| IED ID | IndEnz0002012376 |
| Enzyme Type ID | protease012376 |
| Protein Name |
Protein disulfide-isomerase A3 EC 5.3.4.1 58 kDa glucose-regulated protein 58 kDa microsomal protein p58 Disulfide isomerase ER-60 Endoplasmic reticulum resident protein 57 ER protein 57 ERp57 Endoplasmic reticulum resident protein 60 ER protein 60 ERp60 |
| Gene Name | PDIA3 ERP57 ERP60 GRP58 |
| 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 | MRLRRLALFPGVALLLAAARLAAASDVLELTDDNFESRISDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASIVGFFDDSFSEAHSEFLKAASNLRDNYRFAHTNVESLVNEYDDNGEGIILFRPSHLTNKFEDKTVAYTEQKMTSGKIKKFIQENIFGICPHMTEDNKDLIQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGHKLNFAVASRKTFSHELSDFGLESTAGEIPVVAIRTAKGEKFVMQEEFSRDGKALERFLQDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKLNPKKYEGGRELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL |
| Enzyme Length | 505 |
| Uniprot Accession Number | P30101 |
| Absorption | |
| Active Site | ACT_SITE 57; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 60; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 406; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 409; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000269|PubMed:27897272, ECO:0000269|PubMed:7487104}; |
| DNA Binding | |
| EC Number | 5.3.4.1 |
| Enzyme Function | FUNCTION: Disulfide isomerase which catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds (PubMed:7487104, PubMed:27897272). Associates with calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (PubMed:27897272). Association with calcitriol does not affect its enzymatic activity (PubMed:27897272). {ECO:0000269|PubMed:27897272, ECO:0000269|PubMed:7487104}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Beta strand (20); Chain (1); Compositional bias (1); Disulfide bond (4); Domain (2); Helix (18); Modified residue (8); Motif (1); Mutagenesis (6); Natural variant (1); Region (1); Sequence conflict (10); Signal peptide (1); Site (6); Turn (11) |
| Keywords | 3D-structure;Acetylation;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Isomerase;Methylation;Phosphoprotein;Redox-active center;Reference proteome;Repeat;Signal |
| Interact With | P05067; P10909; Q96HE7; Q86YB8; Itself; Q13162; Q13586; Q03518; P18418; P24643 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:23826168}. Endoplasmic reticulum lumen {ECO:0000250}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545). {ECO:0000269|PubMed:12643545}. |
| Modified Residue | MOD_RES 61; /note=N6-methyllysine; /evidence=ECO:0007744|PubMed:24129315; MOD_RES 129; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P27773; MOD_RES 152; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P27773; MOD_RES 218; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P27773; MOD_RES 252; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P27773; MOD_RES 319; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:24275569; MOD_RES 362; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P27773; MOD_RES 494; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P27773 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|PubMed:1286669, ECO:0000269|PubMed:7487104, ECO:0000269|PubMed:9150948, ECO:0000269|PubMed:9399589, ECO:0007744|PubMed:25944712" |
| Structure 3D | NMR spectroscopy (2); Electron microscopy (1); X-ray crystallography (2) |
| Cross Reference PDB | 2ALB; 2DMM; 2H8L; 3F8U; 6ENY; |
| Mapped Pubmed ID | 10064069; 10436013; 10929008; 11842220; 12032078; 12060494; 12162574; 12235131; 12239218; 14508489; 14508490; 14561893; 14681859; 14718384; 14732712; 14871896; 14871899; 15236594; 15286279; 15328618; 15451439; 15862831; 15896298; 16002696; 16193070; 16368681; 16428306; 16465444; 16473882; 16567808; 16962936; 17055437; 17061245; 17150345; 17170699; 17188166; 17456022; 17467700; 17656363; 17728248; 17822402; 17848102; 17964282; 18039656; 18234856; 18650385; 19054761; 19064571; 19135240; 19196713; 19361863; 19367725; 19411306; 19426129; 19701894; 19714814; 19805454; 19851281; 19942855; 19995546; 20029959; 20035634; 20064506; 20195357; 20360068; 2038058; 20506389; 20562859; 20596667; 20596672; 20711500; 20802462; 21050182; 21057456; 21321085; 21362330; 21598303; 21837552; 21917082; 21941299; 21996511; 22045338; 22168334; 22190034; 22207023; 22266712; 22304920; 22322599; 22503978; 22665516; 22923333; 23226417; 23255428; 23587917; 23625662; 23752268; 23781031; 23782473; 23827315; 23957851; 24030382; 24040290; 24490732; 2450918; 24599957; 24815697; 25081282; 25083866; 25221425; 25605256; 25609649; 25837926; 26125904; 26170458; 26214517; 26361352; 26402295; 26435004; 26496610; 26514267; 26638075; 26724776; 26752685; 26771192; 26772958; 26869642; 27079884; 27363653; 27415599; 27492604; 28044092; 28175305; 28373975; 28723413; 29107940; 29207176; 29305423; 29672884; 30431082; 30670593; 30720090; 30720117; 30958660; 31466719; 31747963; 32316996; 32558906; 32585639; 32687065; 33077910; 33153019; 33707747; 33761087; 33785835; 34064874; 34190687; 34212985; 34363072; |
| Motif | MOTIF 502..505; /note=Prevents secretion from ER; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 56,782 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 5.3.4.1; |