| IED ID | IndEnz0002003603 |
| Enzyme Type ID | protease003603 |
| Protein Name |
Heparin cofactor 2 Heparin cofactor II HC-II Protease inhibitor leuserpin-2 HLS2 Serpin D1 |
| Gene Name | SERPIND1 HCF2 |
| 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 | MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTLEAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPSRS |
| Enzyme Length | 499 |
| Uniprot Accession Number | P05546 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner. {ECO:0000269|PubMed:1939083}.; FUNCTION: Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils. {ECO:0000269|PubMed:1939083}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (18); Chain (1); Erroneous initiation (1); Glycosylation (3); Helix (17); Modified residue (3); Mutagenesis (6); Natural variant (9); Region (3); Repeat (2); Sequence conflict (4); Signal peptide (1); Site (1); Turn (6) |
| Keywords | 3D-structure;Blood coagulation;Chemotaxis;Direct protein sequencing;Disease variant;Glycoprotein;Hemostasis;Heparin-binding;Phosphoprotein;Protease inhibitor;Reference proteome;Repeat;Serine protease inhibitor;Signal;Sulfation;Thrombophilia |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 37; /note=Phosphoserine; by FAM20C; /evidence=ECO:0000269|PubMed:26091039; MOD_RES 79; /note=Sulfotyrosine; /evidence=ECO:0000269|PubMed:12169660; MOD_RES 92; /note=Sulfotyrosine; /evidence=ECO:0000269|PubMed:12169660 |
| Post Translational Modification | PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:3907702 |
| Structure 3D | NMR spectroscopy (7); X-ray crystallography (2) |
| Cross Reference PDB | 1JMJ; 1JMO; 2NAT; 2NCU; 2NCV; 2NCW; 6J12; 6KBO; 6KBV; |
| Mapped Pubmed ID | 10781579; 11856753; 12095635; 12152684; 14982929; 15174051; 15247982; 15292227; 15543340; 16339402; 16981704; 18383370; 18971786; 19747479; 19913121; 20053992; 2019570; 20628086; 20671370; 21107326; 21911577; 22904320; 23300094; 23496873; 23656734; 24136289; 2502206; 2505252; 25130770; 27137928; 2742826; 27430660; 28087279; 28303012; 2866798; 3082357; 3134349; 31383740; 32827448; 3863104; 8338946; 9888880; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,071 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |