P01860
uniprot
P01860
canonical
amino_acid_sequence
ASTKGPSVFPLAPCSRSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYTCNVNHKPSNTKVDKRVELKTPLGDTTHTCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFKWYVDGVEVHNAKTKPREEQYNSTFRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESSGQPENNYNTTPPMLDSDGSFFLYSKLTVDKSRWQQGNIFSCSVMHEALHNRFTQKSLSLSPELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATVTFFKVKWIFSSVVDLKQTIIPDYRNMIGQGA
uniprot
proteins
function
FUNCTION: Constant region of immunoglobulin (Ig) heavy chains. Igs are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound Igs serve as receptors, which upon binding to a specific antigen trigger the clonal expansion and differentiation of B lymphocytes into Ig-secreting plasma cells. Secreted Igs known as antibodies mediate the effector phase of humoral immunity by blocking the interaction of infectious antigens with cellular receptors (via the antigen-binding region) and eliciting effector mechanisms that lead to pathogen neutralization (via the constant region) (PubMed:17576170, PubMed:20176268, PubMed:22158414). The antigen-binding region is formed by the variable domain of one heavy chain paired with the variable domain of its associated light chain. Each Ig molecule has two antigen-binding sites with remarkable affinity for a particular antigen due to V-(D)-J rearrangement, somatic hypermutations and affinity maturation of the variable domains upon antigen exposure (PubMed:17576170, PubMed:20176268, PubMed:22158414). The constant region defines the Ig isotype that perform distinct sets of effector functions. B cells diversify and rearrange their Ig constant regions through class-switch recombination, a process by which the constant region is switched from one Ig isotype to another, namely from IgM and IgD to IgG, IgA and IgE (PubMed:17576170, PubMed:20176268, PubMed:22158414). The constant region of Ig gamma-3 (IgG3) isotype interacts (via the fragment crystallizable, Fc) with receptors on innate immune cells and the complement system to mediate humoral effector functions, including antibody-dependent cellular cytotoxicity or phagocytosis, complement-dependent cytotoxicity and inflammatory responses. {ECO:0000269|PubMed:28566370, ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
uniprot
proteins
mass_dalton
49093
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. Carries predominantly biantennary complex-type glycans attached at Asn-227 residue on the Fc region of each heavy chain. Unique Fc glycan profiles found in secreted IgGs are induced in an antigen-specific way, likely programmed during B cell priming to mount an appropriate Ig effector response (PubMed:29445378, PubMed:39983994). The core glycan is composed of two sequential N-acetylglucosamine (GlcNAc) moieties followed by a central mannose (Man) from which two additional Man residues branch out (alpha1,3 and alpha1,6 antennae) each capped with a GlcNAc. Additional sugar molecules can be added to generate over 30 possible glycans. Such sugar modifications include the addition of one fucose at the initial GlcNAc, galactose (Gal) and sialic acid (Neu5Ac) residues at antennary GlcNAc or a bisecting GlcNAc to the core Man (PubMed:26536155, PubMed:29445378, PubMed:39983994). Variable addition of sugars account for different IgG functional states. IgG3 Fcs carrying afucosylated N-glycans display enhanced affinity for FCGR3A and mediate antibody-dependent cellular cytotoxicity (PubMed:28566370). {ECO:0000269|PubMed:26536155, ECO:0000269|PubMed:28566370, ECO:0000269|PubMed:29445378, ECO:0000269|PubMed:39983994}.; PTM: N-linked glycans at Asn-322 are noncore fucosylated and the vast majority are diantennary species with a bisecting GlcNAc. Among them the most dominant glycans are HexNAc5Hex4, HexNAc5Hex5, and HexNAc5Hex5Sia1. {ECO:0000269|PubMed:26536155}.; PTM: (Microbial infection) Deglycosylation on Asn-227 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway. {ECO:0000269|PubMed:11406581, ECO:0000269|PubMed:20357243, ECO:0000269|PubMed:23865566}.; PTM: O-linked glycans are non-, mono- and disialylated core 1-type O-glycans. {ECO:0000269|PubMed:25759508}.
uniprot
proteins
pubmed
11340299
uniprot
proteins
pubmed
11406581
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
15572068
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
17576170
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
1979064
uniprot
proteins
pubmed
20176268
uniprot
proteins
pubmed
20357243
uniprot
proteins
pubmed
22158414
uniprot
proteins
pubmed
23865566
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25759508
uniprot
proteins
pubmed
26536155
uniprot
proteins
pubmed
28566370
uniprot
proteins
pubmed
29445378
uniprot
proteins
pubmed
3081877
uniprot
proteins
pubmed
37421619
uniprot
proteins
pubmed
39983994
uniprot
proteins
pubmed
402363
uniprot
proteins
pubmed
6774747
uniprot
proteins
pubmed
6808505
uniprot
proteins
pubmed
6811139
uniprot
proteins
pubmed
823945
uniprot
proteins
pubmed
9126488
uniprot
proteins
sequence_length
446
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 398..418; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins