Detail Information for IndEnz0010000399
IED ID IndEnz0010000399
Enzyme Type ID esterase000399
Protein Name Complement C1r subcomponent
EC 3.4.21.41
Complement component 1 subcomponent r

Cleaved into: Complement C1r subcomponent heavy chain; Complement C1r subcomponent light chain
Gene Name C1R
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED
Enzyme Length 705
Uniprot Accession Number P00736
Absorption
Active Site ACT_SITE 502; /note=Charge relay system; ACT_SITE 557; /note=Charge relay system; ACT_SITE 654; /note=Charge relay system
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42).; EC=3.4.21.41;
DNA Binding
EC Number 3.4.21.41
Enzyme Function FUNCTION: C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (42); Chain (3); Disulfide bond (13); Domain (6); Glycosylation (4); Helix (7); Modified residue (2); Natural variant (20); Signal peptide (1); Turn (8)
Keywords 3D-structure;Complement pathway;Direct protein sequencing;Disease variant;Disulfide bond;EGF-like domain;Ehlers-Danlos syndrome;Glycoprotein;Hydrolase;Hydroxylation;Immunity;Innate immunity;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Sushi
Interact With Itself; P09871; P05155
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27745832}.
Modified Residue MOD_RES 167; /note=(3R)-3-hydroxyasparagine; /evidence=ECO:0000269|PubMed:2820791; MOD_RES 206; /note=Phosphoserine; by CK2; /evidence=ECO:0000269|PubMed:8635594
Post Translational Modification PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:2820791}.
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000269|PubMed:3036070
Structure 3D X-ray crystallography (8); NMR spectroscopy (1)
Cross Reference PDB 1APQ; 1GPZ; 1MD7; 1MD8; 2QY0; 6F1C; 6F1D; 6F1H; 6F39;
Mapped Pubmed ID 10925294; 11445589; 12396008; 1249422; 12499050; 12555245; 12788922; 14280442; 15199963; 17996945; 20008834; 20178990; 20592021; 20796027; 20970424; 21988832; 23300094; 23589288; 23650384; 2387866; 26231209; 26709396; 28104818; 28544690; 29311313; 30535813; 31749804; 34155115; 6019133; 70787; 760802; 761607; 814163;
Motif
Gene Encoded By
Mass 80,119
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.41;