| IED ID |
IndEnz0002007442 |
| Enzyme Type ID |
protease007442 |
| Protein Name |
Ovostatin homolog 1
|
| Gene Name |
OVOS1 |
| 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 |
MHVHVCVCLCVCIYTSSCVCACVHMCMRDALLAEGRGGGLAAADDFLYLECCKCFSQESQIAMVCQERSQNETYEVKMNNDTEACRATLNLEERRSVAIRSRENVVFVQTDKPTYKPGQKDVNGIAQFFLDTYTFTYPNITLKDPQNNRIFQRQNVTSFRNITQLSFQLISEPMFGDYWIVVKRNSRETVTHQFAVKRYVLPKFEVTVNAPQTVTISDDEFQVDVCAYNFGQPVQGETQIRVCREYFSSSNCEKNENEICEQFIAQVQTNLDIFTLLCSSFLTVMQISEKTSVFITQLLGTVNFENMDTFYRRGISYFGQLKFSDPNNVPMVNKLLQLELNDEFIGNYTTDENGEAQFSIDTSDIFDPEFNLKVRHQRTEECYLPSWLTPQYLDAHFLVSRFYSRTNSFLKIVPEPKQLECNQQKVVTVHYSLNSEAYEDDSNVKFFYLNGNFSFPISISADLAPAAVLFVYTLHPSGEIVADSVRFQVDKCFKHKVNIKFSNEQGLPGSNASLCLQAAPVLFCALRAVDRNVLLLKSEQQLSAESVSSLYNMVPSIEPYGYFYHGLNLDDGKEDPCIPQRDMFYNGLYYTPVSNYGDGDIYNIVRVRSLRILENIIQTVRTNFPETWMWDLVSVSSSGSANLSFLIPDTITQWEASGFCVNGDVGFGISSTTTLEVSQPFFIEIASPFSVVQNEQFDLIVNVFSYRNTCVEVSYIWECLPGKVNITVVAESKQSSACPNEGMEQQKLNWKDTVVQSFLVEFLFLGDILGLALQNLVVLQMPYGSGEQNAALLASDTYVLDYLKSTEQLTEEVQSKAFFLSILGYQRQLSFKNSDGSYSVFWQQSQKGSIWLSALTFKTLERMKKYVFIDENVQKQTLIWLSSQQKTSGCFKNDGQLFNHALRNALFCLEAALDSGVTNGYNHAILAYAFALAGKEKQVESLLQTLDQSAPKLSKRYYWERERKPKTEEFPSFIPWAPSAQTEKSCYVLLAVISRKIPDLTYASKIVQWLAQRMNSHGGFSSNQVINVGLILIAARGEEGLFSKDQNTVTFSSEGSSEIFQVNGHNRLLVQRSEVTQAPGEYTVDVEGHGCTFIQIFRYTGIRNKSSMVVIDVKMLSGFTPTMSSIEEVNNRSLIFQHKDSYIEYKRADSFPFSVEQSNLVFNIQPAPAMVYDYYEKGRQATAMP |
| Enzyme Length |
1185 |
| Uniprot Accession Number |
Q6IE37 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. {ECO:0000250}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Glycosylation (5); Signal peptide (1) |
| Keywords |
Bait region;Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue |
|
| Post Translational Modification |
|
| Signal Peptide |
SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
|
| Gene Encoded By |
|
| Mass |
134,499 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|