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Low affinity immunoglobulin gamma Fc region receptor II-b (IgG Fc receptor II-b) (CDw32) (Fc-gamma RII-b) (Fc-gamma-RIIb) (FcRII-b) (CD antigen CD32)

 FCG2B_HUMAN             Reviewed;         310 AA.
P31994; A6H8N3; O95649; Q53X85; Q5VXA9; Q8NIA1;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
25-OCT-2017, entry version 200.
RecName: Full=Low affinity immunoglobulin gamma Fc region receptor II-b;
Short=IgG Fc receptor II-b;
AltName: Full=CDw32;
AltName: Full=Fc-gamma RII-b;
Short=Fc-gamma-RIIb;
Short=FcRII-b;
AltName: CD_antigen=CD32;
Flags: Precursor;
Name=FCGR2B; Synonyms=CD32, FCG2, IGFR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1; IIB2; 4 AND 5), AND VARIANT
THR-232.
TISSUE=Lymphocyte;
Ng S., Sinclair N.R.S., Anderson C., Bell D.A., Cairns E.;
"Fc-gamma-RIIb nucleotide sequences in SLE and non-SLE humans in vivo
derived lymphocytes.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
TISSUE=Placenta;
PubMed=2531080;
Stuart S.G., Simister N.E., Clarkson S.B., Kacinski B.M., Shapiro M.,
Mellman I.;
"Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in
macrophages, lymphocytes and IgG-transporting placental epithelium.";
EMBO J. 8:3657-3666(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB1; IIB2 AND IIB3), AND VARIANT
PHE-205.
PubMed=2529342; DOI=10.1084/jem.170.4.1369;
Brooks D.G., Qiu W.Q., Luster A.D., Ravetch J.V.;
"Structure and expression of human IgG FcRII(CD32). Functional
heterogeneity is encoded by the alternatively spliced products of
multiple genes.";
J. Exp. Med. 170:1369-1385(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB2).
TISSUE=Placenta;
PubMed=2142460; DOI=10.1002/eji.1830200624;
Engelhardt W., Geerds C., Frey J.;
"Distribution, inducibility and biological function of the cloned and
expressed human beta Fc receptor II.";
Eur. J. Immunol. 20:1367-1377(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIB2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IIB1 AND IIB2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 132-253, INVOLVEMENT IN SLE, AND VARIANT
THR-232.
PubMed=12115230; DOI=10.1002/art.10257;
Kyogoku C., Dijstelbloem H.M., Tsuchiya N., Hatta Y., Kato H.,
Yamaguchi A., Fukazawa T., Jansen M.D., Hashimoto H.,
van de Winkel J.G.J., Kallenberg C.G.M., Tokunaga K.;
"Fc gamma receptor gene polymorphisms in Japanese patients with
systemic lupus erythematosus: contribution of FCGR2B to genetic
susceptibility.";
Arthritis Rheum. 46:1242-1254(2002).
[9]
INTERACTION WITH FGR.
PubMed=8327512; DOI=10.1073/pnas.90.13.6305;
Hamada F., Aoki M., Akiyama T., Toyoshima K.;
"Association of immunoglobulin G Fc receptor II with Src-like protein-
tyrosine kinase Fgr in neutrophils.";
Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993).
[10]
PHOSPHORYLATION AT TYR-292.
PubMed=8756631; DOI=10.1128/MCB.16.9.4735;
Bewarder N., Weinrich V., Budde P., Hartmann D., Flaswinkel H.,
Reth M., Frey J.;
"In vivo and in vitro specificity of protein tyrosine kinases for
immunoglobulin G receptor (FcgammaRII) phosphorylation.";
Mol. Cell. Biol. 16:4735-4743(1996).
[11]
INTERACTION WITH LYN.
PubMed=9232445; DOI=10.1016/S0165-2478(97)00055-2;
Sarmay G., Koncz G., Pecht I., Gergely J.;
"Fc gamma receptor type IIb induced recruitment of inositol and
protein phosphatases to the signal transductory complex of human B-
cell.";
Immunol. Lett. 57:159-164(1997).
[12]
INTERACTION WITH MEASLES VIRUS N PROTEIN.
PubMed=15914856; DOI=10.1099/vir.0.80791-0;
Laine D., Bourhis J.-M., Longhi S., Flacher M., Cassard L., Canard B.,
Sautes-Fridman C., Rabourdin-Combe C., Valentin H.;
"Measles virus nucleoprotein induces cell-proliferation arrest and
apoptosis through NTAIL-NR and NCORE-FcgammaRIIB1 interactions,
respectively.";
J. Gen. Virol. 86:1771-1784(2005).
[13]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 46-217, AND DISULFIDE BONDS.
PubMed=10064577; DOI=10.1093/emboj/18.5.1095;
Sondermann P., Huber R., Jacob U.;
"Crystal structure of the soluble form of the human fcgamma-receptor
IIb: a new member of the immunoglobulin superfamily at 1.7 A
resolution.";
EMBO J. 18:1095-1103(1999).
[14]
VARIANT ASP-258.
PubMed=8466861; DOI=10.1093/intimm/5.3.239;
Warmerdam P.A., van den Herik-Oudijk I.E., Parren P.W.,
Westerdaal N.A., van de Winkel J.G., Capel P.J.;
"Interaction of a human Fc gamma RIIb1 (CD32) isoform with murine and
human IgG subclasses.";
Int. Immunol. 5:239-247(1993).
[15]
POLYMORPHISM, INVOLVEMENT IN RESISTANCE TO MALARIA, VARIANT THR-232,
AND CHARACTERIZATION OF VARIANT THR-232.
PubMed=17435165; DOI=10.1073/pnas.0608889104;
Clatworthy M.R., Willcocks L., Urban B., Langhorne J., Williams T.N.,
Peshu N., Watkins N.A., Floto R.A., Smith K.G.;
"Systemic lupus erythematosus-associated defects in the inhibitory
receptor FcgammaRIIb reduce susceptibility to malaria.";
Proc. Natl. Acad. Sci. U.S.A. 104:7169-7174(2007).
[16]
POLYMORPHISM, INVOLVEMENT IN SLE, VARIANT THR-232, AND INVOLVEMENT IN
RESISTANCE TO MALARIA.
PubMed=20385827; DOI=10.1073/pnas.0915133107;
Willcocks L.C., Carr E.J., Niederer H.A., Rayner T.F., Williams T.N.,
Yang W., Scott J.A., Urban B.C., Peshu N., Vyse T.J., Lau Y.L.,
Lyons P.A., Smith K.G.;
"A defunctioning polymorphism in FCGR2B is associated with protection
against malaria but susceptibility to systemic lupus erythematosus.";
Proc. Natl. Acad. Sci. U.S.A. 107:7881-7885(2010).
-!- FUNCTION: Receptor for the Fc region of complexed or aggregated
immunoglobulins gamma. Low affinity receptor. Involved in a
variety of effector and regulatory functions such as phagocytosis
of immune complexes and modulation of antibody production by B-
cells. Binding to this receptor results in down-modulation of
previous state of cell activation triggered via antigen receptors
on B-cells (BCR), T-cells (TCR) or via another Fc receptor.
Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform
IIB2 does not trigger phagocytosis.
-!- SUBUNIT: Isoform IIB1 interacts with measles virus N protein. N
protein is released in the blood following lysis of measles
infected cells. This interaction presumably block inflammatory
immune response. Interacts with INPP5D/SHIP1. Interacts with FGR.
Interacts with LYN. {ECO:0000269|PubMed:15914856,
ECO:0000269|PubMed:8327512, ECO:0000269|PubMed:9232445}.
-!- INTERACTION:
P01857:IGHG1; NbExp=31; IntAct=EBI-724784, EBI-356114;
Q92835:INPP5D; NbExp=3; IntAct=EBI-724784, EBI-1380477;
P16333:NCK1; NbExp=2; IntAct=EBI-724784, EBI-389883;
P19174:PLCG1; NbExp=2; IntAct=EBI-724784, EBI-79387;
P29350:PTPN6; NbExp=3; IntAct=EBI-724784, EBI-78260;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=IIB1 {ECO:0000303|PubMed:2529342};
IsoId=P31994-1; Sequence=Displayed;
Name=IIB2 {ECO:0000303|PubMed:2529342};
IsoId=P31994-2; Sequence=VSP_002643;
Name=IIB3 {ECO:0000303|PubMed:2529342};
IsoId=P31994-3; Sequence=VSP_002642;
Name=4;
IsoId=P31994-4; Sequence=VSP_058635;
Name=5;
IsoId=P31994-5; Sequence=VSP_058635, VSP_002643;
-!- TISSUE SPECIFICITY: Is the most broadly distributed Fc-gamma-
receptor. Expressed in monocyte, neutrophils, macrophages,
basophils, eosinophils, Langerhans cells, B-cells, platelets cells
and placenta (endothelial cells). Not detected in natural killer
cells.
-!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to
as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This
motif is involved in modulation of cellular responses. The
phosphorylated ITIM motif can bind the SH2 domain of several SH2-
containing phosphatases.
-!- PTM: Phosphorylated by the SRC-type Tyr-kinases LYN and BLK.
{ECO:0000269|PubMed:8756631}.
-!- POLYMORPHISM: Note=FCGR2B polymorphisms can influence
susceptibility or resistance to malaria [MIM:611162].
{ECO:0000269|PubMed:17435165, ECO:0000269|PubMed:20385827}.
-!- DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A
chronic, relapsing, inflammatory, and often febrile multisystemic
disorder of connective tissue, characterized principally by
involvement of the skin, joints, kidneys and serosal membranes. It
is of unknown etiology, but is thought to represent a failure of
the regulatory mechanisms of the autoimmune system. The disease is
marked by a wide range of system dysfunctions, an elevated
erythrocyte sedimentation rate, and the formation of LE cells in
the blood or bone marrow. {ECO:0000269|PubMed:12115230,
ECO:0000269|PubMed:20385827}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- CAUTION: Has sometimes been attributed to correspond to FcR-IIC.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA35645.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FCGR2BID397.html";
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EMBL; U87560; AAD00627.1; -; mRNA.
EMBL; U87561; AAD00628.1; -; mRNA.
EMBL; U87562; AAD00629.1; -; mRNA.
EMBL; U87563; AAD00630.1; -; mRNA.
EMBL; U87564; AAD00631.1; -; mRNA.
EMBL; U87565; AAD00632.1; -; mRNA.
EMBL; U87566; AAD00633.1; -; mRNA.
EMBL; U87567; AAD00634.1; -; mRNA.
EMBL; U87568; AAD00635.1; -; mRNA.
EMBL; U87569; AAD00636.1; -; mRNA.
EMBL; U87570; AAD00637.1; -; mRNA.
EMBL; U87571; AAD00638.1; -; mRNA.
EMBL; U87572; AAD00639.1; -; mRNA.
EMBL; U87573; AAD00640.1; -; mRNA.
EMBL; U87574; AAD00641.1; -; mRNA.
EMBL; U87575; AAD00642.1; -; mRNA.
EMBL; U87576; AAD00643.1; -; mRNA.
EMBL; U87577; AAD00644.1; -; mRNA.
EMBL; X17653; CAA35644.1; -; mRNA.
EMBL; X17653; CAA35645.1; ALT_INIT; mRNA.
EMBL; M31933; AAA35841.1; -; mRNA.
EMBL; M31934; AAA35842.1; -; mRNA.
EMBL; M31935; AAA35843.1; -; mRNA.
EMBL; X52473; CAA36713.1; -; mRNA.
EMBL; CR407635; CAG28563.1; -; mRNA.
EMBL; AL359541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC031992; AAH31992.1; -; mRNA.
EMBL; BC146678; AAI46679.1; -; mRNA.
EMBL; AB050934; BAB92093.1; -; mRNA.
CCDS; CCDS30924.1; -. [P31994-1]
CCDS; CCDS30925.1; -. [P31994-2]
CCDS; CCDS53414.1; -. [P31994-3]
PIR; JL0119; JL0119.
RefSeq; NP_001002273.1; NM_001002273.2. [P31994-5]
RefSeq; NP_001002274.1; NM_001002274.2. [P31994-2]
RefSeq; NP_001002275.1; NM_001002275.2. [P31994-4]
RefSeq; NP_001177757.1; NM_001190828.1. [P31994-3]
RefSeq; NP_003992.3; NM_004001.4. [P31994-1]
RefSeq; XP_016856160.1; XM_017000671.1. [P31994-1]
RefSeq; XP_016856161.1; XM_017000672.1. [P31994-2]
UniGene; Hs.654395; -.
