C1R Protein Overview: Sequence, Structure, Function and Protein Interaction

C1R Protein Overview

C1R reagents

By large-scale random sequencing of a dendritic cell cDNA library, Lin et al. (2004) cloned C1RL, which they called CLSPA. The deduced 487-amino acid protein has a calculated molecular mass of about 53.5 kD. It has an N-terminal signal peptide, a conserved CUB domain, a truncated complement control protein module, and a trypsin-like serine protease domain. It also has 2 N-glycosylation sites and 3 conserved cysteines in the CUB domain, but it lacks a consensus sequence for activation by upstream trypsin-like proteases. C1RL shares sequence similarity with C1r (613785), C1s (120580), and MASPs (see 600521). PCR analysis detected C1RL expression in all tissues examined except brain. Highest expression was in placenta, liver, kidney, and pancreas. C1RL was secreted by transfected HEK293 cells.

C1R protein family

Belongs to the peptidase S1 family.

C1R protein name

Recommended name
Complement C1r subcomponent

C1R Protein Molecular Weight & PI

The parameters have been computed for the following feature

FT CHAIN 18-705 Complement C1r subcomponent.

Molecular weight (Da)


Theoretical pI


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