| IED ID | IndEnz0002016543 |
| Enzyme Type ID | protease016543 |
| Protein Name |
Serum albumin BmA-serum BmA-skin |
| Gene Name | |
| Organism | Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Bombinatoridae Bombina (firebellied toads) Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad) |
| Enzyme Sequence | MKWTILTALLIISAESKNLYKRDSEPHIRFLGEVYKKVDTIDFRGLVLITLAQHLQKCPFEELAKQVEQITTLAQACAAGARHADCATPLITLFLNRICAVPELSATYDWSTECCAKSDPERHQCFRAHRNPAPGTHYKRPEPEELCESYKKNKEDVLAHYIYEVSRGHPVLYSPAVLGFAYQFNGICSHCCEEEDKTTCFKDRMTQLKKALHIVEVQQKESCRILDNFGVRVLQALKLVKISKKNPKATFEVAQKLTSEVTHLNEDCCHGDMLECMIERMELTEHTCEHHEDISTKLKTCCEKPLIERTHCIVNLENDDIPEDLPKKVTKFVEDPEVCKLFADKKDIFLAEFLYEYGRRHPELSDQLLLRIAKGYEHQLEKCCELENFLECLKDGEHVLADAIKESTELTEKDCAIQQKLGDYLFQNVLLIRYTKKMPHVTTPSLIHITKHMTEVGDKCCALPNTQKMPCAEGGLSLIIGEFCEMEKTHPINEHVKNCCWKSYSNRRNCFTNLGPDDSYVAPEITDDTFHFTEDLCTLPEEELKNKKQGFIATLVKVKPHVTDELYGQIAVEFTKMREKCCAAEDHQACFNAEEPILIEHCKQLAA |
| Enzyme Length | 607 |
| Uniprot Accession Number | Q3T478 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood (By similarity). Potent inhibitor of trypsin but has no inhibitory effect on thrombin, chymotrypsin, elastase and subtilisin. {ECO:0000250|UniProtKB:P02768, ECO:0000269|PubMed:16081656}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (17); Domain (3); Metal binding (5); Propeptide (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Copper;Direct protein sequencing;Disulfide bond;Lipid-binding;Metal-binding;Protease inhibitor;Repeat;Secreted;Serine protease inhibitor;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00769, ECO:0000269|PubMed:16081656}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 69,554 |
| Kinetics | |
| Metal Binding | METAL 27; /note=Copper; /evidence=ECO:0000250|UniProtKB:P02770; METAL 270; /note=Zinc; via pros nitrogen; /evidence=ECO:0000250|UniProtKB:P02768; METAL 272; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P02769; METAL 272; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P02768; METAL 275; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P02769 |
| Rhea ID | |
| Cross Reference Brenda |