PDB; 2FCB; X-ray; 1.74 A; A=46-217.
PDB; 3WJJ; X-ray; 2.60 A; C=45-217.
PDBsum; 2FCB; -.
PDBsum; 3WJJ; -.
ProteinModelPortal; P31994; -.
SMR; P31994; -.
BioGrid; 108507; 5.
DIP; DIP-36638N; -.
ELM; P31994; -.
IntAct; P31994; 15.
MINT; MINT-1376812; -.
STRING; 9606.ENSP00000351497; -.
DrugBank; DB00054; Abciximab.
DrugBank; DB00051; Adalimumab.
DrugBank; DB00092; Alefacept.
DrugBank; DB00087; Alemtuzumab.
DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
DrugBank; DB00074; Basiliximab.
DrugBank; DB00112; Bevacizumab.
DrugBank; DB00002; Cetuximab.
DrugBank; DB00111; Daclizumab.
DrugBank; DB00095; Efalizumab.
DrugBank; DB00005; Etanercept.
DrugBank; DB00056; Gemtuzumab ozogamicin.
DrugBank; DB00078; Ibritumomab tiuxetan.
DrugBank; DB00028; Immune Globulin Human.
DrugBank; DB00075; Muromonab.
DrugBank; DB00108; Natalizumab.
DrugBank; DB00110; Palivizumab.
DrugBank; DB00073; Rituximab.
DrugBank; DB00081; Tositumomab.
DrugBank; DB00072; Trastuzumab.
MEROPS; I43.001; -.
iPTMnet; P31994; -.
PhosphoSitePlus; P31994; -.
BioMuta; FCGR2B; -.
DMDM; 8039788; -.
MaxQB; P31994; -.
PaxDb; P31994; -.
PeptideAtlas; P31994; -.
PRIDE; P31994; -.
Ensembl; ENST00000236937; ENSP00000236937; ENSG00000072694. [P31994-2]
Ensembl; ENST00000358671; ENSP00000351497; ENSG00000072694. [P31994-1]
Ensembl; ENST00000367961; ENSP00000356938; ENSG00000072694. [P31994-3]
GeneID; 2213; -.
KEGG; hsa:2213; -.
UCSC; uc001gaz.3; human. [P31994-1]
CTD; 2213; -.
DisGeNET; 2213; -.
DisGeNET; 9103; -.
EuPathDB; HostDB:ENSG00000072694.19; -.
GeneCards; FCGR2B; -.
HGNC; HGNC:3618; FCGR2B.
HPA; CAB007796; -.
HPA; HPA014730; -.
MalaCards; FCGR2B; -.
MIM; 152700; phenotype.
MIM; 604590; gene.
MIM; 611162; phenotype.
neXtProt; NX_P31994; -.
OpenTargets; ENSG00000072694; -.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA28064; -.
eggNOG; ENOG410J9AP; Eukaryota.
eggNOG; ENOG410YXNK; LUCA.
GeneTree; ENSGT00760000119130; -.
HOGENOM; HOG000251632; -.
HOVERGEN; HBG051602; -.
InParanoid; P31994; -.
KO; K12560; -.
OMA; XAENTIT; -.
OrthoDB; EOG091G0JSA; -.
PhylomeDB; P31994; -.
TreeFam; TF335097; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
SignaLink; P31994; -.
SIGNOR; P31994; -.
EvolutionaryTrace; P31994; -.
GeneWiki; FCGR2B; -.
GenomeRNAi; 2213; -.
PRO; PR:P31994; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000072694; -.
CleanEx; HS_FCGR2B; -.
Genevisible; P31994; HS.
GO; GO:0044297; C:cell body; ISS:BHF-UCL.
GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; ISS:ARUK-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:ARUK-UCL.
GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
GO; GO:0019864; F:IgG binding; IDA:ARUK-UCL.
GO; GO:0019772; F:low-affinity IgG receptor activity; IDA:ARUK-UCL.
GO; GO:0044877; F:macromolecular complex binding; IPI:ARUK-UCL.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:ARUK-UCL.
GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISS:ARUK-UCL.
GO; GO:0021549; P:cerebellum development; ISS:BHF-UCL.
GO; GO:0006952; P:defense response; ISS:ARUK-UCL.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; IDA:ARUK-UCL.
GO; GO:0002316; P:follicular B cell differentiation; TAS:ARUK-UCL.
GO; GO:0002266; P:follicular dendritic cell activation; TAS:ARUK-UCL.
GO; GO:0002436; P:immune complex clearance by monocytes and macrophages; TAS:ARUK-UCL.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0016064; P:immunoglobulin mediated immune response; ISS:ARUK-UCL.
GO; GO:0006954; P:inflammatory response; TAS:ARUK-UCL.
GO; GO:0002313; P:mature B cell differentiation involved in immune response; TAS:ARUK-UCL.
GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; ISS:ARUK-UCL.
GO; GO:0001814; P:negative regulation of antibody-dependent cellular cytotoxicity; TAS:ARUK-UCL.
GO; GO:0050869; P:negative regulation of B cell activation; TAS:ARUK-UCL.
GO; GO:0030889; P:negative regulation of B cell proliferation; ISS:ARUK-UCL.
GO; GO:0050710; P:negative regulation of cytokine secretion; TAS:ARUK-UCL.
GO; GO:0043318; P:negative regulation of cytotoxic T cell degranulation; TAS:ARUK-UCL.
GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; TAS:ARUK-UCL.
GO; GO:2001199; P:negative regulation of dendritic cell differentiation; TAS:ARUK-UCL.
GO; GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; ISS:ARUK-UCL.
GO; GO:0050777; P:negative regulation of immune response; ISS:ARUK-UCL.
GO; GO:0002638; P:negative regulation of immunoglobulin production; ISS:ARUK-UCL.
GO; GO:0032693; P:negative regulation of interleukin-10 production; ISS:ARUK-UCL.
GO; GO:0043031; P:negative regulation of macrophage activation; TAS:ARUK-UCL.
GO; GO:1902564; P:negative regulation of neutrophil activation; TAS:ARUK-UCL.
GO; GO:0050765; P:negative regulation of phagocytosis; TAS:ARUK-UCL.
GO; GO:0001811; P:negative regulation of type I hypersensitivity; ISS:ARUK-UCL.
GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
GO; GO:0002922; P:positive regulation of humoral immune response; TAS:ARUK-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:ARUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
GO; GO:0050766; P:positive regulation of phagocytosis; ISS:ARUK-UCL.
GO; GO:1905898; P:positive regulation of response to endoplasmic reticulum stress; ISS:ARUK-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:ARUK-UCL.
GO; GO:0002819; P:regulation of adaptive immune response; TAS:ARUK-UCL.
GO; GO:0002622; P:regulation of B cell antigen processing and presentation; TAS:ARUK-UCL.
GO; GO:1902950; P:regulation of dendritic spine maintenance; IGI:ARUK-UCL.
GO; GO:0090264; P:regulation of immune complex clearance by monocytes and macrophages; TAS:ARUK-UCL.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0045088; P:regulation of innate immune response; TAS:ARUK-UCL.
GO; GO:0010469; P:regulation of receptor activity; TAS:ARUK-UCL.
GO; GO:0009617; P:response to bacterium; ISS:ARUK-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF13895; Ig_2; 2.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane;
Chromosomal rearrangement; Complete proteome; Disulfide bond;
Glycoprotein; Host-virus interaction; IgG-binding protein;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Proto-oncogene; Receptor; Reference proteome; Repeat; Signal;
Systemic lupus erythematosus; Transmembrane; Transmembrane helix.
SIGNAL 1 42 {ECO:0000255}.
CHAIN 43 310 Low affinity immunoglobulin gamma Fc
region receptor II-b.
/FTId=PRO_0000015147.
TOPO_DOM 43 217 Extracellular. {ECO:0000255}.
TRANSMEM 218 240 Helical. {ECO:0000255}.
TOPO_DOM 241 310 Cytoplasmic. {ECO:0000255}.
DOMAIN 48 127 Ig-like C2-type 1.
DOMAIN 131 213 Ig-like C2-type 2.
MOTIF 290 295 ITIM motif.
MOD_RES 292 292 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000269|PubMed:8756631}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 71 113 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10064577}.
DISULFID 152 196 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10064577}.
VAR_SEQ 39 45 Missing (in isoform IIB3).
{ECO:0000303|PubMed:2529342}.
/FTId=VSP_002642.
VAR_SEQ 46 46 Missing (in isoform 4 and isoform 5).
{ECO:0000303|Ref.1}.
/FTId=VSP_058635.
VAR_SEQ 254 272 Missing (in isoform IIB2 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2142460,
ECO:0000303|PubMed:2529342,
ECO:0000303|PubMed:2531080,
ECO:0000303|Ref.1, ECO:0000303|Ref.5}.
/FTId=VSP_002643.
VARIANT 83 83 Q -> P (in dbSNP:rs5017567).
/FTId=VAR_059430.
VARIANT 205 205 Y -> F (in dbSNP:rs1050499).
{ECO:0000269|PubMed:2529342}.
/FTId=VAR_027045.
VARIANT 232 232 I -> T (associated with susceptibility to
SLE; associated with resistance to
malaria; found at an increased frequency
in African and Asian populations from
areas where malaria is endemic; enhances
phagocytosis of Plasmodium falciparum-
infected erythrocytes in vitro;
dbSNP:rs1050501).
{ECO:0000269|PubMed:12115230,
ECO:0000269|PubMed:17435165,
ECO:0000269|PubMed:20385827,
ECO:0000269|Ref.1}.
/FTId=VAR_015515.
VARIANT 258 258 Y -> D (in dbSNP:rs148534844).
{ECO:0000269|PubMed:8466861}.
/FTId=VAR_008798.
CONFLICT 178 178 D -> I (in Ref. 2; CAA35644/CAA35645).
{ECO:0000305}.
CONFLICT 230 230 T -> I (in Ref. 2; CAA35644/CAA35645).
{ECO:0000305}.
CONFLICT 242 242 V -> G (in Ref. 2; CAA35644/CAA35645).
{ECO:0000305}.
CONFLICT 275 275 P -> S (in Ref. 2; CAA35644/CAA35645).
{ECO:0000305}.
STRAND 51 56 {ECO:0000244|PDB:2FCB}.
STRAND 59 62 {ECO:0000244|PDB:2FCB}.
STRAND 66 72 {ECO:0000244|PDB:2FCB}.
STRAND 83 86 {ECO:0000244|PDB:2FCB}.
STRAND 96 102 {ECO:0000244|PDB:2FCB}.
HELIX 105 107 {ECO:0000244|PDB:2FCB}.
STRAND 109 114 {ECO:0000244|PDB:2FCB}.
STRAND 116 118 {ECO:0000244|PDB:3WJJ}.
STRAND 124 129 {ECO:0000244|PDB:2FCB}.
STRAND 131 136 {ECO:0000244|PDB:2FCB}.
STRAND 140 142 {ECO:0000244|PDB:2FCB}.
STRAND 148 154 {ECO:0000244|PDB:2FCB}.
HELIX 155 157 {ECO:0000244|PDB:2FCB}.
STRAND 161 167 {ECO:0000244|PDB:2FCB}.
STRAND 170 177 {ECO:0000244|PDB:2FCB}.
STRAND 180 183 {ECO:0000244|PDB:2FCB}.
HELIX 188 190 {ECO:0000244|PDB:2FCB}.
STRAND 192 200 {ECO:0000244|PDB:2FCB}.
STRAND 203 206 {ECO:0000244|PDB:2FCB}.
STRAND 210 214 {ECO:0000244|PDB:2FCB}.
SEQUENCE 310 AA; 34044 MW; 2186F8538FF01F36 CRC64;
MGILSFLPVL ATESDWADCK SPQPWGHMLL WTAVLFLAPV AGTPAAPPKA VLKLEPQWIN
VLQEDSVTLT CRGTHSPESD SIQWFHNGNL IPTHTQPSYR FKANNNDSGE YTCQTGQTSL
SDPVHLTVLS EWLVLQTPHL EFQEGETIVL RCHSWKDKPL VKVTFFQNGK SKKFSRSDPN
FSIPQANHSH SGDYHCTGNI GYTLYSSKPV TITVQAPSSS PMGIIVAVVT GIAVAAIVAA
VVALIYCRKK RISALPGYPE CREMGETLPE KPANPTNPDE ADKVGAENTI TYSLLMHPDA
LEEPDDQNRI


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