Detail Information for IndEnz0002000471
IED ID IndEnz0002000471
Enzyme Type ID protease000471
Protein Name Pigment epithelium-derived factor
PEDF
Cell proliferation-inducing gene 35 protein
EPC-1
Serpin F1
Gene Name SERPINF1 PEDF PIG35
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 MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP
Enzyme Length 418
Uniprot Accession Number P36955
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. {ECO:0000269|PubMed:7592790, ECO:0000269|PubMed:8226833}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (15); Chain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (1); Helix (14); Modified residue (4); Natural variant (2); Region (2); Sequence conflict (2); Signal peptide (1); Turn (6)
Keywords 3D-structure;Direct protein sequencing;Dwarfism;Glycoprotein;Osteogenesis imperfecta;Phosphoprotein;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal
Interact With Q7L775; Q9P2X3; Q96EQ0
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Enriched in stage I melanosomes.
Modified Residue MOD_RES 20; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:12737624; MOD_RES 24; /note=Phosphoserine; by CK2; /evidence=ECO:0000269|PubMed:15374885; MOD_RES 114; /note=Phosphoserine; by CK2; /evidence=ECO:0000269|PubMed:15374885; MOD_RES 227; /note=Phosphoserine; by PKA; /evidence=ECO:0000269|PubMed:15374885
Post Translational Modification PTM: The N-terminus is blocked. Extracellular phosphorylation enhances antiangiogenic activity. {ECO:0000269|PubMed:15374885}.; PTM: N- and O-glycosylated. O-glycosylated with a core 1 or possibly core 8 glycan. {ECO:0000269|PubMed:11562499, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169}.
Signal Peptide SIGNAL 1..19
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1IMV;
Mapped Pubmed ID 12200129; 12237317; 12599204; 12603315; 12670505; 12687338; 12711260; 12827055; 12837042; 12860293; 12878936; 12920663; 14991838; 15096582; 15140209; 15150108; 15239109; 15377265; 15713745; 15846509; 15856012; 15994443; 16196102; 16322471; 16409998; 16596284; 16707486; 16740777; 16777976; 16797605; 16896539; 17188371; 17202143; 17213275; 17479108; 17525281; 17593873; 17604022; 17651710; 17658465; 17870167; 18084848; 18180304; 18191271; 18226801; 18312852; 18523656; 18625531; 18676622; 18677713; 18704312; 18715664; 18787046; 18787502; 18792873; 18805795; 18845835; 19091957; 19180572; 19182495; 19223990; 19224861; 19247457; 19253105; 19298519; 19342598; 19503741; 19513563; 19583952; 19635565; 19637042; 19661223; 19913121; 19948828; 20087951; 20104255; 20132989; 20141354; 20228934; 20229034; 20237999; 20381502; 20412062; 20504225; 20628086; 20631025; 20664971; 20678803; 20685859; 20706999; 20709803; 20857208; 21058962; 21067572; 21122834; 21174599; 21209034; 21211310; 21236558; 21275514; 21281801; 21292512; 21323605; 21330424; 21336718; 21570865; 21652703; 21673604; 21697716; 21777264; 21826736; 21846721; 21851923; 21947986; 22028839; 22029535; 22051848; 22113968; 22115973; 22120651; 22215693; 22234980; 22315956; 22457728; 22457810; 22547925; 22570532; 22669302; 22701300; 22792709; 22819570; 22827961; 22837306; 22884488; 22915824; 22917444; 22930782; 23038613; 23055574; 23075882; 23123582; 23218576; 23318725; 23346798; 23359450; 23393224; 23547472; 23547730; 23553951; 23569025; 23600479; 23722394; 23818523; 23844817; 23924722; 23939834; 24078214; 24105071; 24161393; 24255038; 24342618; 24361362; 24698153; 24760990; 24766673; 24810046; 25030625; 25064413; 25127091; 25159325; 25166721; 25172543; 25284724; 25293868; 25363869; 25416956; 25447045; 25450390; 25462587; 25562624; 25678686; 25700221; 25705004; 25820866; 25821324; 25844034; 25868797; 25881671; 25948043; 25992628; 26304116; 26333415; 26427478; 26450919; 26612427; 26693895; 26697494; 26700654; 26746675; 26815784; 26921338; 26966066; 27056980; 27219009; 27278471; 27440994; 27557659; 27576898; 27590659; 27706701; 27716557; 27747237; 27796462; 28122611; 28173817; 28191465; 28197761; 28211523; 28399539; 28420811; 28562170; 28569772; 28602715; 28627623; 28637898; 28648555; 28667418; 28706437; 28747334; 28911166; 28944893; 29244789; 29259049; 29512769; 29574467; 29579411; 29664206; 29736859; 29792311; 29978595; 30142832; 30326915; 30431098; 30439539; 30455080; 30554580; 30904010; 30926171; 30968248; 31173218; 31204718; 31434620; 31582735; 31711388; 31886225; 32377760; 32413570; 32544239; 32724163; 33317138; 33412338; 33484131; 33741351; 34288906; 34684100;
Motif
Gene Encoded By
Mass 46,312
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda