Detail Information for IndEnz0002000163
IED ID IndEnz0002000163
Enzyme Type ID protease000163
Protein Name Gastricsin
EC 3.4.23.3
Pepsinogen C
Gene Name PGC
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 MKWMVVVLVCLQLLEAAVVKVPLKKFKSIRETMKEKGLLGEFLRTHKYDPAWKYRFGDLSVTYEPMAYMDAAYFGEISIGTPPQNFLVLFDTGSSNLWVPSVYCQSQACTSHSRFNPSESSTYSTNGQTFSLQYGSGSLTGFFGYDTLTVQSIQVPNQEFGLSENEPGTNFVYAQFDGIMGLAYPALSVDEATTAMQGMVQEGALTSPVFSVYLSNQQGSSGGAVVFGGVDSSLYTGQIYWAPVTQELYWQIGIEEFLIGGQASGWCSEGCQAIVDTGTSLLTVPQQYMSALLQATGAQEDEYGQFLVNCNSIQNLPSLTFIINGVEFPLPPSSYILSNNGYCTVGVEPTYLSSQNGQPLWILGDVFLRSYYSVYDLGNNRVGFATAA
Enzyme Length 388
Uniprot Accession Number P20142
Absorption
Active Site ACT_SITE 91; ACT_SITE 276
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin.; EC=3.4.23.3;
DNA Binding
EC Number 3.4.23.3
Enzyme Function FUNCTION: Hydrolyzes a variety of proteins.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (1); Beta strand (24); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Helix (16); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (3)
Keywords 3D-structure;Alternative splicing;Aspartyl protease;Digestion;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Reference proteome;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..16; /evidence="ECO:0000269|PubMed:2515193, ECO:0000269|PubMed:6816595"
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1AVF; 1HTR;
Mapped Pubmed ID 12128264; 12508350; 12698190; 12759353; 15200883; 15503827; 15688378; 16937501; 17288837; 17559360; 18256027; 18447628; 18844222; 19132389; 19173902; 19624876; 19731026; 20379614; 21303408; 22066020; 23047493; 23178618; 23311720; 23326145; 23455381; 24009139; 24284944; 24586594; 24895149; 25028655; 25551587; 25857852; 26158864; 26486507; 27865295; 29108629; 30155999; 30400679; 32228342; 32271765; 33127250; 34463892; 8098309; 9391244; 9794784;
Motif
Gene Encoded By
Mass 42,426
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.23.3;