Q7TN75 · PEG10_MOUSE
- ProteinRetrotransposon-derived protein PEG10
- GenePeg10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids958 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Retrotransposon-derived protein that binds its own mRNA and self-assembles into virion-like capsids (PubMed:30951545, 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 (PubMed:16341224, PubMed:30951545).
Involved at the immediate early stage of adipocyte differentiation (PubMed:17707377).
Overexpressed in many cancers and enhances tumor progression: promotes cell proliferation by driving cell cycle progression from G0/G1 (By similarity).
Enhances cancer progression by inhibiting the TGF-beta signaling, possibly via interaction with the TGF-beta receptor ACVRL1 (By similarity).
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 (PubMed:9473521).
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 (PubMed:16341224, PubMed:30951545).
Involved at the immediate early stage of adipocyte differentiation (PubMed:17707377).
Overexpressed in many cancers and enhances tumor progression: promotes cell proliferation by driving cell cycle progression from G0/G1 (By similarity).
Enhances cancer progression by inhibiting the TGF-beta signaling, possibly via interaction with the TGF-beta receptor ACVRL1 (By similarity).
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 (PubMed:9473521).
Miscellaneous
The PEG10 locus is imprinted, giving rise to paternally expressed proteins.
Biotechnology
Can be reprogrammed to form virion-like capsids that deliver engineered cargo mRNAs bearing RNA signals from PEG10 5'- and 3'-UTR into target cells.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular vesicle | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | mRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | apoptotic process | |
Biological Process | cell differentiation | |
Biological Process | mRNA transport | |
Biological Process | placenta development | |
Biological Process | protein homooligomerization | |
Biological Process | vesicle-mediated intercellular transport | |
Biological Process | viral translational frameshifting |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameRetrotransposon-derived protein PEG10
- Short namesMmPEG10
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ7TN75
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Forms virion-like extracellular vesicles that are released from cells.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryonic lethality resulting from placental defects.
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000323027 | 1-958 | Retrotransposon-derived protein PEG10 | |||
Sequence: MAAAGGSSNCPPPPPPPPPNNNNNNNTPKSPGVPDAEDDDERRHDELPEDINNFDEDMNRQFENMNLLDQVELLAQSYSLLDHLDDFDDDDEDDDFDPEPDQDELPEYSDDDDLELQGAAAAPIPNFFSDDDCLEDLPEKFDGNPDMLGPFMYQCQLFMEKSTRDFSVDRIRVCFVTSMLIGRAARWATAKLQRCTYLMHNYTAFMMELKHVFEDPQRREAAKRKIRRLRQGPGPVVDYSNAFQMIAQDLDWTEPALMDQFQEGLNPDIRAELSRQEAPKTLAALITACIHIERRLARDAAAKPDPSPRALVMPPNSQTDPTEPVGGARMRLSKEEKERRRKMNLCLYCGNGGHFADTCPAKASKNSPPGKLPGPAVGGPSATGPERIRSPPSEASTQHLQVMLQIHMPGRPTLFVRAMIDSGASGNFIDQDFVIQNAIPLRIKDWPVMVEAIDGHPIASGPIILETHHLIVDLGDHREILSFDVTQSPFFPIVLGIRWLSTHDPHITWSTRSIVFNSDYCRLRCRMFAQIPSNLLFTVPQPNLHPYLLHHVHPHVHPHMHQHLHQHLHQFLHPDPHQYPHPDPHYHHHQQADMQHQLQQYLYQYLYYHLYPVMHHHLPPDQHEHLHEYLHQYLHQYLHQFLHHHLHPDLHQYLYQYLHNHMNPDPHHHPHPDPPQDPHHPPHQDPHQHPDPHQDPPHQDPHQDAHQDPHMDPHLHQHQHPQPQPHPQQHPNHPQQPPFFYHMAGFRIYHPVRYYYIQNVYTPVDEHVYPGHRVVDPNIEMIPGAHSLPSGHLYSMSESEMNALRNFVDRNVKDGLMTPTVAPNGAQVLQVKRGWKLQVTYNCRAPQSGTIQNQYLRMSLPNMGDPAHLASYGEFVQVPGYPYPAYVYYTSPHMMTAWYPVGRDVHGRIIVVPVVITWSQNTNRQPPVPQYPPPQPPPPPPPPPPPPPPPPASSCSAA | ||||||
Cross-link | 362 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 365 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 367 | In isoform Q7TN75-2; Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 753 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 844 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 857 | Omega-N-methylarginine | ||||
Sequence: R |
Post-translational modification
Isoform 1
Undergoes proteolytic cleavage.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in a subset of adult tissues, including brain and testis (PubMed:11574691, PubMed:30951545).
Expressed during the early process of adipocyte differentiation (PubMed:17707377).
Expressed weakly in mammary gland but strongly in breast carcinomas of a c-MYC-driven transgenic model (PubMed:16423995).
Expressed during the early process of adipocyte differentiation (PubMed:17707377).
Expressed weakly in mammary gland but strongly in breast carcinomas of a c-MYC-driven transgenic model (PubMed:16423995).
Isoform 1
Expressed in adrenal gland, testis and placenta (PubMed:30951545).
Present at lower level in pituitary, ovary, uterus, white adipose, brain and lung (PubMed:30951545).
Present at lower level in pituitary, ovary, uterus, white adipose, brain and lung (PubMed:30951545).
Isoform 2
Expressed in adrenal gland, testis and placenta (PubMed:30951545).
Present at lower level in pituitary, ovary, uterus, white adipose, brain and lung (PubMed:30951545).
Present at lower level in pituitary, ovary, uterus, white adipose, brain and lung (PubMed:30951545).
Induction
Up-regulated by MYC and during adipocyte differentiation.
Developmental stage
Expressed in embryo, placenta and amniotic membrane at 10.5 dpc (PubMed:17942406, PubMed:25888968).
Expressed in placenta at 9.5 dpc and appeared to increase as gestation progresses peaking around 12.5 and 15.5 dpc (at protein level) (PubMed:16341224, PubMed:25888968).
Expressed in embryo at 9.5, 12.5 and 16.5 dpc (PubMed:11574691).
Expressed in developing musculo-skeletal system, during skeletal myogenesis and also in precartilage primordia and derivative chondrogenic cells of the developing skeleton (PubMed:11574691).
Expressed in mesenchymal tissues of developing lung, kidney, gonad, gut and placenta (PubMed:11574691).
Not expressed at stages of chondrocyte hypertrophy and ossification of bones (PubMed:11574691).
Expressed in all extraembryonic tissues at 9.5 and 12.5 dpc and low-level expression in the embryonic brain and vertebral cartilage at 12.5 dpc (PubMed:11574691).
Expressed in placenta at 9.5 dpc and appeared to increase as gestation progresses peaking around 12.5 and 15.5 dpc (at protein level) (PubMed:16341224, PubMed:25888968).
Expressed in embryo at 9.5, 12.5 and 16.5 dpc (PubMed:11574691).
Expressed in developing musculo-skeletal system, during skeletal myogenesis and also in precartilage primordia and derivative chondrogenic cells of the developing skeleton (PubMed:11574691).
Expressed in mesenchymal tissues of developing lung, kidney, gonad, gut and placenta (PubMed:11574691).
Not expressed at stages of chondrocyte hypertrophy and ossification of bones (PubMed:11574691).
Expressed in all extraembryonic tissues at 9.5 and 12.5 dpc and low-level expression in the embryonic brain and vertebral cartilage at 12.5 dpc (PubMed:11574691).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-58 | Disordered | ||||
Sequence: MAAAGGSSNCPPPPPPPPPNNNNNNNTPKSPGVPDAEDDDERRHDELPEDINNFDEDM | ||||||
Compositional bias | 8-24 | Pro residues | ||||
Sequence: SNCPPPPPPPPPNNNNN | ||||||
Compositional bias | 33-57 | Basic and acidic residues | ||||
Sequence: VPDAEDDDERRHDELPEDINNFDED | ||||||
Region | 84-110 | Disordered | ||||
Sequence: LDDFDDDDEDDDFDPEPDQDELPEYSD | ||||||
Region | 131-326 | Necessary for interaction with ACVRL1 | ||||
Sequence: DDCLEDLPEKFDGNPDMLGPFMYQCQLFMEKSTRDFSVDRIRVCFVTSMLIGRAARWATAKLQRCTYLMHNYTAFMMELKHVFEDPQRREAAKRKIRRLRQGPGPVVDYSNAFQMIAQDLDWTEPALMDQFQEGLNPDIRAELSRQEAPKTLAALITACIHIERRLARDAAAKPDPSPRALVMPPNSQTDPTEPVG | ||||||
Region | 299-337 | Disordered | ||||
Sequence: DAAAKPDPSPRALVMPPNSQTDPTEPVGGARMRLSKEEK | ||||||
Zinc finger | 344-361 | CCHC-type | ||||
Sequence: NLCLYCGNGGHFADTCPA | ||||||
Region | 360-396 | Disordered | ||||
Sequence: PAKASKNSPPGKLPGPAVGGPSATGPERIRSPPSEAS | ||||||
Region | 661-739 | Disordered | ||||
Sequence: HMNPDPHHHPHPDPPQDPHHPPHQDPHQHPDPHQDPPHQDPHQDAHQDPHMDPHLHQHQHPQPQPHPQQHPNHPQQPPF | ||||||
Compositional bias | 662-719 | Basic and acidic residues | ||||
Sequence: MNPDPHHHPHPDPPQDPHHPPHQDPHQHPDPHQDPPHQDPHQDAHQDPHMDPHLHQHQ | ||||||
Region | 921-958 | Disordered | ||||
Sequence: NTNRQPPVPQYPPPQPPPPPPPPPPPPPPPPASSCSAA | ||||||
Compositional bias | 926-958 | Pro residues | ||||
Sequence: PPVPQYPPPQPPPPPPPPPPPPPPPPASSCSAA |
Domain
The protein is evolutionarily related to retrotransposon Gag proteins: it contains the capsid (CA) and nucleocapsid (NC) subdomains of gag.
Isoform 1
In addition to the capsid (CA) and nucleocapsid (NC) subdomains of gag proteins, this isoform contains subdomains of pol, namely a protease (PRO) domain and a predicted reverse transcriptase (RT)-like domain.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Ribosomal frameshifting. The ribosomal frameshifting efficiency shows an apparent decrease from 68% at 9.5 dpc to 43% by 21.5 dpc during placenta gestation of isoform 1 compared to isoform 2.
Q7TN75-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsRF1/RF2, RF1/2
- NoteProduced by a -1 ribosomal frameshifting due to a slippery site occurring between the codons for Gly-370 and Lys-371.
- Length958
- Mass (Da)109,849
- Last updated2008-03-18 v2
- Checksum65BA9B1B6714FE14
Q7TN75-2
- Name2
- SynonymsRF1
- NoteProduced by conventional translation.
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BJQ1 | H3BJQ1_MOUSE | Peg10 | 604 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 8-24 | Pro residues | ||||
Sequence: SNCPPPPPPPPPNNNNN | ||||||
Compositional bias | 33-57 | Basic and acidic residues | ||||
Sequence: VPDAEDDDERRHDELPEDINNFDED | ||||||
Alternative sequence | VSP_032009 | 371-376 | in isoform 2 | |||
Sequence: KLPGPA → NSPAPL | ||||||
Alternative sequence | VSP_032010 | 377-958 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 662-719 | Basic and acidic residues | ||||
Sequence: MNPDPHHHPHPDPPQDPHHPPHQDPHQHPDPHQDPPHQDPHQDAHQDPHMDPHLHQHQ | ||||||
Compositional bias | 926-958 | Pro residues | ||||
Sequence: PPVPQYPPPQPPPPPPPPPPPPPPPPASSCSAA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB091827 EMBL· GenBank· DDBJ | BAC77244.1 EMBL· GenBank· DDBJ | mRNA | ||
AC084315 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF302691 EMBL· GenBank· DDBJ | AAG39979.1 EMBL· GenBank· DDBJ | Genomic DNA |