ID W5P511_SHEEP Unreviewed; 2138 AA.
AC W5P511;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Methylcytosine dioxygenase TET {ECO:0000256|RuleBase:RU367064};
DE EC=1.14.11.80 {ECO:0000256|RuleBase:RU367064};
GN Name=TET1 {ECO:0000313|Ensembl:ENSOARP00000005514.1};
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|Ensembl:ENSOARP00000005514.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000005514.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000005514.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000005514.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Dioxygenase that catalyzes the conversion of the modified
CC genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC)
CC and plays a key role in epigenetic chromatin reprogramming during
CC embryonic development. {ECO:0000256|RuleBase:RU367064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a 5-formyl-2'-deoxycytidine in DNA + O2 = a
CC 5-carboxyl-2'-deoxycytidine in DNA + CO2 + H(+) + succinate;
CC Xref=Rhea:RHEA:53832, Rhea:RHEA-COMP:13656, Rhea:RHEA-COMP:13657,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:137731,
CC ChEBI:CHEBI:137732; EC=1.14.11.80;
CC Evidence={ECO:0000256|ARBA:ARBA00034983,
CC ECO:0000256|RuleBase:RU367064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a 5-hydroxymethyl-2'-deoxycytidine in DNA +
CC O2 = a 5-formyl-2'-deoxycytidine in DNA + CO2 + H2O + succinate;
CC Xref=Rhea:RHEA:53828, Rhea:RHEA-COMP:13315, Rhea:RHEA-COMP:13656,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:136731,
CC ChEBI:CHEBI:137731; EC=1.14.11.80;
CC Evidence={ECO:0000256|ARBA:ARBA00034995,
CC ECO:0000256|RuleBase:RU367064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a
CC 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate;
CC Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEBI:136731;
CC EC=1.14.11.80; Evidence={ECO:0000256|ARBA:ARBA00036153,
CC ECO:0000256|RuleBase:RU367064};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU367064};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|RuleBase:RU367064};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU367064};
CC Note=The zinc ions have a structural role.
CC {ECO:0000256|RuleBase:RU367064};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the TET family. {ECO:0000256|ARBA:ARBA00007502,
CC ECO:0000256|RuleBase:RU367064}.
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DR EMBL; AMGL01071313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01071314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01071315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01071316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01071317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004021676.2; XM_004021627.3.
DR SMR; W5P511; -.
DR STRING; 9940.ENSOARP00000005514; -.
DR PaxDb; 9940-ENSOARP00000005514; -.
DR Ensembl; ENSOART00000005601.1; ENSOARP00000005514.1; ENSOARG00000005141.1.
DR GeneID; 101103534; -.
DR KEGG; oas:101103534; -.
DR CTD; 80312; -.
DR eggNOG; ENOG502QURD; Eukaryota.
DR HOGENOM; CLU_001618_2_0_1; -.
DR OMA; VKEQLMH; -.
DR OrthoDB; 5406604at2759; -.
DR Proteomes; UP000002356; Chromosome 25.
DR Bgee; ENSOARG00000005141; Expressed in embryo and 54 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0070579; F:methylcytosine dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006211; P:5-methylcytosine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0080111; P:DNA demethylation; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR InterPro; IPR024779; 2OGFeDO_JBP1/TET_oxygenase_dom.
DR InterPro; IPR040175; TET1/2/3.
DR InterPro; IPR046942; TET_oxygenase.
DR InterPro; IPR002857; Znf_CXXC.
DR PANTHER; PTHR23358:SF2; METHYLCYTOSINE DIOXYGENASE TET1; 1.
DR PANTHER; PTHR23358; UNCHARACTERIZED; 1.
DR Pfam; PF12851; Tet_JBP; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM01333; Tet_JBP; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Dioxygenase {ECO:0000256|RuleBase:RU367064};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU367064};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367064};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367064};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367064};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 581..622
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1909..1986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2066..2093
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1915..1952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1977
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2138 AA; 235933 MW; A883736F9C480349 CRC64;
MSRSRHARPS KLVRREDLNK KKNNQLKKGS KPANKNVATV KTVSPGKLKQ FVQERDVKKK
TEPKLTVPVR SLLTRAGAAR MNLDRTEVLF QNPESLTCNG FTMALRSTSL SRRLSQPPVV
IARPKKVPPP KNLGKQHECD YKVLTDMGVK HSENDSVPMQ DPPVPPDIEK LIGIKNASFI
KDKSQETTQS WSQGVEDSKI ICSTPSDPAA EILSGSLEGT CGGERLFSRE TLNNISDSPR
MFAQDTVCVP LLQRAALKVT SEGNPSIQLE DLGSRVESLK LSDSYLDPIK SEHGCCPTSS
FNKVVPALDL RNCLSIGGSI YPTSLIKLFL AGSEQETLGA KPDHQEVLKA TPDQQEVPDT
TPVLGQAVSA VPHQWEVPGA NPVHGEPLGE TLDPPEIPGA IPVQGEVFGA ILSQQVLGMG
SGTASDPPIF LPAPHNPVAT CNALPAWPEP QGTVSSGLEV PDTMQILPSG SGHTPQPSSN
SEIILVPPVI PMNNIENEKK VHISLLPAHT QGFTLAPERG LQPAPQGIAQ LSLVSPSTLE
GRSSQVSATS MVDINTTVVS RPVPLASTSS PSYTTLLPTL EKKKRKRCGV CEPCQQKTNC
GECTYCKNRK NSHQICKKRK CEELKKKPSV IVSLEVVKEN KRPQREKKPK VLKADFDNKL
VNGPKSESME YSSCAHEEEQ RLELNSCPLE NVTKNEESMT GIEVENWTQN KKSHLTDHVK
GEFSTVKTEV ENLKNSEDDR KKILLTDLLE PQKLFAQTVR NGIKNVHYLP TETNLSFKKI
NIEELGKAFE SNPYKFLKDT ANHNNVMSTI ATSGSCDHLK GKSNVLVIQK PGFNCKSFPD
PVNCNSNSHT SIHNESDQPK SLEIIANRDL KEGSTLQPSL LSLMKDRRLT LEQVVAIEAL
TQLSEAPSEN SSPSKSEKDE ETEQRTASLL NSCKAILYSV RKDLQDPNLK GEPQSLHHCP
SLEKQSSCNA VVFNGQNIIS KSHNSSPSDQ ASTKAQESST VTNSISLLIP NSNSSKTDTN
KNIAQGRITL DSSRSLQPLT TITSKSEYCN QSLDNSIKLD SKDDSSCQDS VHSKIEEDVA
AQLTQLASMI KFNYVKPEDK KVESTPISLV AYNVQQKYNQ EMGTPPQKPP SNVQNNQGSS
VTKQKNTIQK KTKATPSRDR RKKKHMVISC QENDQKKQEQ LSYEYSKLHD IWIASKFQRF
GQFGPHDFPI LLGKIPPLTK VWKPLTQTSS ALEHKKLFPP LAQIKFERYY PELAQEKMKV
EPLDSIPIIQ LKTESNGQAF TENAYTQVQP TVNVNQKAHP LLQPASPTNQ CANVLDGSDQ
RQFQEDVKDQ LMHQRLPTSP GISHETPLPD PAQILRNLNV VCSGGITVVS TKNEEDVCSS
SVGTSEFPPI NSAQKTFNDY AMNFFTNSTK TLVSTTKDSE LPTCNCLDRV IQKDKGPYYT
HLGAGPSVAA VREIMENRYG QKGNAIRIEI VVYTGKEGKS SNGCPVAKWV LRRSSDEEKV
LCLVRQRTGH HCPTAVMVVL IMVWDGIPLP MADKLYSQLT ESLKSYNGHP TDRRCTLNEN
RTCTCQGIDP ETCGASFSFG CSWSMYFNGC KFGRSPSPRR FRIDPSSPLH EKNLEDNLQS
LATELAPIYK QYAPAAYQNQ VALEHIAREC RLGKKEGRPF SGVTACLDFC AHPHRDIHNM
NNGSTVVCTL TREDNRSFGV IPQDEQLHVL PLYKLSDTDE FGSREGMEAK IKSGAIMVLA
PRQKKRMRFT QPVPRSGKKR AAMMTEVLAH KIRAVEKKFI PRIKRKNNSM TNNSKASSLP
LLGNKTETVQ PEIKSETEPH LIFKGSDNTK SYSPAPFIPH PVKEENLAPA FSWSSKTALV
TTAPFKNDAS LSYGFSERGS NPHCIMPSAR HSGANVAAGE CSEIAQPGEM VPLPTLSTPM
TNSLGYSEPP IGPSEQLTSN QPNQQPPFIT SPHELASSLV EEDEQPSEAD EPPSDDPLSD
DPLSPAEEKL PHIVEYWSDS EHIFLDANVG GVAIAPSHGS VLIECARREL HATTPVDHPN
RNHPTRLSLV FYQHKNLNKP QHGFELNKIK FEAKEAKNKK TKASEQKDQA ANEGIELTEV
NEFSQIPSHK ALTLTHDNVV TVSPYALTHV AGPYNHWV
//
