| IED ID | IndEnz0002006340 |
| Enzyme Type ID | protease006340 |
| Protein Name |
Protein disulfide-isomerase A6 EC 5.3.4.1 Endoplasmic reticulum protein 5 ER protein 5 ERp5 Protein disulfide isomerase P5 Thioredoxin domain-containing protein 7 |
| Gene Name | PDIA6 ERP5 P5 TXNDC7 |
| 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 | MALLVLGLVSCTFFLAVNGLYSSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNRPEDYQGGRTGEAIVDAALSALRQLVKDRLGGRSGGYSSGKQGRSDSSSKKDVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGESPVDYDGGRTRSDIVSRALDLFSDNAPPPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGFGYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFPTIVEREPWDGRDGELPVEDDIDLSDVELDDLGKDEL |
| Enzyme Length | 440 |
| Uniprot Accession Number | Q15084 |
| Absorption | |
| Active Site | ACT_SITE 55; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 58; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 190; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 193; /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:12204115, ECO:0000269|PubMed:15466936}; |
| DNA Binding | |
| EC Number | 5.3.4.1 |
| Enzyme Function | FUNCTION: May function as a chaperone that inhibits aggregation of misfolded proteins (PubMed:12204115). Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (PubMed:24508390). May also regulate the UPR via the EIF2AK3 UPR sensor (PubMed:24508390). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (PubMed:15466936). {ECO:0000269|PubMed:12204115, ECO:0000269|PubMed:15466936, ECO:0000269|PubMed:24508390}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Alternative sequence (4); Beta strand (9); Chain (1); Disulfide bond (2); Domain (2); Helix (9); Modified residue (4); Motif (1); Mutagenesis (6); Natural variant (1); Region (1); Sequence conflict (2); Signal peptide (1); Site (6); Turn (6) |
| Keywords | 3D-structure;Alternative splicing;Cell membrane;Chaperone;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Isomerase;Membrane;Phosphoprotein;Redox-active center;Reference proteome;Repeat;Signal |
| Interact With | P05067; O43681; P11021; Q13162; Q96EQ0 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15466936}. Cell membrane {ECO:0000269|PubMed:15466936}. 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 129; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 156; /note="Phosphoserine; by FAM20C"; /evidence="ECO:0000269|PubMed:26091039"; MOD_RES 158; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 428; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence="ECO:0000269|PubMed:15466936, ECO:0000269|PubMed:19892738, ECO:0007744|PubMed:25944712" |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (4) |
| Cross Reference PDB | 1X5D; 3VWW; 3W8J; 4EF0; 4GWR; |
| Mapped Pubmed ID | 17215244; 17353931; 19135240; 19738201; 19887585; 20000738; 20360068; 20379614; 20562859; 20711500; 20953506; 21057456; 21988832; 22106087; 22167753; 22190034; 22215138; 22645275; 22665516; 22936677; 23289620; 23606334; 23663784; 23949117; 24136289; 24189400; 24464223; 24843047; 25015719; 25604459; 25609649; 26125904; 26514267; 26638075; 26655997; 26676989; 26752685; 27462866; 27540907; 27760590; 28866093; 28949004; 29932420; 30431130; 30922965; 30958660; 33761940; 9058200; |
| Motif | MOTIF 437..440; /note=Prevents secretion from ER; /evidence=ECO:0000255|PROSITE-ProRule:PRU10138 |
| Gene Encoded By | |
| Mass | 48,121 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |