ID A0A6P3Q8G8_PTEVA Unreviewed; 580 AA.
AC A0A6P3Q8G8;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=YTH domain-containing family protein {ECO:0000256|RuleBase:RU369095};
GN Name=YTHDF2 {ECO:0000313|RefSeq:XP_011356062.1};
OS Pteropus vampyrus (Large flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Pteropodinae; Pteropus.
OX NCBI_TaxID=132908 {ECO:0000313|Proteomes:UP000515202, ECO:0000313|RefSeq:XP_011356062.1};
RN [1] {ECO:0000313|RefSeq:XP_011356062.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_011356062.1};
RG RefSeq;
RL Submitted (AUG-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: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Cytoplasm, Stress granule
CC {ECO:0000256|ARBA:ARBA00004210}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the YTHDF family. YTHDF2 subfamily.
CC {ECO:0000256|ARBA:ARBA00038031}.
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DR RefSeq; XP_011356062.1; XM_011357760.2.
DR AlphaFoldDB; A0A6P3Q8G8; -.
DR SMR; A0A6P3Q8G8; -.
DR GeneID; 105290541; -.
DR KEGG; pvp:105290541; -.
DR CTD; 51441; -.
DR OMA; SPQARPX; -.
DR OrthoDB; 306690at2759; -.
DR Proteomes; UP000515202; Unplaced.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0062153; F:C5-methylcytidine-containing RNA reader activity; 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:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:Ensembl.
DR GO; GO:0061157; P:mRNA destabilization; IEA:Ensembl.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
DR GO; GO:1903679; P:positive regulation of cap-independent translational initiation; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IEA:Ensembl.
DR GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:2000232; P:regulation of rRNA processing; IEA:Ensembl.
DR GO; GO:0007284; P:spermatogonial cell division; IEA:Ensembl.
DR GO; GO:0034063; P:stress granule assembly; IEA:Ensembl.
DR CDD; cd21134; YTH; 1.
DR FunFam; 3.10.590.10:FF:000001; YTH domain family 1, isoform CRA_a; 1.
DR Gene3D; 3.10.590.10; ph1033 like domains; 1.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR PANTHER; PTHR12357:SF8; YTH DOMAIN-CONTAINING FAMILY PROTEIN 2; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000515202};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU369095}.
FT DOMAIN 411..545
FT /note="YTH"
FT /evidence="ECO:0000259|PROSITE:PS50882"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..350
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..372
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 62462 MW; BC0D523505F79CFA CRC64;
MSASSLLEQR PKGQGNKVQN GSVHQKDGLN DDDFEPYLSP QARPNNAYTA MSDSYLPSYY
SPSIGFSYSL GEAAWSTGGD TAMPYLTSYG QLSNGEPHFL PDAMFGQPGA LGSTPFLGQH
GFNFFPSGID FSAWGNNSSQ GQSTQSSGYS SNYAYAPSSL GGAMIDGQSA FASETLNKAP
GMNTIDQGMA ALKLGSTEVA SNVPKVVGSA VGSGSITSNI VASNSLPPAT IAPPKPASWA
DIASKPAKQQ PKLKTKNGIA GSSLPPPPIK HNMDIGTWDN KGPVAKAPSQ ALVQNIGQQP
TQGSPQPVGQ QVNNSPPVAH ASVGQQTQPL PPPPPQPAQL SVQQQAAQST RWVAPRNRGS
GFGHNGVDGN GVGQSQAGSG STPSEPHPVL EKLRSINNYN PKDFDWNLKH GRVFIIKSYS
EDDIHRSIKY NIWCSTEHGN KRLDAAYRSM NGKGPVYLLF SVNGSGHFCG VAEMKSAVDY
NTCAGVWSQD KWKGRFDVRW IFVKDVPNSQ LRHIRLENNE NKPVTNSRDT QEVPLEKAKQ
VLKIIASYKH TTSIFDDFSH YEKRQEEEES VKKERQGRGK
//
