Detail Information for IndEnz0010001336
IED ID IndEnz0010001336
Enzyme Type ID esterase001336
Protein Name Complement C1s subcomponent
EC 3.4.21.42
C1 esterase
Complement component 1 subcomponent s

Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain
Gene Name C1s r-gsp
Organism Rattus norvegicus (Rat)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MWCFVFFSLLASFSAEPTMYGEILSPNYPQAYPNEVVKTWDIEVPEGFGIHLYFTHLDMELSENCAYDSVQIISGGIEEERLCGQRTSKSPNSPTVEEFQFPYNRLQVVFTSDFSNEERFTGFAAYYSAVDVNECTDFTDVPCSHFCNNFIGGYFCSCPPEYFLHDDMRTCGVNCSGDVFTALIGEIASPNYPNPYPENSRCEYQIRLQEGFRLVLTIRREDFDVEPADSEGNCHDSLTFAAKNQQFGPYCGNGFPGPLTIKTQSNTLDIVFQTDLTGQNKGWKLRYHGDPIPCPKEISANSIWEPEKAKYVFKDVVKITCVDGFEVVEGNVGSTSFYSTCQSNGQWSNSRLECQPVDCGVPEPIENGKVEDPEDTVFGSVIHYTCEEPYYYMEQEEGGEYHCAANGSWVNDQLGVELPKCIPVCGVPTEPFKVQQRIFGGYSTKIQSFPWQVYFESPRGGGALIDEYWVLTAAHVVEGNSDPVMYVGSTLLKIERLRNAQRLITERVIIHPSWKQEDDLNTRTNFDNDIALVQLKDPVKMGPTVAPICLPETSSDYNPSEGDLGLISGWGRTENRTNVIQLRGAKLPITSLEKCQQVKVENPKARSNDYVFTDNMICAGEKGVDSCEGDSGGAFALPVPNVKDPKFYVAGLVSWGKKCGTYGIYTKVKNYVDWILKTMQENSGPKKD
Enzyme Length 688
Uniprot Accession Number Q6P6T1
Absorption
Active Site ACT_SITE 475; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 529; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 631; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Inhibited by SERPING1. {ECO:0000250}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase.; EC=3.4.21.42;
DNA Binding
EC Number 3.4.21.42
Enzyme Function FUNCTION: C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4 (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (3); Disulfide bond (13); Domain (6); Erroneous initiation (2); Glycosylation (2); Metal binding (9); Modified residue (1); Sequence conflict (4); Signal peptide (1)
Keywords Calcium;Complement pathway;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Hydroxylation;Immunity;Innate immunity;Metal-binding;Protease;Reference proteome;Repeat;Serine protease;Signal;Sushi
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 149; /note=(3R)-3-hydroxyasparagine; /evidence=ECO:0000250
Post Translational Modification PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
Signal Peptide SIGNAL 1..15; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12393260;
Motif
Gene Encoded By
Mass 77,071
Kinetics
Metal Binding METAL 60; /note=Calcium; /evidence=ECO:0000250; METAL 68; /note=Calcium; /evidence=ECO:0000250; METAL 113; /note=Calcium; /evidence=ECO:0000250; METAL 131; /note=Calcium; /evidence=ECO:0000250; METAL 132; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 134; /note=Calcium; /evidence=ECO:0000250; METAL 149; /note=Calcium; /evidence=ECO:0000250; METAL 150; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 153; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda