Primary Information |
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BoMiProt ID | Bomi4845 |
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Protein Name | Complement C1q subcomponent subunit A |
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Organism | Bos taurus |
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Uniprot ID | Q5E9E3 |
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Milk Fraction | whey |
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Ref Sequence ID | NP_001014945.1 |
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Aminoacid Length | 244 |
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Molecular Weight | 25802 |
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FASTA Sequence |
Download |
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Gene Name | C1QA |
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Gene ID | 534961 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system |
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Biochemical Properties | Interacts (via C-terminus) with CD33; this interaction activates CD33 inhibitory motifs |
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PTMs | Glycosylation, Hydroxylation and Disulphide bond |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q5E9E3|C1QA_BOVIN Complement C1q subcomponent subunit A OS=Bos taurus OX=9913 GN=C1QA PE=2 SV=1
MEAPRGWLVISVLAISLASSVTEDVCRAPDGTHGSAGIPGRPGRPGLK*48GERGEPGAPAIQ
TGIRGLK*67GDQGDPGPPGNPGRMGYPGPSGPMGPAGLPGLK*100GTKGSPGNIKDQPRPAFSAV
GPNSVSRDNVVVFGKVITNQENVYQN*146NTGRFRCSVPGYYYFTFQVVSNWDICLSIRSSRR
DQIQPLGFCDFNSKGFFQVVSGGTVLHLQQGDQVWIEKDPSKGRIYHGSEADSIFSGFLI
FPSA
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Predicted Disorder Regions | 18-109, 117-124 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | O-linked glycans are Glc-Gal disaccharides typically found as secondary modifications of hydroxylated lysines in collagen-like domains |
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Bibliography | Tenner, A. J., & Volkin, D. B. (1986). Complement subcomponent C1q secreted by cultured human monocytes has subunit structure identical with that of serum C1q. The Biochemical journal, 233(2), 451–458. https://doi.org/10.1042/bj2330451 |