FCG2A_HUMAN
ID FCG2A_HUMAN Reviewed; 317 AA.
AC P12318; Q8WUN1; Q8WW64;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 4.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor II-a;
DE Short=IgG Fc receptor II-a;
DE AltName: Full=CDw32;
DE AltName: Full=Fc-gamma RII-a;
DE Short=Fc-gamma-RIIa;
DE Short=FcRII-a;
DE AltName: CD_antigen=CD32;
DE Flags: Precursor;
GN Name=FCGR2A; Synonyms=CD32, FCG2, FCGR2A1, IGFR2;
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] (ISOFORM 1), AND VARIANT ARG-167.
RX PubMed=2824655; DOI=10.1084/jem.166.6.1668;
RA Stuart S.G., Trounstine M.L., Vaux D.J.T., Koch T., Martens C.L.,
RA Moore K.W.;
RT "Isolation and expression of cDNA clones encoding a human receptor for IgG
RT (Fc gamma RII).";
RL J. Exp. Med. 166:1668-1684(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-167.
RX PubMed=2529342; DOI=10.1084/jem.170.4.1369;
RA Brooks D.G., Qiu W.Q., Luster A.D., Ravetch J.V.;
RT "Structure and expression of human IgG FcRII(CD32). Functional
RT heterogeneity is encoded by the alternatively spliced products of multiple
RT genes.";
RL J. Exp. Med. 170:1369-1385(1989).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-167
RP AND VAL-218.
RC TISSUE=Lung, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-317 (ISOFORM 1), AND VARIANT ARG-167.
RX PubMed=2965389; DOI=10.1073/pnas.85.7.2240;
RA Hibbs M.L., Bonadonna L., Scott B.M., McKenzie I.F.C., Hogarth P.M.;
RT "Molecular cloning of a human immunoglobulin G Fc receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2240-2244(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-317 (ISOFORM 1), AND VARIANT ARG-167.
RX PubMed=3402431; DOI=10.1002/j.1460-2075.1988.tb02913.x;
RA Stengelin S., Stamenkovic I., Seed B.;
RT "Isolation of cDNAs for two distinct human Fc receptors by ligand affinity
RT cloning.";
RL EMBO J. 7:1053-1059(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-317 (ISOFORM 1).
RX PubMed=2526077; DOI=10.1007/bf02421463;
RA Seki T.;
RT "Identification of multiple isoforms of the low-affinity human IgG Fc
RT receptor.";
RL Immunogenetics 30:5-12(1989).
RN [8]
RP PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION AT ASN-97 AND ASN-178, AND
RP CRYSTALLIZATION.
RX PubMed=10397151; DOI=10.1016/s0165-2478(99)00025-5;
RA Powell M.S., Barton P.A., Emmanouilidis D., Wines B.D., Neumann G.M.,
RA Peitersz G.A., Maxwell K.F., Garrett T.P., Hogarth P.M.;
RT "Biochemical analysis and crystallisation of Fc gamma RIIa, the low
RT affinity receptor for IgG.";
RL Immunol. Lett. 68:17-23(1999).
RN [9]
RP INTERACTION WITH FGR.
RX PubMed=8327512; DOI=10.1073/pnas.90.13.6305;
RA Hamada F., Aoki M., Akiyama T., Toyoshima K.;
RT "Association of immunoglobulin G Fc receptor II with Src-like protein-
RT tyrosine kinase Fgr in neutrophils.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993).
RN [10]
RP INTERACTION WITH HCK, AND PHOSPHORYLATION.
RX PubMed=8132624; DOI=10.1016/s0021-9258(17)37050-3;
RA Ghazizadeh S., Bolen J.B., Fleit H.B.;
RT "Physical and functional association of Src-related protein tyrosine
RT kinases with Fc gamma RII in monocytic THP-1 cells.";
RL J. Biol. Chem. 269:8878-8884(1994).
RN [11]
RP PHOSPHORYLATION AT TYR-288 AND TYR-304.
RX PubMed=8756631; DOI=10.1128/mcb.16.9.4735;
RA Bewarder N., Weinrich V., Budde P., Hartmann D., Flaswinkel H., Reth M.,
RA Frey J.;
RT "In vivo and in vitro specificity of protein tyrosine kinases for
RT immunoglobulin G receptor (FcgammaRII) phosphorylation.";
RL Mol. Cell. Biol. 16:4735-4743(1996).
RN [12]
RP 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 [13]
RP INTERACTION WITH INPPL1.
RX PubMed=12690104; DOI=10.1074/jbc.m302907200;
RA Pengal R.A., Ganesan L.P., Fang H., Marsh C.B., Anderson C.L.,
RA Tridandapani S.;
RT "SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and
RT serves to regulate Fcgamma receptor-mediated signaling.";
RL J. Biol. Chem. 278:22657-22663(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 34-207, AND DISULFIDE BONDS.
RX PubMed=10331870; DOI=10.1038/8241;
RA Maxwell K.F., Powell M.S., Hulett M.D., Barton P.A., McKenzie I.F.,
RA Garrett T.P., Hogarth P.M.;
RT "Crystal structure of the human leukocyte Fc receptor, Fc gammaRIIa.";
RL Nat. Struct. Biol. 6:437-442(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 37-208, AND DISULFIDE BONDS.
RX PubMed=11397093; DOI=10.1006/jmbi.2001.4670;
RA Sondermann P., Kaiser J., Jacob U.;
RT "Molecular basis for immune complex recognition: a comparison of Fc-
RT receptor structures.";
RL J. Mol. Biol. 309:737-749(2001).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 37-207 IN COMPLEX WITH APCS,
RP SUBCELLULAR LOCATION, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=19011614; DOI=10.1038/nature07468;
RA Lu J., Marnell L.L., Marjon K.D., Mold C., Du Clos T.W., Sun P.D.;
RT "Structural recognition and functional activation of FcgammaR by innate
RT pentraxins.";
RL Nature 456:989-992(2008).
RN [17]
RP VARIANT ARG-167.
RX PubMed=8636449; DOI=10.1172/jci118552;
RA Salmon J.E., Millard S., Schachter L.A., Arnett F.C., Ginzler E.M.,
RA Gourley M.F., Ramsey-Goldman R., Peterson M.G.E., Kimberly R.P.;
RT "Fc gamma RIIA alleles are heritable risk factors for lupus nephritis in
RT African Americans.";
RL J. Clin. Invest. 97:1348-1354(1996).
CC -!- FUNCTION: Binds to the Fc region of immunoglobulins gamma. Low affinity
CC receptor. By binding to IgG it initiates cellular responses against
CC pathogens and soluble antigens. Promotes phagocytosis of opsonized
CC antigens. {ECO:0000269|PubMed:19011614}.
CC -!- SUBUNIT: Interacts with IGHG1 (PubMed:11711607). Interacts with
CC INPP5D/SHIP1 and INPPL1/SHIP2, regulating its function. Interacts with
CC APCS and FGR. Interacts with HCK. {ECO:0000269|PubMed:11711607,
CC ECO:0000269|PubMed:12690104, ECO:0000269|PubMed:19011614,
CC ECO:0000269|PubMed:8132624, ECO:0000269|PubMed:8327512}.
CC -!- INTERACTION:
CC P12318; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1395970, EBI-741480;
CC P12318; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-1395970, EBI-10173939;
CC P12318-2; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-17187481, EBI-10225815;
CC P12318-2; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-17187481, EBI-1754287;
CC P12318-2; O14735: CDIPT; NbExp=3; IntAct=EBI-17187481, EBI-358858;
CC P12318-2; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-17187481, EBI-11522780;
CC P12318-2; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-17187481, EBI-10267100;
CC P12318-2; Q07325: CXCL9; NbExp=3; IntAct=EBI-17187481, EBI-3911467;
CC P12318-2; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-17187481, EBI-12175685;
CC P12318-2; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-17187481, EBI-11991950;
CC P12318-2; P30301: MIP; NbExp=3; IntAct=EBI-17187481, EBI-8449636;
CC P12318-2; P42857: NSG1; NbExp=3; IntAct=EBI-17187481, EBI-6380741;
CC P12318-2; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-17187481, EBI-749270;
CC P12318-2; O00526: UPK2; NbExp=3; IntAct=EBI-17187481, EBI-10179682;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19011614};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:19011614}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12318-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12318-2; Sequence=VSP_036865;
CC -!- TISSUE SPECIFICITY: Found on monocytes, neutrophils and eosinophil
CC platelets.
CC -!- PTM: Phosphorylated by SRC-type Tyr-kinases such as LYN, BLK, FYN, HCK
CC and SYK. {ECO:0000269|PubMed:8132624, ECO:0000269|PubMed:8756631}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35932.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y00644; CAA68672.1; -; mRNA.
DR EMBL; M31932; AAA35827.1; -; mRNA.
DR EMBL; AL590385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019931; AAH19931.1; -; mRNA.
DR EMBL; BC020823; AAH20823.1; -; mRNA.
DR EMBL; J03619; AAA35932.1; ALT_INIT; mRNA.
DR CCDS; CCDS30922.1; -. [P12318-2]
DR CCDS; CCDS44264.1; -. [P12318-1]
DR PIR; JL0118; JL0118.
DR RefSeq; NP_001129691.1; NM_001136219.1. [P12318-1]
DR RefSeq; NP_067674.2; NM_021642.3. [P12318-2]
DR PDB; 1FCG; X-ray; 2.00 A; A=34-207.
DR PDB; 1H9V; X-ray; 3.00 A; A=37-208.
DR PDB; 3D5O; X-ray; 2.80 A; F=37-207.
DR PDB; 3RY4; X-ray; 1.50 A; A=37-206.
DR PDB; 3RY5; X-ray; 2.30 A; A=37-206.
DR PDB; 3RY6; X-ray; 3.80 A; C=40-206.
DR PDBsum; 1FCG; -.
DR PDBsum; 1H9V; -.
DR PDBsum; 3D5O; -.
DR PDBsum; 3RY4; -.
DR PDBsum; 3RY5; -.
DR PDBsum; 3RY6; -.
DR AlphaFoldDB; P12318; -.
DR SMR; P12318; -.
DR BioGRID; 108506; 60.
DR ELM; P12318; -.
DR IntAct; P12318; 27.
DR MINT; P12318; -.
DR STRING; 9606.ENSP00000271450; -.
DR BindingDB; P12318; -.
DR ChEMBL; CHEMBL5841; -.
DR DrugBank; DB00054; Abciximab.
DR DrugBank; DB00087; Alemtuzumab.
DR DrugBank; DB00112; Bevacizumab.
DR DrugBank; DB06607; Catumaxomab.
DR DrugBank; DB00002; Cetuximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00028; Human immunoglobulin G.
DR DrugBank; DB11767; Sarilumab.
DR GlyGen; P12318; 2 sites.
DR iPTMnet; P12318; -.
DR PhosphoSitePlus; P12318; -.
DR BioMuta; FCGR2A; -.
DR DMDM; 160332371; -.
DR jPOST; P12318; -.
DR MassIVE; P12318; -.
DR MaxQB; P12318; -.
DR PaxDb; P12318; -.
DR PeptideAtlas; P12318; -.
DR PRIDE; P12318; -.
DR ProteomicsDB; 52849; -. [P12318-1]
DR ProteomicsDB; 52850; -. [P12318-2]
DR ABCD; P12318; 8 sequenced antibodies.
DR Antibodypedia; 2489; 1484 antibodies from 44 providers.
DR DNASU; 2212; -.
DR Ensembl; ENST00000271450.12; ENSP00000271450.6; ENSG00000143226.15. [P12318-1]
DR Ensembl; ENST00000367972.8; ENSP00000356949.4; ENSG00000143226.15. [P12318-2]
DR GeneID; 2212; -.
DR KEGG; hsa:2212; -.
DR MANE-Select; ENST00000271450.12; ENSP00000271450.6; NM_001136219.3; NP_001129691.1.
DR UCSC; uc001gam.4; human. [P12318-1]
DR CTD; 2212; -.
DR DisGeNET; 2212; -.
DR GeneCards; FCGR2A; -.
DR HGNC; HGNC:3616; FCGR2A.
DR HPA; ENSG00000143226; Tissue enhanced (lymphoid tissue, placenta).
DR MalaCards; FCGR2A; -.
DR MIM; 146790; gene.
DR neXtProt; NX_P12318; -.
DR OpenTargets; ENSG00000143226; -.
DR PharmGKB; PA28063; -.
DR VEuPathDB; HostDB:ENSG00000143226; -.
DR eggNOG; ENOG502SVEW; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_1_2_1; -.
DR InParanoid; P12318; -.
DR OMA; VIFCLVM; -.
DR OrthoDB; 1246375at2759; -.
DR PhylomeDB; P12318; -.
DR TreeFam; TF335097; -.
DR PathwayCommons; P12318; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR SignaLink; P12318; -.
DR SIGNOR; P12318; -.
DR BioGRID-ORCS; 2212; 10 hits in 1037 CRISPR screens.
DR ChiTaRS; FCGR2A; human.
DR EvolutionaryTrace; P12318; -.
DR GeneWiki; FCGR2A; -.
DR GenomeRNAi; 2212; -.
DR Pharos; P12318; Tbio.
DR PRO; PR:P12318; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P12318; protein.
DR Bgee; ENSG00000143226; Expressed in blood and 105 other tissues.
DR ExpressionAtlas; P12318; baseline and differential.
DR Genevisible; P12318; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
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:0002376; P:immune system process; IEA:UniProtKB-KW.
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 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 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW IgG-binding protein; Immunity; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:10397151"
FT CHAIN 34..317
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT II-a"
FT /id="PRO_0000015145"
FT TOPO_DOM 34..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..118
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..204
FT /note="Ig-like C2-type 2"
FT REGION 292..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:8756631"
FT MOD_RES 304
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:8756631"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10397151"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10397151"
FT DISULFID 62..104
FT /evidence="ECO:0000269|PubMed:10331870,
FT ECO:0000269|PubMed:11397093, ECO:0000269|PubMed:19011614,
FT ECO:0007744|PDB:1FCG"
FT DISULFID 143..187
FT /evidence="ECO:0000269|PubMed:10331870,
FT ECO:0000269|PubMed:11397093, ECO:0000269|PubMed:19011614,
FT ECO:0007744|PDB:1FCG"
FT VAR_SEQ 35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036865"
FT VARIANT 63
FT /note="Q -> R (in dbSNP:rs9427398)"
FT /id="VAR_054857"
FT VARIANT 140
FT /note="M -> V (in dbSNP:rs4986941)"
FT /id="VAR_054858"
FT VARIANT 167
FT /note="H -> R (may be associated with susceptibility to
FT lupus nephritis; does not efficiently recognize IgG2;
FT dbSNP:rs1801274)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2529342, ECO:0000269|PubMed:2824655,
FT ECO:0000269|PubMed:2965389, ECO:0000269|PubMed:3402431,
FT ECO:0000269|PubMed:8636449"
FT /id="VAR_003955"
FT VARIANT 218
FT /note="I -> V (in dbSNP:rs17851834)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_054859"
FT CONFLICT 2
FT /note="T -> A (in Ref. 2; AAA35827)"
FT /evidence="ECO:0000305"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1FCG"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:3RY4"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1H9V"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:3RY4"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3RY4"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3RY4"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3RY4"
SQ SEQUENCE 317 AA; 35001 MW; 07F73F3BB282DFF6 CRC64;
MTMETQMSQN VCPRNLWLLQ PLTVLLLLAS ADSQAAAPPK AVLKLEPPWI NVLQEDSVTL
TCQGARSPES DSIQWFHNGN LIPTHTQPSY RFKANNNDSG EYTCQTGQTS LSDPVHLTVL
SEWLVLQTPH LEFQEGETIM LRCHSWKDKP LVKVTFFQNG KSQKFSHLDP TFSIPQANHS
HSGDYHCTGN IGYTLFSSKP VTITVQVPSM GSSSPMGIIV AVVIATAVAA IVAAVVALIY
CRKKRISANS TDPVKAAQFE PPGRQMIAIR KRQLEETNND YETADGGYMT LNPRAPTDDD
KNIYLTLPPN DHVNSNN
