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Database: UniProt
Entry: I3MNF0_ICTTR
LinkDB: I3MNF0_ICTTR
Original site: I3MNF0_ICTTR 
ID   I3MNF0_ICTTR            Unreviewed;       458 AA.
AC   I3MNF0;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=N6-adenosine-methyltransferase non-catalytic subunit {ECO:0000256|ARBA:ARBA00026130, ECO:0000256|RuleBase:RU369092};
DE   AltName: Full=Methyltransferase-like protein 14 {ECO:0000256|ARBA:ARBA00032942, ECO:0000256|RuleBase:RU369092};
GN   Name=METTL14 {ECO:0000313|Ensembl:ENSSTOP00000013175.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000013175.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000013175.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: The METTL3-METTL14 heterodimer forms a N6-methyltransferase
CC       complex that methylates adenosine residues at the N(6) position of some
CC       mRNAs and regulates the circadian clock, differentiation of embryonic
CC       stem cells and cortical neurogenesis. In the heterodimer formed with
CC       METTL3, METTL14 constitutes the RNA-binding scaffold that recognizes
CC       the substrate rather than the catalytic core. N6-methyladenosine (m6A),
CC       which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs,
CC       plays a role in mRNA stability and processing. M6A acts as a key
CC       regulator of mRNA stability by promoting mRNA destabilization and
CC       degradation. In embryonic stem cells (ESCs), m6A methylation of mRNAs
CC       encoding key naive pluripotency-promoting transcripts results in
CC       transcript destabilization. M6A regulates spermatogonial
CC       differentiation and meiosis and is essential for male fertility and
CC       spermatogenesis. M6A also regulates cortical neurogenesis: m6A
CC       methylation of transcripts related to transcription factors, neural
CC       stem cells, the cell cycle and neuronal differentiation during brain
CC       development promotes their destabilization and decay, promoting
CC       differentiation of radial glial cells. {ECO:0000256|RuleBase:RU369092}.
CC   -!- SUBUNIT: Heterodimer; heterodimerizes with METTL3 to form an
CC       antiparallel heterodimer that constitutes an active methyltransferase.
CC       {ECO:0000256|RuleBase:RU369092}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369092}.
CC   -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00489, ECO:0000256|RuleBase:RU369092}.
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DR   EMBL; AGTP01114083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01114084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01114085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01114086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3MNF0; -.
DR   SMR; I3MNF0; -.
DR   STRING; 43179.ENSSTOP00000013175; -.
DR   Ensembl; ENSSTOT00000014708.3; ENSSTOP00000013175.3; ENSSTOG00000014707.3.
DR   eggNOG; KOG2097; Eukaryota.
DR   GeneTree; ENSGT00550000075003; -.
DR   HOGENOM; CLU_046318_1_0_1; -.
DR   InParanoid; I3MNF0; -.
DR   TreeFam; TF323641; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; IEA:Ensembl.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0021861; P:forebrain radial glial cell differentiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:Ensembl.
DR   GO; GO:0061157; P:mRNA destabilization; IEA:UniProtKB-UniRule.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:Ensembl.
DR   GO; GO:1901533; P:negative regulation of hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0019827; P:stem cell population maintenance; IEA:UniProtKB-UniRule.
DR   InterPro; IPR045123; METTL14-like.
DR   InterPro; IPR007757; MT-A70-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13107; N6-ADENOSINE-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR13107:SF0; N6-ADENOSINE-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT; 1.
DR   Pfam; PF05063; MT-A70; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51143; MT_A70; 1.
DR   PROSITE; PS51592; SAM_MTA70L_2; 1.
PE   3: Inferred from homology;
KW   Differentiation {ECO:0000256|RuleBase:RU369092};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   RNA-binding {ECO:0000256|RuleBase:RU369092};
KW   Spermatogenesis {ECO:0000256|RuleBase:RU369092}.
FT   REGION          395..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  52231 MW;  175CD8E014545068 CRC64;
     MDSRLQEIRE RQKLRRQGLA ELLSLGAESA DSIGAVLNSK DEQREIAETR ETCRASYDTS
     APNAKRKCLD EGETDEDKVE EYKDELEMQQ EEENLPYEEE IYKDSSTFLK GTQSLNPHND
     YCQHFVDTGH RPQNFIRDVG LADRFEEYPK LRELIRLKDE LIAKSNTPPM YLQADIEAFD
     IRELTPKFDV ILLEPPLEEY YRETGITANE RCWTWDDIMK LEIDEIAAPR SFIFLWCGSG
     EGLDLGRVCL RKWGYRRCED ICWIKTNKNN PGKTKTLDPK AVFQRTKEHC LMGIKGTVKR
     STDGDFIHAN VDIDLIITEE PEIGNIEKPV EIFHIIEHFC LGRRRLHLFG RDSTIRPGWL
     TVGPTLTNSN YNAETYASYF SAPNSYLTGC TEEIERLRPK SPPPKSKSDR GGGAPRGGGR
     GGTSAGRGRE RNRSNFRGER GGFRGGRGGA HRGGFPPR
//
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