Overview
| Uniprot ID | A0A0B4J1V0 |
|---|
| Protein Name | Immunoglobulin heavy variable 3-15 |
|---|
| Gene Name | IGHV3-15 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 73 |
WVGRIKSKTDGGTTD |
| 86 |
TDYAAPVKGRFTISR |
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: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
MEFGLSWIFL
20
AAILKGVQCE
30
VQLVESGGGL
40
VKPGGSLRLS
50
CAASGFTFSN
60
AWMSWVRQAP
70
GKGLEWVGRI
80
KSKTDGGTTD
90
YAAPVKGRFT
100
ISRDDSKNTL
110
YLQMNSLKTE
DTAVYYCTT
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0005576 |
extracellular region |
| Cellular Component |
GO:0019814 |
immunoglobulin complex |
| Molecular Function |
GO:0003823 |
antigen binding |
| Biological Process |
GO:0016064 |
immunoglobulin mediated 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.