| IED ID |
IndEnz0002004582 |
| Enzyme Type ID |
protease004582 |
| Protein Name |
Protein OS-9
|
| Gene Name |
Os9 |
| Organism |
Mus musculus (Mouse) |
| 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
Glires (Rodents and rabbits)
Rodentia
Myomorpha (mice and others)
Muroidea
Muridae
Murinae
Mus
Mus
Mus musculus (Mouse)
|
| Enzyme Sequence |
MAAEVLLSSLLGLLFLGLLLPARLTGGVGSLNLEELSEMRYGIQILPLPVMGGQSQASDVVVVSSKYKQRYECRLPAGAIHFQREREEETPAYQGPGIPELLSPMRDAPCLLKTKDWWTYEFCYGRHIQQYHMEDSEIKGDVLYLGHYQSSFNWDDETAKASKQHRLKRYHSQTYGNGSKCDLNGKPREAEVRFLCDEGAGISGDYIDRVDEPVSCSYVLTIRTSRLCPHPLLRPPASAAPQAILCHPALQPDEYMAYLQRQAESKQHEEKTTEEVQDTDRQVWSGSKAAGAPPKKEDVSPAKEEKESELWKLQGPEEQAAAREEAQAGEQDLNHEAAADPAPSPPNDFQNNVQVKLIRSPADLIRLIEELKAAEKGKPSVRREQPGDDTTEAPQREAEGTKAKGKDGEPPGLMEEEDGDDEEEEEEEEEDEEEQQLLGEFEKELEGMLLPSNRERLRSEVKAGMERELENIIQETEKELDPEGLRKESEREQAILALTSTLDKLIKRLQENQSPELVQKYKKRRVVPQKPPPSPHPTEEEPEHRVRVRVTKLRPGGPNRDLTVLEMNRENPQLKQIEGLVTEVLEREGLTAEGKIEIKIVRPGAEGKEEDTRWLTDEDTRNLKEIFFNILVQGAEEANKERQRQSELESNYRRVWGSPGGEDTGDLDEFDF |
| Enzyme Length |
672 |
| Uniprot Accession Number |
Q8K2C7 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
BINDING 117; /note=A mannooligosaccharide derivative; /evidence=ECO:0000250|UniProtKB:Q13438; BINDING 118; /note=A mannooligosaccharide derivative; /evidence=ECO:0000250|UniProtKB:Q13438; BINDING 130; /note=A mannooligosaccharide derivative; /evidence=ECO:0000250|UniProtKB:Q13438; BINDING 182; /note=A mannooligosaccharide derivative; /evidence=ECO:0000250|UniProtKB:Q13438; BINDING 188; /note=A mannooligosaccharide derivative; /evidence=ECO:0000250|UniProtKB:Q13438; BINDING 212; /note=A mannooligosaccharide derivative; /evidence=ECO:0000250|UniProtKB:Q13438; BINDING 218; /note=A mannooligosaccharide derivative; /evidence=ECO:0000250|UniProtKB:Q13438 |
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4 (By similarity). {ECO:0000250}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Alternative sequence (1); Binding site (7); Chain (1); Compositional bias (4); Disulfide bond (3); Domain (1); Glycosylation (1); Region (4); Sequence conflict (2); Signal peptide (1) |
| Keywords |
Alternative splicing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Lectin;Reference proteome;Signal |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. |
| Modified Residue |
|
| Post Translational Modification |
PTM: Intramolecular disulfide bonds. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000269|PubMed:19084021}. |
| Signal Peptide |
SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
10725249;
11217851;
12466851;
12520002;
14610273;
14681479;
17932042;
18417469;
21267068;
21523322;
21677750;
26721884;
29097366;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
76,108 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|