ID A0A096P519_PAPAN Unreviewed; 2132 AA.
AC A0A096P519;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 54.
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:ENSPANP00000020444.1};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000020444.1, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000020444.1, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000020444.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_003903908.1; XM_003903859.3.
DR STRING; 9555.ENSPANP00000020444; -.
DR Ensembl; ENSPANT00000002760.3; ENSPANP00000020444.1; ENSPANG00000022122.3.
DR GeneID; 101000648; -.
DR KEGG; panu:101000648; -.
DR CTD; 80312; -.
DR eggNOG; ENOG502QURD; Eukaryota.
DR GeneTree; ENSGT00940000158935; -.
DR HOGENOM; CLU_001618_2_0_1; -.
DR OMA; VKEQLMH; -.
DR OrthoDB; 5406604at2759; -.
DR Proteomes; UP000028761; Chromosome 11.
DR Bgee; ENSPANG00000022122; Expressed in postnatal subventricular zone and 43 other cell types or tissues.
DR ExpressionAtlas; A0A096P519; baseline.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
DR GO; GO:0008327; F:methyl-CpG binding; IEA:Ensembl.
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:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0080111; P:DNA demethylation; IEA:UniProtKB-UniRule.
DR GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin formation; IEA:Ensembl.
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 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:UP000028761};
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 584..625
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1774..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..1980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2070..2091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1970
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2132 AA; 235026 MW; 4CBA52A40D393BD8 CRC64;
MSRSRHARPS RLVRKEDVNK KKKNSQLRKT TKGANKNVAS VKTLSPGKLK QLIQERDVKK
KTEPKPPMPV RSLLTRAGAA RMNLDRTEVL FQNPESLTCN GFTMALRSTS LSRRLSQPPL
VIAKSKKVPL SKGLEKQHDC DYKILPDLGV KHSENDSVPT QDTQVLPDIE TLISIQNPSL
LKGKSQETTQ SWSQRVEDSK INIPTHSGPA AEILPGPLEG TCCDEGLFSE ETFNDTSGSP
KMFAQDTVCA PFPQRATPKV TSQGNPSIQL EELGSRVESL KLSDSYLDPI KSEHNCYPTS
SLNKVIPELN LRNCLALGGS TSPTSVIKFL LAGSKQATLG AKPDHQEAFK ATANQQEVSD
TTSFLGQAFG AIPHQWELPG ADPVHGEALR ETPDLPEIRG AIPVQGEVFG TILDQQETLG
MSGSVVPDLP VFLPVSPNPV ATFNAPSKWP EPQGAVSYGL AVQGAIQILP LGSGHTPQSS
SISEKNSLPP VMAISNVENE KQVHISFLPA NTQGFPLAPE RGLFHASLGM AQLSQAGPSK
SDRGSSQVSV TSTVHVVNTT VVTIPVPMVS TSSSSYTTLL PTLEKKKRKR CGVCEPCQQK
TNCGECTYCK NRKNSHQICK KRKCEELKKK PSVLVPLEVI KENKRPQREK KPKVLKADFD
NKPVNGPKSE SMDYSRCGHG EEQKLELNPH PVENVTKNED SMTGIEVEKW TQNKKSHLTD
HVKGDFSANV PEAEKSKNSE VDKKQTKSPK LFVQTIRNGI KHVHCLPAET NVSFKKFNIE
EFGKTLENSS YKFLKDTANH NNAMSSVATD MSCDHLKGRS NVLVFQQPGF NCNSIPHSSH
SNIHRHASIH NEGDQPKTPE NIPSKEPKDG SPVQPSLLSL MKDRRLTLEQ VVAIEALTQL
SEAPSENSSP SKSEKDEESE QRTASLLNSC KAILYTVRKD LQDPNLQGEP QKLHHCPSLE
KQSSCNTVVF NGQANSHISS ATNQASTKSH EYSKLTNSLS LFIPKSNSPK IDTNKSIAQG
IITLDNCSND LHQLPPRNNE VEYCNQLLDS SKNLDSDDLS CQDATHTQIE EDVATQLTQL
ASIIKFNYIK SEDKNVESTP TSLVTCNAQQ KYNQEKGTIQ QKPPSSVHNN HGSSLTKQKN
PAQKKTKSTP SRERRKKKPT VVSYQENDQQ KWEKLSYMYG TICDIWIASK FQNFGQFCPH
DFPTVFGKIS SSTKIWKPLA QTRSIMQPKT VFPPLTQIKL QRYPESAEEK MKVEPLDSLS
LFHLKTESNG KAFTDKAYNS QVQLTVNANQ KAHPLTQPSS PPHQCANVMA GDDQIRFQQV
VKEQLMDQRL PTLPGISQET PLPESALTLR NVNVVCSGGI TVVSTKSEEE VCSSSVGTSE
FSTVDSAQKN FNDYAMNFFT NPTKNLVSVT KDSELPTCNC LDRVIQKDKG PYYTHLGAGP
SVAAVREIME NRYGQKGNAI RIEIVVYTGK EGKSSHGCPI AKWVLRRSSD EEKVLCLVRQ
RTGHHCPTAV MVVLIMVWDG IPLPMADRLY TELTENLKSY NGHPTDRRCT LNENRTCTCQ
GIDPETCGAS FSFGCSWSMY FNGCKFGRSP SPRRFRIDPS SPLHEKNLED NLQSLATRLA
PIYKQYAPVA YQNQVEYENV ARECRLGSKE GRPFSGVTAC LDFCAHPHRD IHNMNNGSTV
VCTLTREDNR SLGVIPQDEQ LHVLPLYKLS DTDEFGSKEG MEAKIKSGAI EVLAPRRKKR
TCFTQPVPRS GKKRAAMMTE VLAHKIRAVE KKPIPRVKRK SNSTTTNNSK ASPLPALGSK
TETVQPEVKS ETEPHFILKS SDNTKTYSLM PSAPHPVKEA SPVFSWSPKT ASATPAPLKN
DAAASCGFSE RSSTPHCTMS LGRLSGANAA AVEGPGISQL GEAAPLPTLS APVMEPLVNS
EPPTGVTEPL TSHQPNHQPS FLTSPQDLDS SPMEEDEQHS EADEPPSDEP LSDDPLSPAE
EKLPHIDEYW SDSEHIFLDA NIGGVAIAPA HGSVLIECAR RELHATTPVE HPNRNHPTRL
SLVFYQHKNL NKPQHGFELN KIKFEAKEAK NKKMKASEQK DQAANEGPEL SSEVNELNQI
PSHKALTLTH DNVVTVSPYA LTHVAGPYNH WV
//
