Detail Information for IndEnz0002000536
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