Primary Information |
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BoMiProt ID | Bomi5 |
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Protein Name | Complement C4 |
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Organism | Bos taurus |
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Uniprot ID | P01030 |
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Milk Fraction | Whey |
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Aminoacid Length | 920 |
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Molecular Weight | 101885 |
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FASTA Sequence |
Download |
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Gene Name | C4 |
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Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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Protein Function | most heterogeneous protein of the complement system; act as opsonizing molecules; C4b2a complex (the CP C3 convertase) remains on the activator and
mediates downstream activation by cleaving C3 into C3b and C3a; C4b may offer
a nucleophile for the cleavage of the thioester in nascent C3b |
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Biochemical Properties | C4A is more prone to attach to amine groups
of an activator, whereas C4B reacts preferentially with hydroxyl
groups; |
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Significance in milk | recruit inflammatory
leucocytes to the sites of an inflammation and activate their
effector mechanisms |
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PTMs | Glycosylated: 4 N linked glycosylation site; α and ß-chains are glycosylated, but no
accurate assessment of carbohydrate content in the
γ-chain has been reported; C4 in human plasma contains
mannose, galactose, glucosamine and sialic acid; contain
complex biantennary glycans with varying degrees
of sialylation; Human C4A recovered from cerebrospinal fluid was identified to
contain an O-linked core 1 glycan; sulfation of three tyrosine residues |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | 1TMH; (73-95) |
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Additional Comments | Carbohydrate incorporation can be blocked by tunicamycin; underglycosylated pro-C4 protein is
more rapidly catabolized than the corresponding
fully glycosylated protein; underglycosylated
native C4, produced in the presence of
tunicamycin, had approximately the same specific
biological activity as glycosylated C4 |