IED ID | IndEnz0002000536 |
Enzyme Type ID | protease000536 |
Protein Name |
Retrotransposon-derived protein PEG10 Embryonal carcinoma differentiation-regulated protein Mammalian retrotransposon-derived protein 2 Myelin expression factor 3-like protein 1 MEF3-like protein 1 Paternally expressed gene 10 protein Retrotransposon gag domain-containing protein 3 Retrotransposon-derived gag-like polyprotein Ty3/Gypsy-like protein |
Gene Name | PEG10 EDR KIAA1051e MAR2 MART2 MEF3L1 RGAG3 |
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 | MTERRRDELSEEINNLREKVMKQSEENNNLQSQVQKLTEENTTLREQVEPTPEDEDDDIELRGAAAAAAPPPPIEEECPEDLPEKFDGNPDMLAPFMAQCQIFMEKSTRDFSVDRVRVCFVTSMMTGRAARWASAKLERSHYLMHNYPAFMMEMKHVFEDPQRREVAKRKIRRLRQGMGSVIDYSNAFQMIAQDLDWNEPALIDQYHEGLSDHIQEELSHLEVAKSLSALIGQCIHIERRLARAAAARKPRSPPRALVLPHIASHHQVDPTEPVGGARMRLTQEEKERRRKLNLCLYCGTGGHYADNCPAKASKSSPAGKLPGPAVEGPSATGPEIIRSPQDDASSPHLQVMLQIHLPGRHTLFVRAMIDSGASGNFIDHEYVAQNGIPLRIKDWPILVEAIDGRPIASGPVVHETHDLIVDLGDHREVLSFDVTQSPFFPVVLGVRWLSTHDPNITWSTRSIVFDSEYCRYHCRMYSPIPPSLPPPAPQPPLYYPVDGYRVYQPVRYYYVQNVYTPVDEHVYPDHRLVDPHIEMIPGAHSIPSGHVYSLSEPEMAALRDFVARNVKDGLITPTIAPNGAQVLQVKRGWKLQVSYDCRAPNNFTIQNQYPRLSIPNLEDQAHLATYTEFVPQIPGYQTYPTYAAYPTYPVGFAWYPVGRDGQGRSLYVPVMITWNPHWYRQPPVPQYPPPQPPPPPPPPPPPPSYSTL |
Enzyme Length | 708 |
Uniprot Accession Number | Q86TG7 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Retrotransposon-derived protein that binds its own mRNA and self-assembles into virion-like capsids (PubMed:34413232). Forms virion-like extracellular vesicles that encapsulate their own mRNA and are released from cells, enabling intercellular transfer of PEG10 mRNA (PubMed:34413232). Binds its own mRNA in the 5'-UTR region, in the region near the boundary between the nucleocapsid (NC) and protease (PRO) coding sequences and in the beginning of the 3'-UTR region (PubMed:34413232). Involved in placenta formation: required for trophoblast stem cells differentiation (By similarity). Involved at the immediate early stage of adipocyte differentiation (By similarity). Overexpressed in many cancers and enhances tumor progression: promotes cell proliferation by driving cell cycle progression from G0/G1 (PubMed:12810624, PubMed:16423995, PubMed:26235627, PubMed:28193232). Enhances cancer progression by inhibiting the TGF-beta signaling, possibly via interaction with the TGF-beta receptor ACVRL1 (PubMed:15611116, PubMed:26235627, PubMed:30094509). May bind to the 5'-GCCTGTCTTT-3' DNA sequence of the MB1 domain in the myelin basic protein (MBP) promoter; additional evidences are however required to confirm this result (By similarity). {ECO:0000250|UniProtKB:Q7TN75, ECO:0000269|PubMed:12810624, ECO:0000269|PubMed:15611116, ECO:0000269|PubMed:16423995, ECO:0000269|PubMed:26235627, ECO:0000269|PubMed:28193232, ECO:0000269|PubMed:30094509, ECO:0000269|PubMed:34413232}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (4); Chain (1); Coiled coil (1); Compositional bias (1); Cross-link (2); Erroneous translation (1); Modified residue (5); Mutagenesis (1); Region (4); Zinc finger (1) |
Keywords | 3D-structure;Alternative initiation;Apoptosis;Coiled coil;Cytoplasm;DNA-binding;Differentiation;Isopeptide bond;Membrane;Metal-binding;Methylation;Nucleus;Phosphoprotein;RNA-binding;Reference proteome;Ribosomal frameshifting;Transport;Transposable element;Ubl conjugation;Zinc;Zinc-finger |
Interact With | Q13137; O95751; Q8N448; Q17RB0; A6ZKI3; Q8IUQ4; Q9H0E2; Q9NQT4; O95751; Q96QF0-7; Q9BWD3; Q17RB0; A6ZKI3 |
Induction | INDUCTION: Expression is directly regulated by E2F1 and E2F4, which bind to its promoter and direct its expression (PubMed:17050006, PubMed:18625225, PubMed:28193232, PubMed:28992046). Up-regulated by MYC (PubMed:16423995). Strongly overepressed in a number of tumors, such has hepatocellular carcinoma (HCC), pancreatic or neuroendocrine prostate cancers (PubMed:20362226, PubMed:26235627, PubMed:28193232). {ECO:0000269|PubMed:16423995, ECO:0000269|PubMed:17050006, ECO:0000269|PubMed:18625225, ECO:0000269|PubMed:20362226, ECO:0000269|PubMed:26235627, ECO:0000269|PubMed:28193232, ECO:0000269|PubMed:28992046}. |
Subcellular Location | SUBCELLULAR LOCATION: Extracellular vesicle membrane {ECO:0000269|PubMed:34413232}. Cytoplasm {ECO:0000269|PubMed:12810624, ECO:0000269|PubMed:15611116, ECO:0000269|PubMed:16423995, ECO:0000269|PubMed:17621626}. Nucleus {ECO:0000269|PubMed:12810624}. Note=Forms virion-like extracellular vesicles that are released from cells (PubMed:34413232). Detected predominantly in the cytoplasm of breast and prostate carcinomas, in hepatocellular carcinoma (HCC) and B-cell chronic lymphocytic leukemia (B-CLL) cells and in the Hep-G2 cell line (PubMed:12810624). {ECO:0000269|PubMed:12810624, ECO:0000269|PubMed:34413232}. |
Modified Residue | MOD_RES 507; /note="Omega-N-methylarginine"; /evidence="ECO:0000250|UniProtKB:Q7TN75"; MOD_RES 598; /note="Omega-N-methylarginine"; /evidence="ECO:0000250|UniProtKB:Q7TN75"; MOD_RES 611; /note="Omega-N-methylarginine"; /evidence="ECO:0000250|UniProtKB:Q7TN75"; MOD_RES Q86TG7-2:316; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES Q86TG7-2:321; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231" |
Post Translational Modification | PTM: [Isoform 1]: Undergoes proteolytic cleavage. {ECO:0000269|PubMed:17942406}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 7LGA; |
Mapped Pubmed ID | 14576465; 15231748; 15767280; 16225771; 18550496; 20460050; 20484977; 20711500; 21205473; 21455631; 21516116; 21767414; 21903422; 21988832; 22137777; 22673314; 23414517; 23902751; 25199998; 25416956; 25497084; 25526181; 25665578; 25687862; 26496610; 26680220; 26934961; 27370270; 28004118; 29044189; 29727698; 30450735; 30953817; 31241046; 31318088; 31530569; 31702614; 32244497; 32847979; 33149023; 33391523; 33515207; |
Motif | |
Gene Encoded By | |
Mass | 80,173 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |