Detail Information for IndEnz0002001042
IED ID IndEnz0002001042
Enzyme Type ID protease001042
Protein Name Serglycin
Hematopoietic proteoglycan core protein
Platelet proteoglycan core protein
P.PG
Secretory granule proteoglycan core protein
Gene Name SRGN PRG PRG1
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 MMQKLLKCSRLVLALALILVLESSVQGYPTRRARYQWVRCNPDSNSANCLEEKGPMFELLPGESNKIPRLRTDLFPKTRIQDLNRIFPLSEDYSGSGFGSGSGSGSGSGSGFLTEMEQDYQLVDESDAFHDNLRSLDRNLPSDSQDLGQHGLEEDFML
Enzyme Length 158
Uniprot Accession Number P10124
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization. {ECO:0000269|PubMed:11911826, ECO:0000269|PubMed:16420477, ECO:0000269|PubMed:16870619}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (1); Glycosylation (8); Natural variant (1); Region (2); Repeat (9); Sequence conflict (1); Signal peptide (1)
Keywords Apoptosis;Biomineralization;Direct protein sequencing;Disulfide bond;Glycoprotein;Golgi apparatus;Lysosome;Proteoglycan;Reference proteome;Repeat;Secreted;Signal
Interact With P10144; P11226; P61601; O00623; O43765; Q96EQ0; Q9UMX0; Q9UMX0-2; Q9UHD9
Induction INDUCTION: By Epstein-Barr virus (EBV).
Subcellular Location SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:11154222}. Cytolytic granule {ECO:0000269|PubMed:11154222}. Secreted, extracellular space {ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:16870619}. Golgi apparatus {ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:15136585}. Note=Found in mast cell granules and in cytoplasmic granules of cytolytic T lymphocytes from where it is secreted upon cell activation (By similarity). Secreted constitutively by endothelial cells and macrophages (PubMed:11154222). Located to Golgi apparatus during neutrophil differentiation (PubMed:15136585). {ECO:0000250|UniProtKB:P13609, ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:15136585}.
Modified Residue
Post Translational Modification PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate. {ECO:0000250}.
Signal Peptide SIGNAL 1..27; /evidence="ECO:0000269|PubMed:3214420, ECO:0000269|PubMed:3402609"
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 14506241; 14739229; 15788411; 16189514; 16713569; 17909965; 18000860; 20711500; 21075844; 21268013; 21289131; 21516116; 21849484; 21900206; 22807344; 23376071; 23387827; 23601700; 23640497; 23996242; 24403068; 24513305; 24995621; 25416956; 26496610; 26581653; 26694746; 27809309; 27819672; 28005267; 29842969; 31018746; 31145901; 31898491; 32292495; 32370744; 32712749; 33081679; 33314317; 33634997; 34969735; 6457647; 8467233;
Motif
Gene Encoded By
Mass 17,652
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda