ID A0A1S2ZW63_ERIEU Unreviewed; 456 AA.
AC A0A1S2ZW63;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|RefSeq:XP_007525548.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007525548.1};
RN [1] {ECO:0000313|RefSeq:XP_007525548.1}
RP IDENTIFICATION.
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007525548.1; XM_007525486.2.
DR AlphaFoldDB; A0A1S2ZW63; -.
DR STRING; 9365.ENSEEUP00000006076; -.
DR CTD; 57721; -.
DR eggNOG; KOG2097; Eukaryota.
DR InParanoid; A0A1S2ZW63; -.
DR OrthoDB; 179166at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IEA:UniProtKB-UniRule.
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:0061157; P:mRNA destabilization; IEA:UniProtKB-UniRule.
DR GO; GO:0080009; P:mRNA methylation; IEA:UniProtKB-UniRule.
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:UP000079721};
KW RNA-binding {ECO:0000256|RuleBase:RU369092};
KW Spermatogenesis {ECO:0000256|RuleBase:RU369092}.
FT REGION 49..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 52217 MW; 93A73E8BB407AEC9 CRC64;
MDSRLQEIRE RQKLRRQLLA QQLGAESADS IGAVLNSKDE QREIAETRET CRASYDTSAP
HAKRKYQEEG ETDEDKMEEY KDELEMQQEE ENLPYEEEIY KDSSTFLKGT QSLNPHNDYC
QHFVDTGHRP QNFIRDVGLA DRFEEYPKLR ELIRLKDELI AKSNTPPMYL QADIEAFDIR
ELTPKFDVIL LEPPLEEYYR ETGITANEKC WTWDDIMKLE IDEIAAPRSF IFLWCGSGEG
LDLGRVCLRK WGYRRCEDIC WIKTNKNNPG KTKTLDPKAV FQRTKEHCLM GIKGTVKRST
DGDFIHANVD IDLIITEEPE IGNIEKPVEI FHIIEHFCLG RRRLHLFGRD STIRPGWLTV
GPTLTNSNYN AETYASYFSA PNSYLTGCTE EIERLRPKSP PPKSKSDRGG GAPRGGGRGG
TSAGRGRERN RSNFRGERGG FRGGRGGAHR GGFPPR
//
