Immunoglobulin kappa constant
Details
- Name
- Immunoglobulin kappa constant
- Kind
- protein
- Synonyms
- Ig kappa chain C region
- Ig kappa chain C region AG
- Ig kappa chain C region CUM
- Ig kappa chain C region EU
- Ig kappa chain C region OU
- Ig kappa chain C region ROY
- Ig kappa chain C region TI
- Gene Name
- IGKC
- UniProtKB Entry
- P01834Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0055453|Immunoglobulin kappa constant RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQD SKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
- Number of residues
- 107
- Molecular Weight
- 11764.95
- Theoretical pI
- 5.68
- GO Classification
- Processesadaptive immune response / immunoglobulin mediated immune responseComponentsIgA immunoglobulin complex / IgD immunoglobulin complex / IgE immunoglobulin complex / IgG immunoglobulin complex / IgM immunoglobulin complex
- General Function
- Constant region of immunoglobulin light 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:20176268, PubMed:22158414). 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
- C1-set (PF07654)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
- Not Available
- Chromosome Location
- Not Available
- Locus
- 2p12
- External Identifiers
Resource Link UniProtKB ID P01834 UniProtKB Entry Name IGKC_HUMAN GenBank Protein ID 185945 GenBank Gene ID J00241 GeneCard ID IGKC HGNC ID HGNC:5716 PDB ID(s) 1A4J, 1A4K, 1CLY, 1D5B, 1D5I, 1D6V, 1DFB, 1GAF, 1HEZ, 1HKL, 1HZH, 1I7Z, 1MIM, 1N0X, 1UCB, 2NY7, 2O5X, 2O5Y, 2O5Z, 2QQK, 2QQL, 2QQN, 2QSC, 2R56, 2RFX, 2VXQ, 3B2U, 3B2V, 3BDY, 3BE1, 3BKY, 3BN9, 3BQU, 3C08, 3C09, 3CFJ, 3CFK, 3CSY, 3D0L, 3D85, 3DVG, 3DVN, 3EYF, 3EYO, 3EYQ, 3IU3, 3O11, 3QCT, 3QCU, 3QCV, 3RU8, 3U0W, 3U7W, 3U7Y, 3VH8, 3WUW, 3X11, 3X12, 4D3C, 4D9R, 4HIX, 4NM4, 4NM8, 4XMP, 4XNY, 4XNZ, 4XXD, 4YDV, 5B38, 5B39, 5C7K, 5ESV, 5ESZ, 5EWI, 5VEB, 5VIY, 6AU5, 6AXP, 6AYN, 6AZK, 6AZL, 6B9Y, 6B9Z, 6BAE, 6BAH, 6DCV, 6DCW, 6N2X, 6N32, 6N35, 6OGE, 6OKP, 7CZY, 7CZZ, 7XQ8, 8C1C, 8DAO, 8DBZ - General References
- Gottlieb PD, Cunningham BA, Rutishauser U, Edelman GM: The covalent structure of a human gamma G-immunoglobulin. VI. Amino acid sequence of the light chain. Biochemistry. 1970 Aug 4;9(16):3155-61. [Article]
- Gall WE, Edelman GM: The covalent structure of a human gamma G-immunoglobulin. X. Intrachain disulfide bonds. Biochemistry. 1970 Aug 4;9(16):3188-96. [Article]
- Suter L, Barnikol HU, Watanabe S, Hilschmann N: [Rule of antibody structure. The primary structure of a monoclonal immunoglobulin L-chain of kappa-type, subgroup 3 (Bence-Jones protein Ti). IV. The complete amino acid sequence and its significance for the mechanism of antibody production]. Hoppe Seylers Z Physiol Chem. 1972 Feb;353(2):189-208. [Article]
- Hieter PA, Max EE, Seidman JG, Maizel JV Jr, Leder P: Cloned human and mouse kappa immunoglobulin constant and J region genes conserve homology in functional segments. Cell. 1980 Nov;22(1 Pt 1):197-207. [Article]
- Hilschmann N: [The complete amino acid sequence of Bence Jones protein Cum (kappa-type)]. Hoppe Seylers Z Physiol Chem. 1967 Dec;348(12):1718-22. [Article]
- Titani K, Shinoda T, Putnam FW: The amino acid sequence of a kappa type Bence-Jones protein. 3. The complete sequence and the location of the disulfide bridges. J Biol Chem. 1969 Jul 10;244(13):3550-60. [Article]
- Kohler H, Shimizu A, Paul C, Putnam FW: Macroglobulin structure: variable sequence of light and heavy chains. Science. 1970 Jul 3;169(3940):56-9. [Article]
- Olsen KE, Sletten K, Westermark P: Extended analysis of AL-amyloid protein from abdominal wall subcutaneous fat biopsy: kappa IV immunoglobulin light chain. Biochem Biophys Res Commun. 1998 Apr 28;245(3):713-6. [Article]
- Azkargorta M, Soria J, Ojeda C, Guzman F, Acera A, Iloro I, Suarez T, Elortza F: Human Basal Tear Peptidome Characterization by CID, HCD, and ETD Followed by in Silico and in Vitro Analyses for Antimicrobial Peptide Identification. J Proteome Res. 2015 Jun 5;14(6):2649-58. doi: 10.1021/acs.jproteome.5b00179. Epub 2015 May 20. [Article]
- Stavnezer-Nordgren J, Kekish O, Zegers BJ: Molecular defects in a human immunoglobulin kappa chain deficiency. Science. 1985 Oct 25;230(4724):458-61. [Article]
Associated Data
- Drug Relations