Overview
| Uniprot ID | P06312 |
| Protein Name | Immunoglobulin kappa variable 4-1 |
| Gene Name | IGKV4-1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 65 |
YLAWYQQKPGQPPKL |
Function
V segment of the variable domain of immunoglobulins light chain 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: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)
Protein Sequence
10
MVLQTQVFIS
20
LLLWISGAYG
30
DIVMTQSPDS
40
LAVSLGERAT
50
INCKSSQSVL
60
YSSNNKNYLA
70
WYQQKPGQPP
80
KLLIYWASTR
90
ESGVPDRFSG
100
SGSGTDFTLT
110
ISSLQAEDVA
120
VYYCQQYYST
P
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0072562 |
blood microparticle |
| Cellular Component |
GO:0005576 |
extracellular region |
| Cellular Component |
GO:0019814 |
immunoglobulin complex |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Molecular Function |
GO:0003823 |
antigen binding |
| Biological Process |
GO:0002250 |
adaptive immune response |
| Biological Process |
GO:0006955 |
immune response |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.