ID A0A2U3UYN4_TURTR Unreviewed; 402 AA.
AC A0A2U3UYN4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Retrotransposon-derived protein PEG10 isoform 2 {ECO:0000313|RefSeq:NP_001278029.1};
GN Name=PEG10 {ECO:0000313|RefSeq:NP_001278029.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:NP_001278029.1};
RN [1] {ECO:0000313|RefSeq:NP_001278029.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17942406; DOI=10.1074/jbc.M705676200;
RA Clark M.B., Janicke M., Gottesbuhren 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 [2] {ECO:0000313|RefSeq:NP_001278029.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20084274;
RA Lux H., Flammann H., Hafner M., Lux A.;
RT "Genetic and molecular analyses of PEG10 reveal new aspects of genomic
RT organization, transcription and translation.";
RL PLoS ONE 5:e8686-e8686(2010).
RN [3] {ECO:0000313|RefSeq:NP_001278029.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; NP_001278029.1; NM_001291100.1.
DR AlphaFoldDB; A0A2U3UYN4; -.
DR GeneID; 101335320; -.
DR CTD; 23089; -.
DR OrthoDB; 1469084at2759; -.
DR Proteomes; UP000245320; Chromosome 9.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR032567; LDOC1-rel.
DR InterPro; IPR005162; Retrotrans_gag_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR PANTHER; PTHR15503:SF31; RETROTRANSPOSON-DERIVED PROTEIN PEG10; 1.
DR Pfam; PF03732; Retrotrans_gag; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 372..386
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 44922 MW; E303A069999128DE CRC64;
MRNKKLLKTK RRKGGRGGQD PGLSPHRSEA ALGRSPPTPP LTLGPDCPPP PPPPPPNDPA
SPSSSPCSGQ RGQYNPNLAE RRREDLSEEI NNLREKVMKQ SEENNNLQNQ VQKLTEENTS
LREQVEPAPE EEEDDIELCG AAAAAAPATP IEEESPEDLP EKFDGNPDML VPFMAQCQLF
MEKSTRDFSI DRVRVCFVTS MMTGRAARWA SAKLERSHYL MHNYPAFMTE MKHVFEDPQR
REAAKRKIRR LRQGMGSVID YSNTFQMIAQ DLDWNEPALI DQYHEGLSDH IQAELSRLEV
TKSLSALIGQ CIHIERRLAR AAAARKPRSP PRALVMPHVN SHHQVDPTEP VGGARMRLTQ
EEKERRRKLN LCLYCGNGGH YADNCPAKAS KASPAGNSPA PL
//
