Detail Information for IndEnz0002014574
IED ID IndEnz0002014574
Enzyme Type ID protease014574
Protein Name Aspartic protease 2
Na-APR-2
EC 3.4.23.-
Necepsin I
Pepsin-like aspartic protease 2
Gene Name apr-2 ncpI
Organism Necator americanus (Human hookworm)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Strongylida Ancylostomatoidea Ancylostomatidae Bunostominae Necator Necator americanus (Human hookworm)
Enzyme Sequence MRSILVLVALIGCIAAGVYKIPLKRITPPMIKMLRAGTWETYVEGMRKRQLQLLKEHKVHIQDVLGYANMEYLGEITIGTPQQKFLVVLDTGSSNLWVPDDSCYKEKRPDRCLVSNCDAGLVCQVFCPDPKCCEHTREFKQVNACKDKHRFDQKNSNTYVKTNKTWAIAYGTGDARGFFGRDTVRLGAEGKDQLVINDTWFGQAEHIAEFFSNTFLDGILGLAFQELSEGGVAPPIIRAIDLGLLDQPIFTVYFENVGDKEGVYGGVFTWGGLDPDHCEDEVTYEQLTEATYWQFRLKGVSSKNFSSTAGWEAISDTGTSLNGAPRGILRSIARQYNGQYVASQGLYVVDCSKNVTVDVTIGDRNYTMTAKNLVLEIQADICIMAFFEMDMFIGPAWILGDPFIREYCNIHDIEKKRIGFAAVKH
Enzyme Length 425
Uniprot Accession Number Q9N9H4
Absorption
Active Site ACT_SITE 90; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 316; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103
Activity Regulation ACTIVITY REGULATION: Inhibited by pepstatin A. {ECO:0000269|PubMed:12552433}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.23.-
Enzyme Function FUNCTION: Aspartic protease which cleaves several human serum proteins including hemoglobin, fibrinogen and albumin. Appears to cleave preferentially between P1 (Ala, Leu, Val, Phe and Gly) and P1' (Ala and Leu) residues. {ECO:0000269|PubMed:12552433}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:12552433};
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (5); Signal peptide (1)
Keywords Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12552433}. Note=Secreted into the gut lumen. {ECO:0000269|PubMed:12552433}.
Modified Residue
Post Translational Modification PTM: Cleaved into a mature form. {ECO:0000269|PubMed:12552433}.
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 47,650
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda