Detail Information for IndEnz0002015312
IED ID IndEnz0002015312
Enzyme Type ID protease015312
Protein Name Immunoglobulin heavy variable 3-30
Ig heavy chain V-III region BUR
Ig heavy chain V-III region CAM
Ig heavy chain V-III region GA
Ig heavy chain V-III region NIE
Gene Name IGHV3-30
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 MEFGLSWVFLVALLRGVQCQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVISYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAK
Enzyme Length 117
Uniprot Accession Number P01768
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function 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: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:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (1); Domain (1); Modified residue (1); Non-terminal residue (1); Sequence conflict (39); Signal peptide (1)
Keywords Adaptive immunity;Cell membrane;Direct protein sequencing;Disulfide bond;Immunity;Immunoglobulin;Immunoglobulin domain;Membrane;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal
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 MOD_RES 20; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:107164, ECO:0000269|PubMed:4208843, ECO:0000269|PubMed:6774332, ECO:0000269|PubMed:826475"
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence="ECO:0000269|PubMed:107164, ECO:0000269|PubMed:4208843, ECO:0000269|PubMed:6774332, ECO:0000269|PubMed:826475"
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10026222; 10051622; 10072481; 10498607; 10523831; 10556826; 10579907; 10648173; 1081164; 10861086; 10917520; 10925294; 10931839; 11071869; 11226282; 11368773; 11425868; 11449366; 11507089; 11606584; 11713268; 11779189; 11854399; 11877257; 11909947; 11955599; 11994425; 12089510; 12117970; 12181444; 12217391; 12396008; 12417718; 12453414; 12456653; 12473184; 1249422; 12573241; 12660731; 12670955; 12869549; 1314888; 1372004; 1374290; 1375264; 1376928; 14280442; 14630197; 15010370; 1506682; 15161916; 15184383; 15199963; 1550550; 15509800; 15536084; 15686303; 1569953; 15809313; 15879134; 1599430; 16456001; 16546099; 16849466; 16921024; 16938345; 16978534; 1702903; 1705565; 1707541; 1714601; 17308335; 17498065; 17993265; 18006696; 18052078; 18070890; 18818202; 19206206; 19372136; 19592646; 2011584; 20192804; 20807769; 21037092; 21469132; 21822214; 2303036; 2304550; 23593269; 23675550; 23836650; 2474607; 25200415; 2529342; 3500860; 4589993; 6019133; 6335036; 70787; 7512959; 7516890; 7517665; 7518558; 7521687; 7522622; 7524079; 7526393; 7528327; 7530449; 7538118; 7561031; 7565679; 7592958; 7594458; 760802; 7608543; 761607; 7618087; 7681402; 7688784; 7706301; 7718892; 7927516; 803528; 8071371; 814163; 8163536; 8166770; 8226994; 8306975; 8327478; 8340414; 8475064; 8541526; 8611682; 8629002; 8630736; 8657103; 8663278; 8702662; 8809042; 8862523; 8910399; 8947047; 8986718; 8995445; 9000504; 9042338; 9050880; 9188445; 9199344; 9295361; 9314552; 9326643; 9341187; 9480991; 9547345; 9601638; 9697839; 9705962; 9857068; 9885284; 9890995;
Motif
Gene Encoded By
Mass 12,947
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda