PEG10_MOUSE
ID PEG10_MOUSE Reviewed; 958 AA.
AC Q7TN75; Q9EQ11;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Retrotransposon-derived protein PEG10 {ECO:0000305};
DE Short=MmPEG10 {ECO:0000303|PubMed:34413232};
DE AltName: Full=Embryonal carcinoma differentiation regulated protein {ECO:0000303|PubMed:11574691};
DE AltName: Full=Mammalian retrotransposon-derived protein 2 {ECO:0000303|PubMed:25888968};
DE AltName: Full=Myelin expression factor 3 {ECO:0000303|PubMed:9473521};
DE Short=MyEF-3 {ECO:0000303|PubMed:9473521};
DE AltName: Full=Myelin expression factor 3-like protein 1;
DE Short=MEF3-like protein 1;
DE AltName: Full=Paternally expressed gene 10 protein {ECO:0000303|PubMed:12840045};
DE AltName: Full=Retrotransposon gag domain-containing protein 3;
DE AltName: Full=Retrotransposon-derived gag-like polyprotein;
DE AltName: Full=Ty3/Gypsy-like protein {ECO:0000303|PubMed:11158386};
GN Name=Peg10 {ECO:0000303|PubMed:12840045, ECO:0000312|MGI:MGI:2157785};
GN Synonyms=Edr {ECO:0000303|PubMed:11574691}, Mar2,
GN Mart2 {ECO:0000303|PubMed:25888968}, Mef3l1, Rgag3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12840045; DOI=10.1101/gr.906803;
RA Ono R., Shiura H., Aburatani H., Kohda T., Kaneko-Ishino T., Ishino F.;
RT "Identification of a large novel imprinted gene cluster on mouse proximal
RT chromosome 6.";
RL Genome Res. 13:1696-1705(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-661.
RC STRAIN=C57BL/6J;
RX PubMed=11158386; DOI=10.1093/oxfordjournals.molbev.a003801;
RA Volff J., Korting C., Schartl M.;
RT "Ty3/Gypsy retrotransposon fossils in mammalian genomes: did they evolve
RT into new cellular functions?";
RL Mol. Biol. Evol. 18:266-270(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 132-364.
RX PubMed=9473521; DOI=10.1006/bbrc.1997.7821;
RA Steplewski A., Krynska B., Tretiakova A., Haas S., Khalili K., Amini S.;
RT "MyEF-3, a developmentally controlled brain-derived nuclear protein which
RT specifically interacts with myelin basic protein proximal regulatory
RT sequences.";
RL Biochem. Biophys. Res. Commun. 243:295-301(1998).
RN [5]
RP PROTEIN SEQUENCE OF 310-329 AND 418-442, IDENTIFICATION BY MASS
RP SPECTROMETRY, RIBOSOMAL FRAMESHIFT, AND DEVELOPMENTAL STAGE.
RX PubMed=17942406; DOI=10.1074/jbc.m705676200;
RA Clark M.B., Jaenicke M., Gottesbuehren U., Kleffmann T., Legge M.,
RA Poole E.S., Tate W.P.;
RT "Mammalian gene PEG10 expresses two reading frames by high efficiency -1
RT frameshifting in embryonic-associated tissues.";
RL J. Biol. Chem. 282:37359-37369(2007).
RN [6]
RP RIBOSOMAL FRAMESHIFT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11574691; DOI=10.1093/nar/29.19.4079;
RA Shigemoto K., Brennan J., Walls E., Watson C.J., Stott D., Rigby P.W.,
RA Reith A.D.;
RT "Identification and characterisation of a developmentally regulated
RT mammalian gene that utilises -1 programmed ribosomal frameshifting.";
RL Nucleic Acids Res. 29:4079-4088(2001).
RN [7]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16423995; DOI=10.1158/0008-5472.can-05-1553;
RA Li C.-M., Margolin A.A., Salas M., Memeo L., Mansukhani M., Hibshoosh H.,
RA Szabolcs M., Klinakis A., Tycko B.;
RT "PEG10 is a c-MYC target gene in cancer cells.";
RL Cancer Res. 66:665-672(2006).
RN [8]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16341224; DOI=10.1038/ng1699;
RA Ono R., Nakamura K., Inoue K., Naruse M., Usami T., Wakisaka-Saito N.,
RA Hino T., Suzuki-Migishima R., Ogonuki N., Miki H., Kohda T., Ogura A.,
RA Yokoyama M., Kaneko-Ishino T., Ishino F.;
RT "Deletion of Peg10, an imprinted gene acquired from a retrotransposon,
RT causes early embryonic lethality.";
RL Nat. Genet. 38:101-106(2006).
RN [9]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=17707377; DOI=10.1016/j.febslet.2007.07.074;
RA Hishida T., Naito K., Osada S., Nishizuka M., Imagawa M.;
RT "peg10, an imprinted gene, plays a crucial role in adipocyte
RT differentiation.";
RL FEBS Lett. 581:4272-4278(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-753; ARG-844 AND ARG-857, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=25888968; DOI=10.1186/s12977-015-0138-8;
RA Henke C., Strissel P.L., Schubert M.T., Mitchell M., Stolt C.C.,
RA Faschingbauer F., Beckmann M.W., Strick R.;
RT "Selective expression of sense and antisense transcripts of the sushi-ichi-
RT related retrotransposon--derived family during mouse placentogenesis.";
RL Retrovirology 12:9-9(2015).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-362 AND LYS-365, AND
RP TISSUE SPECIFICITY.
RX PubMed=30951545; DOI=10.1371/journal.pone.0214110;
RA Abed M., Verschueren E., Budayeva H., Liu P., Kirkpatrick D.S., Reja R.,
RA Kummerfeld S.K., Webster J.D., Gierke S., Reichelt M., Anderson K.R.,
RA Newman R.J., Roose-Girma M., Modrusan Z., Pektas H., Maltepe E., Newton K.,
RA Dixit V.M.;
RT "The Gag protein PEG10 binds to RNA and regulates trophoblast stem cell
RT lineage specification.";
RL PLoS ONE 14:e0214110-e0214110(2019).
RN [14]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RX PubMed=34413232; DOI=10.1126/science.abg6155;
RA Segel M., Lash B., Song J., Ladha A., Liu C.C., Jin X., Mekhedov S.L.,
RA Macrae R.K., Koonin E.V., Zhang F.;
RT "Mammalian retrovirus-like protein PEG10 packages its own mRNA and can be
RT pseudotyped for mRNA delivery.";
RL Science 373:882-889(2021).
CC -!- FUNCTION: Retrotransposon-derived protein that binds its own mRNA and
CC self-assembles into virion-like capsids (PubMed:30951545,
CC PubMed:34413232). Forms virion-like extracellular vesicles that
CC encapsulate their own mRNA and are released from cells, enabling
CC intercellular transfer of PEG10 mRNA (PubMed:34413232). Binds its own
CC mRNA in the 5'-UTR region, in the region near the boundary between the
CC nucleocapsid (NC) and protease (PRO) coding sequences and in the
CC beginning of the 3'-UTR region (PubMed:34413232). Involved in placenta
CC formation: required for trophoblast stem cells differentiation
CC (PubMed:16341224, PubMed:30951545). Involved at the immediate early
CC stage of adipocyte differentiation (PubMed:17707377). Overexpressed in
CC many cancers and enhances tumor progression: promotes cell
CC proliferation by driving cell cycle progression from G0/G1 (By
CC similarity). Enhances cancer progression by inhibiting the TGF-beta
CC signaling, possibly via interaction with the TGF-beta receptor ACVRL1
CC (By similarity). May bind to the 5'-GCCTGTCTTT-3' DNA sequence of the
CC MB1 domain in the myelin basic protein (MBP) promoter; additional
CC evidences are however required to confirm this result (PubMed:9473521).
CC {ECO:0000250|UniProtKB:Q86TG7, ECO:0000269|PubMed:16341224,
CC ECO:0000269|PubMed:17707377, ECO:0000269|PubMed:30951545,
CC ECO:0000269|PubMed:34413232, ECO:0000269|PubMed:9473521}.
CC -!- SUBUNIT: Homooligomer; homooligomerizes into virion-like capsids
CC (PubMed:34413232). Interacts with ACVRL1 (By similarity). Interacts
CC with SIAH1 and SIAH2 (By similarity). {ECO:0000250|UniProtKB:Q86TG7,
CC ECO:0000269|PubMed:34413232}.
CC -!- SUBCELLULAR LOCATION: Extracellular vesicle membrane
CC {ECO:0000269|PubMed:30951545, ECO:0000269|PubMed:34413232}. Cytoplasm
CC {ECO:0000269|PubMed:30951545}. Nucleus {ECO:0000250|UniProtKB:Q86TG7}.
CC Note=Forms virion-like extracellular vesicles that are released from
CC cells. {ECO:0000269|PubMed:30951545, ECO:0000269|PubMed:34413232}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=The ribosomal frameshifting efficiency shows an apparent
CC decrease from 68% at 9.5 dpc to 43% by 21.5 dpc during placenta
CC gestation of isoform 1 compared to isoform 2.
CC {ECO:0000269|PubMed:11574691, ECO:0000269|PubMed:17942406};
CC Name=1; Synonyms=RF1/RF2 {ECO:0000303|PubMed:17942406}, RF1/2
CC {ECO:0000303|PubMed:30951545};
CC IsoId=Q7TN75-1; Sequence=Displayed;
CC Name=2; Synonyms=RF1 {ECO:0000303|PubMed:17942406};
CC IsoId=Q7TN75-2; Sequence=VSP_032009, VSP_032010;
CC -!- TISSUE SPECIFICITY: Expressed in a subset of adult tissues, including
CC brain and testis (PubMed:11574691, PubMed:30951545). Expressed during
CC the early process of adipocyte differentiation (PubMed:17707377).
CC Expressed weakly in mammary gland but strongly in breast carcinomas of
CC a c-MYC-driven transgenic model (PubMed:16423995).
CC {ECO:0000269|PubMed:11574691, ECO:0000269|PubMed:16423995,
CC ECO:0000269|PubMed:17707377, ECO:0000269|PubMed:30951545}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in adrenal gland, testis and
CC placenta (PubMed:30951545). Present at lower level in pituitary, ovary,
CC uterus, white adipose, brain and lung (PubMed:30951545).
CC {ECO:0000269|PubMed:30951545}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in adrenal gland, testis and
CC placenta (PubMed:30951545). Present at lower level in pituitary, ovary,
CC uterus, white adipose, brain and lung (PubMed:30951545).
CC {ECO:0000269|PubMed:30951545}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo, placenta and amniotic
CC membrane at 10.5 dpc (PubMed:17942406, PubMed:25888968). Expressed in
CC placenta at 9.5 dpc and appeared to increase as gestation progresses
CC peaking around 12.5 and 15.5 dpc (at protein level) (PubMed:16341224,
CC PubMed:25888968). Expressed in embryo at 9.5, 12.5 and 16.5 dpc
CC (PubMed:11574691). Expressed in developing musculo-skeletal system,
CC during skeletal myogenesis and also in precartilage primordia and
CC derivative chondrogenic cells of the developing skeleton
CC (PubMed:11574691). Expressed in mesenchymal tissues of developing lung,
CC kidney, gonad, gut and placenta (PubMed:11574691). Not expressed at
CC stages of chondrocyte hypertrophy and ossification of bones
CC (PubMed:11574691). Expressed in all extraembryonic tissues at 9.5 and
CC 12.5 dpc and low-level expression in the embryonic brain and vertebral
CC cartilage at 12.5 dpc (PubMed:11574691). {ECO:0000269|PubMed:11574691,
CC ECO:0000269|PubMed:16341224, ECO:0000269|PubMed:17942406,
CC ECO:0000269|PubMed:25888968}.
CC -!- INDUCTION: Up-regulated by MYC and during adipocyte differentiation.
CC {ECO:0000269|PubMed:16423995, ECO:0000269|PubMed:17707377}.
CC -!- DOMAIN: The protein is evolutionarily related to retrotransposon Gag
CC proteins: it contains the capsid (CA) and nucleocapsid (NC) subdomains
CC of gag. {ECO:0000269|PubMed:34413232}.
CC -!- DOMAIN: [Isoform 1]: In addition to the capsid (CA) and nucleocapsid
CC (NC) subdomains of gag proteins, this isoform contains subdomains of
CC pol, namely a protease (PRO) domain and a predicted reverse
CC transcriptase (RT)-like domain. {ECO:0000269|PubMed:34413232}.
CC -!- PTM: Ubiquitinated (PubMed:30951545). Deubiquitinated at Lys-362 and
CC Lys-365 by USP9X (PubMed:30951545). {ECO:0000269|PubMed:30951545}.
CC -!- PTM: [Isoform 1]: Undergoes proteolytic cleavage.
CC {ECO:0000250|UniProtKB:Q86TG7}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality resulting from placental
CC defects. {ECO:0000269|PubMed:16341224}.
CC -!- BIOTECHNOLOGY: Can be reprogrammed to form virion-like capsids that
CC deliver engineered cargo mRNAs bearing RNA signals from PEG10 5'- and
CC 3'-UTR into target cells. {ECO:0000269|PubMed:34413232}.
CC -!- MISCELLANEOUS: The PEG10 locus is imprinted, giving rise to paternally
CC expressed proteins. {ECO:0000269|PubMed:12840045}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by a -1 ribosomal frameshifting
CC due to a slippery site occurring between the codons for Gly-370 and
CC Lys-371. {ECO:0000269|PubMed:11574691, ECO:0000269|PubMed:17942406}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by conventional translation.
CC {ECO:0000269|PubMed:11574691, ECO:0000269|PubMed:17942406}.
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DR EMBL; AB091827; BAC77244.1; -; mRNA.
DR EMBL; AC084315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF302691; AAG39979.1; -; Genomic_DNA.
DR CCDS; CCDS57407.1; -. [Q7TN75-2]
DR RefSeq; NP_001035701.1; NM_001040611.1. [Q7TN75-2]
DR RefSeq; NP_570947.2; NM_130877.2.
DR AlphaFoldDB; Q7TN75; -.
DR SMR; Q7TN75; -.
DR BioGRID; 228380; 4.
DR IntAct; Q7TN75; 2.
DR STRING; 10090.ENSMUSP00000127306; -.
DR iPTMnet; Q7TN75; -.
DR PhosphoSitePlus; Q7TN75; -.
DR MaxQB; Q7TN75; -.
DR PaxDb; Q7TN75; -.
DR PRIDE; Q7TN75; -.
DR ProteomicsDB; 287820; -. [Q7TN75-1]
DR ProteomicsDB; 287821; -. [Q7TN75-2]
DR Antibodypedia; 30119; 403 antibodies from 34 providers.
DR DNASU; 170676; -.
DR Ensembl; ENSMUST00000176204; ENSMUSP00000134963; ENSMUSG00000092035. [Q7TN75-2]
DR GeneID; 170676; -.
DR KEGG; mmu:170676; -.
DR UCSC; uc033iob.1; mouse. [Q7TN75-2]
DR CTD; 23089; -.
DR MGI; MGI:2157785; Peg10.
DR VEuPathDB; HostDB:ENSMUSG00000092035; -.
DR eggNOG; ENOG502S3G3; Eukaryota.
DR GeneTree; ENSGT00950000183173; -.
DR InParanoid; Q7TN75; -.
DR OMA; RRCRMED; -.
DR OrthoDB; 583605at2759; -.
DR BioGRID-ORCS; 170676; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Peg10; mouse.
DR PRO; PR:Q7TN75; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q7TN75; protein.
DR Bgee; ENSMUSG00000092035; Expressed in ectoplacental cone and 106 other tissues.
DR ExpressionAtlas; Q7TN75; baseline and differential.
DR Genevisible; Q7TN75; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0110077; P:vesicle-mediated intercellular transport; IDA:UniProtKB.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR032567; LDOC1-rel.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR005162; Retrotrans_gag_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR15503; PTHR15503; 1.
DR Pfam; PF03732; Retrotrans_gag; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Differentiation; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Membrane; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosomal frameshifting;
KW RNA-binding; Transport; Transposable element; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..958
FT /note="Retrotransposon-derived protein PEG10"
FT /id="PRO_0000323027"
FT ZN_FING 344..361
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..326
FT /note="Necessary for interaction with ACVRL1"
FT /evidence="ECO:0000250|UniProtKB:Q86TG7"
FT REGION 299..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..958
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 753
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 844
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 857
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:30951545"
FT CROSSLNK 365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:30951545"
FT VAR_SEQ 371..376
FT /note="KLPGPA -> NSPAPL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032009"
FT VAR_SEQ 377..958
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032010"
FT MOD_RES Q7TN75-2:367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 958 AA; 109849 MW; 65BA9B1B6714FE14 CRC64;
MAAAGGSSNC PPPPPPPPPN NNNNNNTPKS PGVPDAEDDD ERRHDELPED INNFDEDMNR
QFENMNLLDQ VELLAQSYSL LDHLDDFDDD DEDDDFDPEP DQDELPEYSD DDDLELQGAA
AAPIPNFFSD DDCLEDLPEK FDGNPDMLGP FMYQCQLFME KSTRDFSVDR IRVCFVTSML
IGRAARWATA KLQRCTYLMH NYTAFMMELK HVFEDPQRRE AAKRKIRRLR QGPGPVVDYS
NAFQMIAQDL DWTEPALMDQ FQEGLNPDIR AELSRQEAPK TLAALITACI HIERRLARDA
AAKPDPSPRA LVMPPNSQTD PTEPVGGARM RLSKEEKERR RKMNLCLYCG NGGHFADTCP
AKASKNSPPG KLPGPAVGGP SATGPERIRS PPSEASTQHL QVMLQIHMPG RPTLFVRAMI
DSGASGNFID QDFVIQNAIP LRIKDWPVMV EAIDGHPIAS GPIILETHHL IVDLGDHREI
LSFDVTQSPF FPIVLGIRWL STHDPHITWS TRSIVFNSDY CRLRCRMFAQ IPSNLLFTVP
QPNLHPYLLH HVHPHVHPHM HQHLHQHLHQ FLHPDPHQYP HPDPHYHHHQ QADMQHQLQQ
YLYQYLYYHL YPVMHHHLPP DQHEHLHEYL HQYLHQYLHQ FLHHHLHPDL HQYLYQYLHN
HMNPDPHHHP HPDPPQDPHH PPHQDPHQHP DPHQDPPHQD PHQDAHQDPH MDPHLHQHQH
PQPQPHPQQH PNHPQQPPFF YHMAGFRIYH PVRYYYIQNV YTPVDEHVYP GHRVVDPNIE
MIPGAHSLPS GHLYSMSESE MNALRNFVDR NVKDGLMTPT VAPNGAQVLQ VKRGWKLQVT
YNCRAPQSGT IQNQYLRMSL PNMGDPAHLA SYGEFVQVPG YPYPAYVYYT SPHMMTAWYP
VGRDVHGRII VVPVVITWSQ NTNRQPPVPQ YPPPQPPPPP PPPPPPPPPP PASSCSAA
