| IED ID | IndEnz0018000894 |
| Enzyme Type ID | peroxidase000894 |
| Protein Name |
Probable oxidoreductase PXDNL EC 1.-.-.- Cardiac peroxidase Inactive peroxidasin-like protein Polysomal ribonuclease 1 PRM1 Vascular peroxidase 2 |
| Gene Name | PXDNL VPO2 |
| 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 | MEPRLFCWTTLFLLAGWCLPGLPCPSRCLCFKSTVRCMHLMLDHIPQVPQQTTVLDLRFNRIREIPGSAFKKLKNLNTLLLNNNHIRKISRNAFEGLENLLYLYLYKNEIHALDKQTFKGLISLEHLYIHFNQLEMLQPETFGDLLRLERLFLHNNKLSKIPAGSFSNLDSLKRLRLDSNALVCDCDLMWLGELLQGFAQHGHTQAAATCEYPRRLHGRAVASVTVEEFNCQSPRITFEPQDVEVPSGNTVYFTCRAEGNPKPEIIWIHNNHSLDLEDDTRLNVFDDGTLMIRNTRESDQGVYQCMARNSAGEAKTQSAMLRYSSLPAKPSFVIQPQDTEVLIGTSTTLECMATGHPHPLITWTRDNGLELDGSRHVATSSGLYLQNITQRDHGRFTCHANNSHGTVQAAANIIVQAPPQFTVTPKDQVVLEEHAVEWLCEADGNPPPVIVWTKTGGQLPVEGQHTVLSSGTLRIDRAAQHDQGQYECQAVSSLGVKKVSVQLTVKPKALAVFTQLPQDTSVEVGKNINISCHAQGEPQPIITWNKEGVQITESGKFHVDDEGTLTIYDAGFPDQGRYECVARNSFGLAVTNMFLTVTAIQGRQAGDDFVESSILDAVQRVDSAINSTRRHLFSQKPHTSSDLLAQFHYPRDPLIVEMARAGEIFEHTLQLIRERVKQGLTVDLEGKEFRYNDLVSPRSLSLIANLSGCTARRPLPNCSNRCFHAKYRAHDGTCNNLQQPTWGAALTAFARLLQPAYRDGIRAPRGLGLPVGSRQPLPPPRLVATVWARAAAVTPDHSYTRMLMHWGWFLEHDLDHTVPALSTARFSDGRPCSSVCTNDPPCFPMNTRHADPRGTHAPCMLFARSSPACASGRPSATVDSVYAREQINQQTAYIDGSNVYGSSERESQALRDPSVPRGLLKTGFPWPPSGKPLLPFSTGPPTECARQEQESPCFLAGDHRANEHLALAAMHTLWFREHNRMATELSALNPHWEGNTVYQEARKIVGAELQHITYSHWLPKVLGDPGTRMLRGYRGYNPNVNAGIINSFATAAFRFGHTLINPILYRLNATLGEISEGHLPFHKALFSPSRIIKEGGIDPVLRGLFGVAAKWRAPSYLLSPELTQRLFSAAYSAAVDSAATIIQRGRDHGIPPYVDFRVFCNLTSVKNFEDLQNEIKDSEIRQKLRKLYGSPGDIDLWPALMVEDLIPGTRVGPTLMCLFVTQFQRLRDGDRFWYENPGVFTPAQLTQLKQASLSRVLCDNGDSIQQVQADVFVKAEYPQDYLNCSEIPKVDLRVWQDCCADCRSRGQFRAVTQESQKKRSAQYSYPVDKDMELSHLRSRQQDKIYVGEDARNVTVLAKTKFSQDFSTFAAEIQETITALREQINKLEARLRQAGCTDVRGVPRKAEERWMKEDCTHCICESGQVTCVVEICPPAPCPSPELVKGTCCPVCRDRGMPSDSPEKR |
| Enzyme Length | 1463 |
| Uniprot Accession Number | A1KZ92 |
| Absorption | |
| Active Site | ACT_SITE 812; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: Probable oxidoreductase (Probable). Lacks peroxidase activity (PubMed:24253521). Inhibits the peroxidase activity of PXDN through its interaction (PubMed:24253521). {ECO:0000269|PubMed:24253521, ECO:0000305|PubMed:24253521}.; FUNCTION: [Isoform PMR1]: Endonuclease selectively degrading some target mRNAs while they are engaged by translating ribosomes, among which albumin and beta-globin mRNAs. {ECO:0000269|PubMed:22543864}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (4); Chain (1); Disulfide bond (10); Domain (7); Erroneous gene model prediction (1); Erroneous initiation (2); Frameshift (1); Glycosylation (1); Metal binding (6); Natural variant (7); Repeat (5); Sequence conflict (2); Signal peptide (1); Site (1) |
| Keywords | Alternative splicing;Calcium;Cell membrane;Cytoplasm;Disulfide bond;Endonuclease;Endoplasmic reticulum;Glycoprotein;Heme;Hydrolase;Immunoglobulin domain;Iron;Leucine-rich repeat;Membrane;Metal-binding;Nuclease;Oxidoreductase;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Increased by Angiotensin-2. {ECO:0000269|PubMed:24253521}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24253521}. Endoplasmic reticulum {ECO:0000269|PubMed:24253521}. Cell membrane {ECO:0000269|PubMed:24253521}.; SUBCELLULAR LOCATION: [Isoform PMR1]: Cytoplasm. Note=Associates with polysomes. |
| Modified Residue | |
| Post Translational Modification | PTM: Phosphorylation by SRC on tyrosine residues is required for targeting to polysomes. {ECO:0000269|PubMed:22543864}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20237496; 20379614; 20800603; 27257068; 28780169; 30622330; |
| Motif | |
| Gene Encoded By | |
| Mass | 163,686 |
| Kinetics | |
| Metal Binding | METAL 813; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 891; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 893; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 895; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 897; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 1057; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | |
| Cross Reference Brenda | 1.11.1.7; |