| IED ID | IndEnz0002004117 |
| Enzyme Type ID | protease004117 |
| Protein Name |
Immunoglobulin heavy constant alpha 1 Ig alpha-1 chain C region Ig alpha-1 chain C region BUR Ig alpha-1 chain C region TRO |
| Gene Name | IGHA1 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | ASPTSPKVFPLSLCSTQPDGNVVIACLVQGFFPQEPLSVTWSESGQGVTARNFPPSQDASGDLYTTSSQLTLPATQCLAGKSVTCHVKHYTNPSQDVTVPCPVPSTPPTPSPSTPPTPSPSCCHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGVTFTWTPSSGKSAVQGPPERDLCGCYSVSSVLPGCAEPWNHGKTFTCTAAYPESKTPLTATLSKSGNTFRPEVHLLPPPSEELALNELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTFAVTSILRVAAEDWKKGDTFSCMVGHEALPLAFTQKTIDRLAGKPTHVNVSVVMAEVDGTCY |
| Enzyme Length | 353 |
| Uniprot Accession Number | P01876 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 352; /note=3-hydroxy-L-kynurenine; binds multimeric 3-hydroxykynurenine chromophore; covalent; in form alpha-1-microglobulin complex |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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:22158414, PubMed:20176268). 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). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:2241915}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (18); Binding site (1); Chain (1); Compositional bias (1); Disulfide bond (10); Domain (3); Erroneous initiation (1); Glycosylation (11); Helix (4); Natural variant (1); Non-terminal residue (1); Region (1); Sequence conflict (6); Turn (3) |
| Keywords | 3D-structure;Adaptive immunity;Cell membrane;Chromophore;Chromosomal rearrangement;Direct protein sequencing;Disulfide bond;Glycoprotein;Immunity;Immunoglobulin;Immunoglobulin domain;Membrane;Reference proteome;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. |
| Modified Residue | |
| Post Translational Modification | PTM: 3-Hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with alpha-1-microglobulin to form heterogeneous polycyclic chromophores including hydroxanthommatin. The chromophore reacts with accessible cysteines forming non-reducible thioether cross-links with Ig alpha-1 chain C region Cys-352. {ECO:0000269|PubMed:7506257}.; PTM: N- and O-glycosylated. N-glycan at Asn-144: Hex5HexNAc4. {ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (4); X-ray crystallography (5) |
| Cross Reference PDB | 1IGA; 1OW0; 2ESG; 2QEJ; 3CHN; 6LX3; 6LXW; 6UE7; 6XJA; |
| Mapped Pubmed ID | 10064707; 10438530; 11779189; 11877257; 12023968; 12768205; 15174051; 15731049; 16212417; 16376934; 17353931; 17511028; 17848512; 18323783; 18538846; 18826328; 19079336; 19153537; 19531670; 19596235; 20007591; 20562859; 22810585; 22864623; 23386615; 24586974; 24676358; 24725412; 24918438; 24928472; 25609649; 25647400; 25694468; 26596049; 26986150; 28035353; 29299950; 30388165; 32398862; 32699192; 33122053; 33247098; 33341801; 33578917; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,655 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |