Immunoglobulin heavy variable 3-30

Details

Name
Immunoglobulin heavy variable 3-30
Synonyms
  • Ig heavy chain V-III region BUR
  • Ig heavy chain V-III region CAM
  • Ig heavy chain V-III region GA
  • Ig heavy chain V-III region NIE
Gene Name
IGHV3-30
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049971|Immunoglobulin heavy variable 3-30
MEFGLSWVFLVALLRGVQCQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAP
GKGLEWVAVISYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAK
Number of residues
117
Molecular Weight
12946.69
Theoretical pI
Not Available
GO Classification
Functions
antigen binding / serine-type endopeptidase activity
Processes
complement activation / complement activation, classical pathway / Fc-epsilon receptor signaling pathway / Fc-gamma receptor signaling pathway involved in phagocytosis / immune response / leukocyte migration / receptor-mediated endocytosis / regulation of complement activation / regulation of immune response
Components
extracellular region / extracellular space / plasma membrane
General Function
V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). 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:20176268, PubMed:17576170).
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 IDP01768
UniProtKB Entry NameHV330_HUMAN
HGNC IDHGNC:5591
General References
  1. 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]
  2. Florent G, Lehman D, Putnam FW: The switch point in mu heavy chains of human IgM immunoglobulins. Biochemistry. 1974 Jun 4;13(12):2482-98. [Article]
  3. Ponstingl H, Hilschmann N: [The rule of antibody structure. The primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie). III. The chymotryptic peptides of the H-chain, alignment of the tryptic peptides and discussion of the complete structure]. Hoppe Seylers Z Physiol Chem. 1976 Nov;357(11):1571-604. [Article]
  4. Putnam FW, Liu YS, Low TL: Primary structure of a human IgA1 immunoglobulin. IV. Streptococcal IgA1 protease, digestion, Fab and Fc fragments, and the complete amino acid sequence of the alpha 1 heavy chain. J Biol Chem. 1979 Apr 25;254(8):2865-74. [Article]
  5. Lehman DW, Putnam FW: Amino acid sequence of the variable region of a human mu chain: location of a possible JH segment. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3239-43. [Article]
  6. Dreker L, Schwarz J, Reichel W, Hilschmann N: [Rule of antibody structure. the primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie), I: Purification and characterization of the protein, the L- and H-chains, the cyanogenbromide cleavage products, and the disulfide bridges (author's transl)]. Hoppe Seylers Z Physiol Chem. 1976 Nov;357(11):1515-40. [Article]
  7. Lefranc MP: Nomenclature of the human immunoglobulin heavy (IGH) genes. Exp Clin Immunogenet. 2001;18(2):100-16. [Article]
  8. Teng G, Papavasiliou FN: Immunoglobulin somatic hypermutation. Annu Rev Genet. 2007;41:107-20. [Article]
  9. 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]
  10. 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]
  11. Lefranc MP: Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and Rise of Immunoinformatics. Front Immunol. 2014 Feb 5;5:22. doi: 10.3389/fimmu.2014.00022. eCollection 2014. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB083964-{[(Z)-(5-oxo-2-phenyl-1,3-oxazol-4(5H)-ylidene)methyl]amino}butanoic acidexperimentalunknownDetails
DB08635N-(TRANS-4'-NITRO-4-STILBENYL)-N-METHYL-5-AMINO-PENTANOIC ACIDexperimentalunknownDetails