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Database: UniProt
Entry: A0A4U5TUZ4_COLLU
LinkDB: A0A4U5TUZ4_COLLU
Original site: A0A4U5TUZ4_COLLU 
ID   A0A4U5TUZ4_COLLU        Unreviewed;       653 AA.
AC   A0A4U5TUZ4;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   08-OCT-2025, entry version 23.
DE   RecName: Full=YTH domain-containing family protein {ECO:0000256|RuleBase:RU369095};
GN   ORFNames=D9C73_028342 {ECO:0000313|EMBL:TKS65263.1};
OS   Collichthys lucidus (Big head croaker) (Sciaena lucida).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Collichthys.
OX   NCBI_TaxID=240159 {ECO:0000313|EMBL:TKS65263.1, ECO:0000313|Proteomes:UP000298787};
RN   [1] {ECO:0000313|EMBL:TKS65263.1, ECO:0000313|Proteomes:UP000298787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JT15FE1705JMU {ECO:0000313|EMBL:TKS65263.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TKS65263.1};
RA   Cai M., Xiao S.;
RT   "Genome Assembly of Collichthys lucidus.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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   EMBL; ML240575; TKS65263.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U5TUZ4; -.
DR   STRING; 240159.A0A4U5TUZ4; -.
DR   Proteomes; UP000298787; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; IEA:TreeGrafter.
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:0000398; P:mRNA splicing, via spliceosome; IEA:TreeGrafter.
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:UP000298787};
KW   RNA-binding {ECO:0000256|RuleBase:RU369095}.
FT   DOMAIN          278..415
FT                   /note="YTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50882"
FT   REGION          1..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..44
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..64
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..154
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..200
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..244
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..435
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..573
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  75042 MW;  81285CDAE1B60391 CRC64;
     MMSCITLRLN ETSVTRKRKS ERSDSQDLKR LRPSSGHAPS RSSSTNKRAP GPPLSSSSKK
     AASSPRGRHA AATSSYRHEY YEERRGRRGA REATRSRGGE EVRRRESQRG LEGLTQKLRR
     TSPSPHEEDN QSEDEAAAEY GSEAGSGSSS PAASHVEEEE DDDQEEEEEE EEEEGMEEEE
     EEEEEEGEKE DEEEEEEEEE YERRGGEGND YDTRSEAGDS RSASSVSFSD DGESVHSGSA
     SEASGSEKKR EKLSSSVRAV RKGMENPTSK LRYILRDARF FLIKSNNHEN VSLAKAKGVW
     STLPVNEKKL NAAFRSARSV VLVFSVRESG KFQGFARLAS ESHHGGSPIH WVLPAGMNAK
     MLGGVFKIDW LCRRELPFTK TAHLSNPWNE HKPVKIGRDG QEIQPDIGAQ LCALFPLDES
     VDVHQVARRV RHKRRTPSEP RPRGRPPQRE PGRRRPEEYD LHGRKRPRAD GPPDFNQRAG
     FIQDLRNQPV DRRFSSVRRD VFLNGSYNDY MRDYHHSVGP PAPWQTLAAY PGVEQPPPHH
     PPYYHHSHPP PPPHQAYHHH HHPPLPQHEA PPPRFRDKQR APQHRAFTSS PHDYDMRVDD
     FLRRTQAVVS SRRERERQRE RERGGPRRER ERERARDRER ERERDKERGR YRR
//
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