| IED ID | IndEnz0010001277 |
| Enzyme Type ID | esterase001277 |
| Protein Name |
Plasma protease C1 inhibitor C1 Inh C1Inh C1 esterase inhibitor C1-inhibiting factor Serpin G1 |
| Gene Name | SERPING1 C1IN C1NH |
| 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 | MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFVLWDQQHKFPVFMGRVYDPRA |
| Enzyme Length | 500 |
| Uniprot Accession Number | P05155 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein. {ECO:0000269|PubMed:8495195}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (16); Chain (1); Compositional bias (1); Disulfide bond (2); Erroneous gene model prediction (1); Glycosylation (15); Helix (12); Natural variant (48); Region (3); Repeat (7); Sequence conflict (9); Signal peptide (1); Site (2); Turn (5) |
| Keywords | 3D-structure;Alternative splicing;Blood coagulation;Complement pathway;Direct protein sequencing;Disease variant;Disulfide bond;Fibrinolysis;Glycoprotein;Hemostasis;Immunity;Innate immunity;Protease inhibitor;Reference proteome;Repeat;Secreted;Serine protease inhibitor;Signal |
| Interact With | P00736; P09871; O43889-2; O00187; A0A7D5SLD3; P0C6X7; P0C6X7; O82882; Q79GN7 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Highly glycosylated (49%) with N- and O-glycosylation. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan heterogeneity at Asn-25: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16040958, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17488724, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:3756141}.; PTM: Can be proteolytically cleaved by E.coli stcE. {ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:15096536}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000269|PubMed:6416294 |
| Structure 3D | X-ray crystallography (3); Electron microscopy (1) |
| Cross Reference PDB | 2OAY; 5DU3; 5DUQ; 7AKV; |
| Mapped Pubmed ID | 10570951; 11437612; 11933207; 12421980; 12492481; 14568956; 1459574; 15174051; 15325085; 15356570; 15583734; 15596402; 15596403; 15607116; 15879149; 15971231; 16237761; 16470590; 16617246; 17230419; 17498209; 17502473; 17521609; 17709141; 17908769; 17916775; 18022239; 18035804; 18535392; 18586324; 18758157; 18842294; 19169411; 19201015; 19344414; 19423540; 19607829; 19706314; 19752569; 19925520; 20016407; 20024535; 20062564; 20120775; 20161815; 20237496; 2026621; 20306692; 20351192; 20406964; 20438785; 20576771; 20606025; 20628624; 20711500; 20800603; 20804470; 21345278; 21526158; 21623829; 21683246; 21695123; 21852020; 21864911; 21988832; 22001489; 22014012; 22078245; 22230421; 22276768; 22456031; 22456345; 22831796; 22882460; 23123409; 23318225; 23399388; 23437219; 23583915; 23607270; 23640497; 23688413; 23966370; 24262729; 24412907; 24468257; 24552232; 24565773; 25053016; 25208595; 25352749; 25369003; 2563376; 2578463; 2579948; 25800206; 25800435; 26154504; 26248961; 26347576; 26371246; 26476955; 26535898; 26782794; 26812872; 26895475; 27187751; 27197075; 27338096; 27818099; 28135312; 28194776; 28484054; 28595743; 28758643; 28889214; 29036225; 29343682; 29513108; 29548426; 29567681; 29753808; 29885370; 29920929; 30278448; 30379966; 30398465; 30508583; 30554660; 30685616; 30784776; 30817230; 3099750; 31334892; 31397881; 31409531; 31933486; 31982983; 32065705; 32163480; 32179338; 32351099; 32445210; 32531085; 32659156; 32717572; 32887189; 32896191; 33034800; 33130967; 33730015; 33758081; 33808005; 33914953; 34348603; 34871158; 34971012; 4178758; 4703226; 6457647; 760802; 761607; 7852321; 8467233; 8798678; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,154 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |