ID D4YW73_SHEEP Unreviewed; 1333 AA.
AC D4YW73;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Retrotransposon-like 1 {ECO:0000313|EMBL:ADE59015.1};
GN Name=PEG11 {ECO:0000313|EMBL:ADE59015.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|EMBL:ADE59015.1};
RN [1] {ECO:0000313|EMBL:ADE59015.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11337479; DOI=10.1101/gr.172701;
RA Charlier C., Segers K., Wagenaar D., Karim L., Berghmans S., Jaillon O.,
RA Shay T., Weissenbach J., Cockett N., Gyapay G., Georges M.;
RT "Human-ovine comparative sequencing of a 250-kb imprinted domain
RT encompassing the callipyge (clpg) locus and identification of six imprinted
RT transcripts: DLK1, DAT, GTL2, PEG11, antiPEG11, and MEG8.";
RL Genome Res. 11:850-862(2001).
RN [2] {ECO:0000313|EMBL:ADE59015.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12586730;
RA Smit M., Segers K., Carrascosa L.G., Shay T., Baraldi F., Gyapay G.,
RA Snowder G., Georges M., Cockett N., Charlier C.;
RT "Mosaicism of Solid Gold supports the causality of a noncoding A-to-G
RT transition in the determinism of the callipyge phenotype.";
RL Genetics 163:453-456(2003).
RN [3] {ECO:0000313|EMBL:ADE59015.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16690740; DOI=10.1073/pnas.0602844103;
RA Takeda H., Caiment F., Smit M., Hiard S., Tordoir X., Cockett N.,
RA Georges M., Charlier C.;
RT "The callipyge mutation enhances bidirectional long-range DLK1-GTL2
RT intergenic transcription in cis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8119-8124(2006).
RN [4] {ECO:0000313|EMBL:ADE59015.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20944086; DOI=10.1101/gr.108787.110;
RA Caiment F., Charlier C., Hadfield T., Cockett N., Georges M., Baurain D.;
RT "Assessing the effect of the CLPG mutation on the microRNA catalog of
RT skeletal muscle using high-throughput sequencing.";
RL Genome Res. 20:1651-1662(2010).
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DR EMBL; AF354168; ADE59015.1; -; Genomic_DNA.
DR CDD; cd00303; retropepsin_like; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR032549; DUF4939.
DR InterPro; IPR032567; LDOC1-rel.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR041577; RT_RNaseH_2.
DR PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR PANTHER; PTHR15503:SF40; RETROTRANSPOSON-LIKE PROTEIN 1; 1.
DR Pfam; PF16297; DUF4939; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE 4: Predicted;
FT DOMAIN 183..267
FT /note="DUF4939"
FT /evidence="ECO:0000259|Pfam:PF16297"
FT DOMAIN 832..928
FT /note="Reverse transcriptase/retrotransposon-derived
FT protein RNase H-like"
FT /evidence="ECO:0000259|Pfam:PF17919"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..124
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1333 AA; 151029 MW; 2F4827F7B7410392 CRC64;
MIEPSEDSFE TMMERKNPSS KQMESSEGSS ETTVETPPGG RAEAAGLAGG LAQETGEQSI
DLRQDMEEPS SGPHREIKDP PNDLLQDLEE SCEGCHLEEG GPFGGAPGGM EEEEEDNPWE
SQEDQDYYTD LAESEEDESP EEPDSSTVEV MGMVRSIISL YFRMQDLREQ QRVAEEILMN
AINKGQLPTP KQFSGDRREY HEFIVLCQLI LQSYPRVFCN DRLRVGYVIS HLSGMAMEWA
SDLVEKESSM IDDFPAFLEA MNDTFEYRQA LRVAEDAMFN LRQGDRAAIE YINEFQSLVP
TLGWPDEVLQ AHLCQGLKED IRQYLFSIPQ PNSLENLIAL VLQIEDKLAE RRAMLRLAPE
ARPRHLTWLD SPVPERWTVS TWLPNEFHPG IKRKHLFLLL LVRVNPYHSV AVQALVDSGA
TSNYMDEGFA QEHYVELYQK PYAELVQTAD GSLVGNEPVW LYTEPLVCLH QNHQESLEFD
IVASSKFSVI LGIKWLQLHA PDIDWVKGRC TFHSPYCLKN CFRPPPPCIA LEHHAVSLLP
GLPHQYSDLA DVFNPKEADE ETSDQPSSDG SDDLSESEPS ELQQAGDSDQ SEETFYDCAS
TAPWEPVDAG VQEKAKQEEF WDLQDMLTSR HDYIQMIPEL FDQLHGATWF TKLELRGTIV
EESMDIHQTE DVWKVAFGLE LQEMASYQPF LICADPIIPQ GVIHFILKDM IGLFVISYGQ
DVLVYSMSQE EHYHHVRQVL VRFRYHHVYC SLQRSQFHRH TAEFLGFVVT PKGVRLNKSI
VSTITGYPTP GSRKSLRNLM EFAFPYRHFV ERFADITEPL VRQLRADQPF DWGDKEQEAF
VGLKRAFRKA PLLYHPKPQN QFYLQTGVTK TSLYASLIQM DKRTGKKACC AFYSRNISPM
EVEASLAEMK ILPIRAAFMV WCRYLENTEE PIMILLNKED LASLNNDRLT VLLPGHWVFF
FAHFNFDVKE MPTSEDAQPL PRRQRLRKRA QQSQAATTTR PTMLVTMRGP PGGQSPESEN
EEESEDALHP DEPNGQNLQH GLLALIPVDQ IFNSFLAHFS MAQIRAVMLH FYRSLLLWKN
LLAMAALLVM LRFRRRLALL PAPAADPARP PPQRSLRLFL DASLLTSSGI ASAVTQLFTQ
MPPLVGANAL PPEELAELFL GPRPWQLHSL HGLRITPSFW QMLCQFFGIG GPALEGTQTH
PSPRLVPHVE GDDCVVLRDA LQDDLQRFRQ CGLHDGLQDT SQDAQDAQGG AWARRPLQHP
PTQAEALARL ADIRSTQGLS IVTHRELMAR ALTDFLAAVS TQALPTLVEA SPPSERATLE
ELPSDSDEDA DLD
//
