Immunoglobulin heavy constant gamma 3

Details

Name
Immunoglobulin heavy constant gamma 3
Synonyms
  • HDC
  • Heavy chain disease protein
  • Ig gamma-3 chain C region
Gene Name
IGHG3
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052521|Immunoglobulin heavy constant gamma 3
ASTKGPSVFPLAPCSRSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTQTYTCNVNHKPSNTKVDKRVELKTPLGDTTHTCPRCPEPKSC
DTPPPCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPAPELLGGPSVFLFPPKPKDT
LMISRTPEVTCVVVDVSHEDPEVQFKWYVDGVEVHNAKTKPREEQYNSTFRVVSVLTVLH
QDWLNGKEYKCKVSNKALPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVK
GFYPSDIAVEWESSGQPENNYNTTPPMLDSDGSFFLYSKLTVDKSRWQQGNIFSCSVMHE
ALHNRFTQKSLSLSPGK
Number of residues
377
Molecular Weight
41286.64
Theoretical pI
Not Available
GO Classification
Functions
antigen binding / immunoglobulin receptor binding
Processes
B cell receptor signaling pathway / complement activation / complement activation, classical pathway / defense response to bacterium / Fc-gamma receptor signaling pathway involved in phagocytosis / innate immune response / phagocytosis, engulfment / phagocytosis, recognition / positive regulation of B cell activation / regulation of complement activation / retina homeostasis
Components
blood microparticle / external side of plasma membrane / extracellular exosome / extracellular region / extracellular space / immunoglobulin complex, circulating
General Function
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
Specific Function
Antigen binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP01860
UniProtKB Entry NameIGHG3_HUMAN
HGNC IDHGNC:5527
General References
  1. Frangione B, Rosenwasser E, Prelli F, Franklin EC: Primary structure of human gamma 3 immunoglobulin deletion mutant: gamma 3 heavy-chain disease protein Wis. Biochemistry. 1980 Sep 2;19(18):4304-8. [Article]
  2. Michaelsen TE, Frangione B, Franklin EC: Primary structure of the "hinge" region of human IgG3. Probable quadruplication of a 15-amino acid residue basic unit. J Biol Chem. 1977 Feb 10;252(3):883-9. [Article]
  3. Wolfenstein-Todel C, Frangione B, Prelli F, Franklin EC: The amino acid sequence of "heavy chain disease" protein ZUC. Structure of the Fc fragment of immunoglobulin G3. Biochem Biophys Res Commun. 1976 Aug 23;71(4):907-14. [Article]
  4. Huck S, Fort P, Crawford DH, Lefranc MP, Lefranc G: Sequence of a human immunoglobulin gamma 3 heavy chain constant region gene: comparison with the other human C gamma genes. Nucleic Acids Res. 1986 Feb 25;14(4):1779-89. [Article]
  5. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [Article]
  6. Takahashi N, Ueda S, Obata M, Nikaido T, Nakai S, Honjo T: Structure of human immunoglobulin gamma genes: implications for evolution of a gene family. Cell. 1982 Jun;29(2):671-9. [Article]
  7. Alexander A, Steinmetz M, Barritault D, Frangione B, Franklin EC, Hood L, Buxbaum JN: gamma Heavy chain disease in man: cDNA sequence supports partial gene deletion model. Proc Natl Acad Sci U S A. 1982 May;79(10):3260-4. [Article]
  8. Lefranc MP: Nomenclature of the human immunoglobulin heavy (IGH) genes. Exp Clin Immunogenet. 2001;18(2):100-16. [Article]
  9. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [Article]
  10. Teng G, Papavasiliou FN: Immunoglobulin somatic hypermutation. Annu Rev Genet. 2007;41:107-20. [Article]
  11. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [Article]
  12. Schroeder HW Jr, Cavacini L: Structure and function of immunoglobulins. J Allergy Clin Immunol. 2010 Feb;125(2 Suppl 2):S41-52. doi: 10.1016/j.jaci.2009.09.046. [Article]
  13. McHeyzer-Williams M, Okitsu S, Wang N, McHeyzer-Williams L: Molecular programming of B cell memory. Nat Rev Immunol. 2011 Dec 9;12(1):24-34. doi: 10.1038/nri3128. [Article]
  14. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  15. Stavenhagen K, Plomp R, Wuhrer M: Site-Specific Protein N- and O-Glycosylation Analysis by a C18-Porous Graphitized Carbon-Liquid Chromatography-Electrospray Ionization Mass Spectrometry Approach Using Pronase Treated Glycopeptides. Anal Chem. 2015 Dec 1;87(23):11691-9. doi: 10.1021/acs.analchem.5b02366. Epub 2015 Nov 12. [Article]
  16. Plomp R, Dekkers G, Rombouts Y, Visser R, Koeleman CA, Kammeijer GS, Jansen BC, Rispens T, Hensbergen PJ, Vidarsson G, Wuhrer M: Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3). Mol Cell Proteomics. 2015 May;14(5):1373-84. doi: 10.1074/mcp.M114.047381. Epub 2015 Mar 10. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB15258Imlifidaseapproved, investigationalyescleavageDetails