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Overview

Uniprot IDP01602
Protein NameImmunoglobulin kappa variable 1-5
Gene NameIGKV1-5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
72 APKLLIYKASSLESG

Function

V region of the variable domain of immunoglobulin light 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 MDMRVPAQLL 20 GLLLLWLPGA 30 KCDIQMTQSP 40 STLSASVGDR 50 VTITCRASQS 60 ISSWLAWYQQ 70 KPGKAPKLLI 80 YKASSLESGV 90 PSRFSGSGSG 100 TEFTLTISSL 110 QPDDFATYYC QQYNSYS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070062 extracellular exosome
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.