Overview
| Uniprot ID | P01877 |
|---|
| Protein Name | Immunoglobulin heavy constant alpha 2 |
|---|
| Gene Name | IGHA2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 245 |
LARGFSPKDVLVRWL |
Function
Constant region of immunoglobulin heavy 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). Ig alpha is the major immunoglobulin class in body secretions (PubMed:2241915)
Protein Sequence
10
ASPTSPKVFP
20
LSLDSTPQDG
30
NVVVACLVQG
40
FFPQEPLSVT
50
WSESGQNVTA
60
RNFPPSQDAS
70
GDLYTTSSQL
80
TLPATQCPDG
90
KSVTCHVKHY
100
TNSSQDVTVP
110
CRVPPPPPCC
120
HPRLSLHRPA
130
LEDLLLGSEA
140
NLTCTLTGLR
150
DASGATFTWT
160
PSSGKSAVQG
170
PPERDLCGCY
180
SVSSVLPGCA
190
QPWNHGETFT
200
CTAAHPELKT
210
PLTANITKSG
220
NTFRPEVHLL
230
PPPSEELALN
240
ELVTLTCLAR
250
GFSPKDVLVR
260
WLQGSQELPR
270
EKYLTWASRQ
280
EPSQGTTTYA
290
VTSILRVAAE
300
DWKKGETFSC
310
MVGHEALPLA
320
FTQKTIDRMA
330
GSCCVADWQM
340
PPPYVVLDLP
350
QETLEEETPG
360
ANLWPTTITF
370
LTLFLLSLFY
380
STALTVTSVR
390
GPSGKREGPQ
Y
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0072562 |
blood microparticle |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Cellular Component |
GO:0005576 |
extracellular region |
| Cellular Component |
GO:0005615 |
extracellular space |
| Cellular Component |
GO:0042571 |
immunoglobulin complex, circulating |
| Cellular Component |
GO:0071748 |
monomeric IgA immunoglobulin complex |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0071752 |
secretory dimeric IgA immunoglobulin complex |
| Cellular Component |
GO:0071751 |
secretory IgA immunoglobulin complex |
| Molecular Function |
GO:0003823 |
antigen binding |
| Biological Process |
GO:0002250 |
adaptive immune response |
| Biological Process |
GO:0019731 |
antibacterial humoral response |
| Biological Process |
GO:0050853 |
B cell receptor signaling pathway |
| Biological Process |
GO:0006958 |
complement activation, classical pathway |
| Biological Process |
GO:0003094 |
glomerular filtration |
| Biological Process |
GO:0006955 |
immune response |
| Biological Process |
GO:0060267 |
positive regulation of respiratory burst |
Reference
[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.