P0DOX5
uniprot
P0DOX5
canonical
amino_acid_sequence
QVQLVQSGGGVVQPGRSLRLSCAASGFTFSRYTIHWVRQAPGKGLEWVAVMSYNGNNKHYADSVNGRFTISRNDSKNTLYLNMNSLRPEDTAVYYCARIRDTAMFFAHWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
uniprot
proteins
function
FUNCTION: 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, PubMed:24626930, PubMed:29449492). 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). {ECO:0000269|PubMed:24626930, ECO:0000269|PubMed:29449492, ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
uniprot
proteins
mass_dalton
49329
uniprot
proteins
mutagenesis
MUTAGEN 255; /note="I->A: Impaired ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:24626930"; MUTAGEN 302; /note="Y->D,A: Enhanced ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:29449492"; MUTAGEN 302; /note="Y->R: Impaired ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:29449492"; MUTAGEN 324; /note="K->A: Impaired ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:29449492"; MUTAGEN 329; /note="A->K: Impaired ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:29449492"; MUTAGEN 331; /note="P->A: Impaired ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:29449492"; MUTAGEN 333; /note="P->A: Impaired ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:29449492"; MUTAGEN 435; /note="H->A: Impaired ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:24626930"; MUTAGEN 436; /note="N->A: Impaired ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:24626930"; MUTAGEN 437; /note="H->R: Enhanced ability to activate the classical complement pathway."; /evidence="ECO:0000269|PubMed:24626930
uniprot
proteins
pubmed
1002129
uniprot
proteins
pubmed
17576170
uniprot
proteins
pubmed
19358553
uniprot
proteins
pubmed
20176268
uniprot
proteins
pubmed
22158414
uniprot
proteins
pubmed
24626930
uniprot
proteins
pubmed
29449492
uniprot
proteins
pubmed
826475
uniprot
proteins
sequence_length
449
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
uniprot
proteins