPTAL LLLVSAGMRT EDLPKAVVFL EPQWYRVLEK DSVTLKCQGA YSPEDNSTQW
FHNESLISSQ ASSYFIDAAT VDDSGEYRCQ TNLSTLSDPV QLEVHIGWLL LQAPRWVFKE
EDPIHLRCHS WKNTALHKVT YLQNGKGRKY FHHNSDFYIP KATLKDSGSY FCRGLFGSKN
VSSETVNITI TQGLAVSTIS SFFPPGYQVS FCLVMVLLFA VDTGLYFSVK TNIRSSTRDW
KDHKFKWRKD PQDK
