Detail Information for IndEnz0002009295
IED ID IndEnz0002009295
Enzyme Type ID protease009295
Protein Name Ovalbumin
OVA
Egg albumin
Gene Name SERPINB14
Organism Dromaius novaehollandiae (Emu)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Palaeognathae Casuariiformes (Emu and cassowaries) Dromaiidae (emus) Dromaius Dromaius novaehollandiae (Emu)
Enzyme Sequence MGSIGAASTEFCFDMFKELKVHHVNENIIYSPLSIISILSMVFLGARENTKTQMEKVIHFDKITGFGESLESQCGTSVSVHASLKDILSEITKPSDNYSLSLASKLYAEETYPVLPEYLQCIKELYKGSLETVSFQTAADQARELINSWVETQTNGVIKNFLQPGSVDPQTEMVLVDAIYFKGTWEKAFKDEDTQEVPFRITEQESKPVQMMYQAGSFKVATVAAEKMKILELPYASGELSMFVLLPDDISGLEQLETTISIEKLSEWTSSNMMEDRKMKVYLPHMKIEEKYNLTSVLVALGMTDLFSPSANLSGISTAQTLKMSEAIHGAYVEIYEAGSEMATSTGVLVEAASVSEEFRVDHPFLFLIKHNPSNSILFFGRCIFP
Enzyme Length 386
Uniprot Accession Number E2RVI8
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Storage protein of egg white. Lacks protease inhibitory activity (By similarity). {ECO:0000250|UniProtKB:P01012}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (18); Chain (1); Disulfide bond (1); Glycosylation (1); Helix (11); Initiator methionine (1); Modified residue (3); Site (1); Turn (7)
Keywords 3D-structure;Acetylation;Direct protein sequencing;Disulfide bond;Glycoprotein;Phosphoprotein;Secreted
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01012}.
Modified Residue MOD_RES 2; /note=N-acetylglycine; /evidence=ECO:0000250|UniProtKB:P01012; MOD_RES 69; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P01012; MOD_RES 345; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P01012
Post Translational Modification PTM: The N-terminus is blocked. {ECO:0000269|PubMed:21058653}.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 6KGA;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 43,081
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda