| IED ID | IndEnz0002008667 |
| Enzyme Type ID | protease008667 |
| Protein Name |
Protein OS-9 Amplified in osteosarcoma 9 |
| Gene Name | OS9 |
| 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 | MAAETLLSSLLGLLLLGLLLPASLTGGVGSLNLEELSEMRYGIEILPLPVMGGQSQSSDVVIVSSKYKQRYECRLPAGAIHFQREREEETPAYQGPGIPELLSPMRDAPCLLKTKDWWTYEFCYGRHIQQYHMEDSEIKGEVLYLGYYQSAFDWDDETAKASKQHRLKRYHSQTYGNGSKCDLNGRPREAEVRFLCDEGAGISGDYIDRVDEPLSCSYVLTIRTPRLCPHPLLRPPPSAAPQAILCHPSLQPEEYMAYVQRQADSKQYGDKIIEELQDLGPQVWSETKSGVAPQKMAGASPTKDDSKDSDFWKMLNEPEDQAPGGEEVPAEEQDPSPEAADSASGAPNDFQNNVQVKVIRSPADLIRFIEELKGGTKKGKPNIGQEQPVDDAAEVPQREPEKERGDPERQREMEEEEDEDEDEDEDEDERQLLGEFEKELEGILLPSDRDRLRSEVKAGMERELENIIQETEKELDPDGLKKESERDRAMLALTSTLNKLIKRLEEKQSPELVKKHKKKRVVPKKPPPSPQPTEEDPEHRVRVRVTKLRLGGPNQDLTVLEMKRENPQLKQIEGLVKELLEREGLTAAGKIEIKIVRPWAEGTEEGARWLTDEDTRNLKEIFFNILVPGAEEAQKERQRQKELESNYRRVWGSPGGEGTGDLDEFDF |
| Enzyme Length | 667 |
| Uniprot Accession Number | Q13438 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 117; /note="A mannooligosaccharide derivative"; /evidence="ECO:0000269|PubMed:21172656, ECO:0007744|PDB:3AIH"; BINDING 118; /note="A mannooligosaccharide derivative"; /evidence="ECO:0000269|PubMed:21172656, ECO:0007744|PDB:3AIH"; BINDING 130; /note="A mannooligosaccharide derivative"; /evidence="ECO:0000269|PubMed:21172656, ECO:0007744|PDB:3AIH"; BINDING 182; /note="A mannooligosaccharide derivative"; /evidence="ECO:0000269|PubMed:21172656, ECO:0007744|PDB:3AIH"; BINDING 188; /note="A mannooligosaccharide derivative"; /evidence="ECO:0000269|PubMed:21172656, ECO:0007744|PDB:3AIH"; BINDING 212; /note="A mannooligosaccharide derivative"; /evidence="ECO:0000269|PubMed:21172656, ECO:0007744|PDB:3AIH"; BINDING 218; /note="A mannooligosaccharide derivative"; /evidence="ECO:0000269|PubMed:21172656, ECO:0007744|PDB:3AIH" |
| 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. {ECO:0000269|PubMed:17932042, ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19084021, ECO:0000269|PubMed:19346256, ECO:0000269|PubMed:21172656}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (6); Beta strand (8); Binding site (7); Chain (1); Compositional bias (4); Disulfide bond (3); Domain (1); Glycosylation (1); Helix (1); Mutagenesis (1); Natural variant (3); Region (5); Sequence conflict (6); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Alternative splicing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Lectin;Reference proteome;Signal |
| Interact With | Q9GZT9; Q9H6Z9; O75460-1; Q16665; Q9UBV2 |
| Induction | INDUCTION: Up-regulated in response to endoplasmic reticulum stress (at protein level). {ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19084021}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19084021}. |
| Modified Residue | |
| Post Translational Modification | PTM: Intramolecular disulfide bonds.; PTM: Isoform 1 and isoform 2 are N-glycosylated. {ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19084021}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3AIH; |
| Mapped Pubmed ID | 11146634; 11812794; 12747754; 15231748; 15611333; 15721254; 16169070; 16901789; 18711132; 18716059; 18952287; 18985028; 19002207; 19914915; 1998343; 20549515; 20711500; 20936779; 21357747; 21404621; 21559462; 21988832; 22190034; 23097496; 23232094; 23414517; 23719536; 23867461; 24019521; 24685677; 2475911; 24795221; 24899641; 24910992; 25314054; 2570460; 25999789; 26496610; 26638075; 28419469; 29706535; 32437666; 7523390; 7529176; 7553863; 7553864; |
| Motif | |
| Gene Encoded By | |
| Mass | 75,562 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |