IED ID | IndEnz0001000040 |
Enzyme Type ID | amylase000040 |
Protein Name |
Protein sel-1 homolog 1 Suppressor of lin-12-like protein 1 Sel-1L |
Gene Name | Sel1l Sel1h |
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 | MQVRVRLSLLLLCAVLLGSAAATSDDKTNQDDSLDSKSSLPTDESVKDHTTTGKVVAGQIFVDSEEAEVESLLQDEEDSSKTQEEEISFLESPNPSSKTYEELKRVRKPVLTAIEGTAHGEPCHFPFLFLDKEYDECTSDGREDGRLWCATTYDYKTDEKWGFCETEEDAAKRRQMQEAEMIYQAGMKILNGSNRKSQKREAYRYLQKAAGMNHTKALERVSYALLFGDYLTQNIQAAKEMFEKLTEEGSPKGQTGLGFLYASGLGVNSSQAKALVYYTFGALGGNLIAHMILGYRYWAGIGVLQSCESALTHYRLVANHVASDISLTGGSVVQRIRLPDEVENPGMNSGMLEEDLIQYYQFLAEKGDVQAQVGLGQLHLHGGRGVEQNHQRAFDYFNLAANAGNSHAMAFLGKMYSEGSDIVPQSNETALHYFKKAADMGNPVGQSGLGMAYLYGRGVQVNYDLALKYFQKAAEQGWVDGQLQLGSMYYNGIGVKRDYKQALKYFNLASQGGHILAFYNLAQMHASGTGVMRSCHTAVELFKNVCERGRWSERLMTAYNSYKDEDYNAAVVQYLLLAEQGYEVAQSNAAFILDQREATIVGENETYPRALLHWNRAASQGYTVARIKLGDYHFYGFGTDVDYETAFIHYRLASEQQHSAQAMFNLGYMHEKGLGIKQDIHLAKRFYDMAAEASPDAQVPVFLALCKLGVVYFLQYIREANIRDLFTQLDMDQLLGPEWDLYLMTIIALLLGTVIAYRQRQHQDIPVPRPPGPRPAPPQQEGPPEQQPPQ |
Enzyme Length | 790 |
Uniprot Accession Number | Q9Z2G6 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:25066055, PubMed:24453213). Enhances SYVN1 stability (PubMed:24453213). Plays a role in LPL maturation and secretion (PubMed:25066055). Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells (PubMed:20170518, PubMed:24453213). May play a role in Notch signaling (PubMed:20170518). {ECO:0000269|PubMed:20170518, ECO:0000269|PubMed:24453213, ECO:0000269|PubMed:25066055}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (1); Beta strand (3); Chain (1); Compositional bias (2); Disulfide bond (2); Domain (1); Glycosylation (5); Helix (10); Modified residue (1); Mutagenesis (4); Region (7); Repeat (11); Signal peptide (1); Topological domain (2); Transmembrane (1) |
Keywords | 3D-structure;Alternative splicing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Membrane;Notch signaling pathway;Phosphoprotein;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UBV2}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9UBV2}. |
Modified Residue | MOD_RES 64; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UBV2 |
Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:25066055}. |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 5B26; |
Mapped Pubmed ID | 10746565; 11217851; 12466851; 12520002; 12904583; 14517990; 16615898; 20197277; 20562862; 21454627; 21536682; 21677750; 24324549; 24952961; 26496610; 26551274; 26631554; 26857093; 27568564; 28248965; 28816361; 28920918; 28920920; 29457782; 29558472; 30389665; 30626610; 31477895; 32182217; |
Motif | |
Gene Encoded By | |
Mass | 88,340 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |