Detail Information for IndEnz0002009293
IED ID IndEnz0002009293
Enzyme Type ID protease009293
Protein Name Ovalbumin
Egg albumin
Gene Name SERPINB14
Organism Coturnix coturnix (Common quail) (Tetrao coturnix)
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 Neognathae Galloanserae Galliformes Phasianidae (turkeys) Perdicinae Coturnix Coturnix coturnix (Common quail) (Tetrao coturnix)
Enzyme Sequence MGSIGAASMEFCFDVFKELKVHHANDNMLYSPFAILSTLAMVFLGAKDSTRTQINKVVHFDKLPGFGDSIEAQCGTSANVHSSLRDILNQITKQNDAYSFSLASRLYAQETYTVVPEYLQCVKELYRGGLESVNFQTAADQARGLINAWVESQTNGIIRNILQPSSVDSQTAMVLVNAIAFKGLWEKAFKAEDTQTIPFRVTEQESKPVQMMHQIGSFKVASMASEKMKILELPFASGTMSMLVLLPDDVSGLEQLESTISFEKLTEWTSSSIMEERKVKVYLPRMKMEEKYNLTSLLMAMGITDLFSSSANLSGISSVGSLKIPQAVHAAYAEINEAGRDVVGSAEAGVDATEEFRADHPFLFCVKHIETNAILLFGRCVSP
Enzyme Length 383
Uniprot Accession Number Q6V115
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Storage protein of egg white. Lack protease inhibitory activity (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (1); Glycosylation (2); Initiator methionine (1); Modified residue (3); Signal peptide (1); Site (1)
Keywords Acetylation;Disulfide bond;Glycoprotein;Phosphoprotein;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue MOD_RES 2; /note=N-acetylglycine; /evidence=ECO:0000250; MOD_RES 69; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 345; /note=Phosphoserine; /evidence=ECO:0000250
Post Translational Modification PTM: The signal sequence is not cleaved. The functional signal for membrane translocation of ovalbumin becomes accessible when the nascent chain is 50 to 60 residues long. The hydrophobic sequence which lies between residues 27 and 43 folds back on the preceding residues to form an amphipathic hairpin structure which is the signal element recognized by the membrane (By similarity). {ECO:0000250}.
Signal Peptide SIGNAL 22..48; /note=Not cleaved; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 42,209
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda