ID A0A2K5UZ42_MACFA Unreviewed; 736 AA.
AC A0A2K5UZ42;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE RecName: Full=YTH domain-containing family protein {ECO:0000256|RuleBase:RU369095};
GN Name=YTHDC1 {ECO:0000313|Ensembl:ENSMFAP00000017745.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000017745.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000017745.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000017745.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSMFAP00000017745.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-
CC containing RNAs, and regulates mRNA stability. M6A is a modification
CC present at internal sites of mRNAs and some non-coding RNAs and plays a
CC role in mRNA stability and processing. {ECO:0000256|RuleBase:RU369095}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the YTHDF family.
CC {ECO:0000256|RuleBase:RU369095}.
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DR RefSeq; XP_005555239.1; XM_005555182.5.
DR AlphaFoldDB; A0A2K5UZ42; -.
DR SMR; A0A2K5UZ42; -.
DR STRING; 9541.ENSMFAP00000017745; -.
DR Ensembl; ENSMFAT00000068287.2; ENSMFAP00000017745.1; ENSMFAG00000031927.2.
DR GeneID; 102130625; -.
DR CTD; 91746; -.
DR VEuPathDB; HostDB:ENSMFAG00000031927; -.
DR GeneTree; ENSGT00940000155803; -.
DR OMA; RKTRMTS; -.
DR OrthoDB; 5842105at2759; -.
DR Proteomes; UP000233100; Chromosome 5.
DR Bgee; ENSMFAG00000031927; Expressed in lung and 13 other cell types or tissues.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA reader activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0006376; P:mRNA splice site recognition; IEA:Ensembl.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:TreeGrafter.
DR CDD; cd21134; YTH; 1.
DR FunFam; 3.10.590.10:FF:000002; YTH domain-containing protein 1 isoform X1; 1.
DR Gene3D; 3.10.590.10; ph1033 like domains; 1.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR PANTHER; PTHR12357:SF3; YTH DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR12357; YTH YT521-B HOMOLOGY DOMAIN-CONTAINING; 1.
DR Pfam; PF04146; YTH; 1.
DR PROSITE; PS50882; YTH; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU369095}.
FT DOMAIN 356..493
FT /note="YTH"
FT /evidence="ECO:0000259|PROSITE:PS50882"
FT REGION 1..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..326
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 85745 MW; 46CDDBAF3C8EE33B CRC64;
MAADSREEKD GELNVLDDIL TEVPEQDDEL YNPESEQDKN EKKGSKRKSD RMESTDTKRQ
KPSVHSRQLV SKPLSSSVSN NKRIVSTKGK SVTEYKNEEY QRSERNKRLD ADRKIRLSSS
ASREPYKNQP EKTCVRKRDP ERRAKSPTPD GSERIGLEVD RRASRSSQSS KEEVNSEEYG
SDHETGSSGS SDEQGNNTEN EEEGVEEDVE EDEEVEEDAE EDEEVDEDGE EEEEEEEEEE
EEEEEEEEEE YEQDERDQKE EGNDYDTRSE ASDSGSESVS FTDGSVRSGS GTDGSDEKKK
ERKRARGISP IVFDRSGSSA SESYAGSEKK HEKLSSSVRA VRKDQTSKLK YVLQDARFFL
IKSNNHENVS LAKAKGVWST LPVNEKKLNL AFRSARSVIL IFSVRESGKF QGFARLSSES
HHGGSPIHWV LPAGMSAKML GGVFKIDWIC RRELPFTKSA HLTNPWNEHK PVKIGRDGQE
IELECGTQLC LLFPPDESID LYQVIHKMRH KRRMHSQPRS RGRPSRREPV RDVGRRRPED
YDIHNSRKKP RIDYPPEFHQ RPGYLKDPRY QEVDSFTNLI PNRRFSGVRR DVFLNGSYND
YVREFHNMGP PPPWQGMPPY PGMEQPPHHP YYQHHAPPPQ AHPPYSGHHP VPHEARYRDK
RVHDYDMRVD DFLRRTQAVV SGRRSRPRER DRERERDRPR DNRRDRERDR GRDRERERER
LCDRDRDRGE RGRYRR
//
