FL2D_XENLA
ID FL2D_XENLA Reviewed; 393 AA.
AC Q4KLT6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Pre-mRNA-splicing regulator WTAP {ECO:0000305};
DE AltName: Full=Female-lethal(2)D homolog {ECO:0000250|UniProtKB:Q15007};
DE AltName: Full=WT1-associated protein {ECO:0000250|UniProtKB:Q15007};
DE AltName: Full=Wilms tumor 1-associating protein {ECO:0000250|UniProtKB:Q15007};
GN Name=wtap {ECO:0000250|UniProtKB:Q15007};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Associated component of the WMM complex, a complex that
CC mediates N6-methyladenosine (m6A) methylation of RNAs, a modification
CC that plays a role in the efficiency of mRNA splicing and RNA
CC processing. {ECO:0000250|UniProtKB:Q15007}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM. Component of the MACOM subcomplex.
CC {ECO:0000250|UniProtKB:Q15007}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q15007}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q15007}.
CC -!- SIMILARITY: Belongs to the fl(2)d family. {ECO:0000305}.
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DR EMBL; BC099007; AAH99007.1; -; mRNA.
DR RefSeq; NP_001089582.1; NM_001096113.1.
DR RefSeq; XP_018117590.1; XM_018262101.1.
DR AlphaFoldDB; Q4KLT6; -.
DR SMR; Q4KLT6; -.
DR DNASU; 734639; -.
DR GeneID; 734639; -.
DR KEGG; xla:734639; -.
DR CTD; 734639; -.
DR Xenbase; XB-GENE-864912; wtap.L.
DR OMA; FRTITNQ; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 734639; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR033757; WTAP.
DR PANTHER; PTHR15217; PTHR15217; 1.
DR Pfam; PF17098; Wtap; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Developmental protein; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome.
FT CHAIN 1..393
FT /note="Pre-mRNA-splicing regulator WTAP"
FT /id="PRO_0000308628"
FT REGION 242..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 44295 MW; AC2C520E8F39FE0D CRC64;
MTNEEPLPKK VRLNESDFKV LPREDLLQRW KQYEAYVQAL ENKYTDLNSN DVTGLRESEE
KLKQQQQESA RRENILVMRL ATKEQEMQEC TNQIQHLKQV QQPSVAQLRA TMVDPAINLF
FIKMKAELEQ TKDKLEQAQN ELSAWKFTPD SQTGKKLMAK CRMLIQENQE LGRQLSQGRI
AQLEAELALQ KKYSEELKSS QDELNDFIIQ LDEEVEGMQS TILVLQQQLK DSRQQLSQFQ
QQIQISGNRT PSSEPKDEGE TSGKDCGRIL NGPSNGGSSL QRTHSSAGLY REGSSTEDDF
SASPINEGKL SNHSQERTSR DGSSYINPLS TGYESVDSPT GSENSLTHQS NDTDSNHDSQ
EEKPVSGKGN RTVSSRHLQN GLDSSVNVQG SVL