MEPCE_DANRE
ID MEPCE_DANRE Reviewed; 645 AA.
AC A3KQ55;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=7SK snRNA methylphosphate capping enzyme {ECO:0000250|UniProtKB:Q7L2J0};
DE Short=MePCE {ECO:0000250|UniProtKB:Q7L2J0};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q7L2J0};
DE AltName: Full=Bicoid-interacting protein 3 homolog {ECO:0000303|PubMed:19416841};
DE Short=Bin3 homolog {ECO:0000303|PubMed:19416841};
DE Short=zBCDIN3 {ECO:0000303|PubMed:19416841};
GN Name=mepce {ECO:0000250|UniProtKB:Q7L2J0};
GN Synonyms=bcdin3 {ECO:0000303|PubMed:19416841}; ORFNames=si:ch211-283h6.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=19416841; DOI=10.1073/pnas.0903188106;
RA Barboric M., Lenasi T., Chen H., Johansen E.B., Guo S., Peterlin B.M.;
RT "7SK snRNP/P-TEFb couples transcription elongation with alternative
RT splicing and is essential for vertebrate development.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7798-7803(2009).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that adds
CC a methylphosphate cap at the 5'-end of 7SK snRNA (7SK RNA), leading to
CC stabilize it. Also has a non-enzymatic function as part of the 7SK RNP
CC complex: the 7SK RNP complex sequesters the positive transcription
CC elongation factor b (P-TEFb) in a large inactive 7SK RNP complex
CC preventing RNA polymerase II phosphorylation and subsequent
CC transcriptional elongation. The 7SK RNP complex also promotes snRNA
CC gene transcription by RNA polymerase II via interaction with the little
CC elongation complex (LEC). In the 7SK RNP complex, MEPCE is required to
CC stabilize 7SK RNA and facilitate the assembly of 7SK RNP complex: it
CC has a non-enzymatic function (By similarity). MEPCE has a non-enzymatic
CC function in the 7SK RNP complex; interaction with LARP7 within the 7SK
CC RNP complex occluding its catalytic center (By similarity).
CC {ECO:0000250|UniProtKB:Q7L2J0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-guanosine-ribonucleotide-snRNA + S-
CC adenosyl-L-methionine = a 5'-end methyltriphosphate-guanosine-
CC ribonucleotide-snRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58780, Rhea:RHEA-COMP:15220, Rhea:RHEA-COMP:15221,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138278,
CC ChEBI:CHEBI:142789; Evidence={ECO:0000250|UniProtKB:Q7L2J0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58781;
CC Evidence={ECO:0000250|UniProtKB:Q7L2J0};
CC -!- SUBUNIT: Component of the 7SK snRNP complex.
CC {ECO:0000250|UniProtKB:Q7L2J0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7L2J0}.
CC -!- DISRUPTION PHENOTYPE: Transcription elongation and RNA splicing
CC defects, as well as aberrant anterior (brain) morphologies.
CC {ECO:0000269|PubMed:19416841}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; BX537304; CAM56504.1; -; Genomic_DNA.
DR AlphaFoldDB; A3KQ55; -.
DR SMR; A3KQ55; -.
DR STRING; 7955.ENSDARP00000121674; -.
DR PeptideAtlas; A3KQ55; -.
DR ZFIN; ZDB-GENE-030131-3936; mepcea.
DR ZFIN; ZDB-GENE-060526-155; sftpbb.
DR eggNOG; KOG2899; Eukaryota.
DR InParanoid; A3KQ55; -.
DR OrthoDB; 1185441at2759; -.
DR TreeFam; TF324061; -.
DR PRO; PR:A3KQ55; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:1990276; F:RNA 5'-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008173; F:RNA methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; ISS:UniProtKB.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
DR GO; GO:0016073; P:snRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0040031; P:snRNA modification; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR039772; Bin3-like.
DR InterPro; IPR010675; Bin3_C.
DR InterPro; IPR024160; BIN3_SAM-bd_dom.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12315; PTHR12315; 1.
DR Pfam; PF06859; Bin3; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51515; BIN3_SAM; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..645
FT /note="7SK snRNA methylphosphate capping enzyme"
FT /id="PRO_0000420468"
FT DOMAIN 380..642
FT /note="Bin3-type SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00848"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 370
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 382
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 400..402
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 423..424
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 516..517
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 538
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
SQ SEQUENCE 645 AA; 71700 MW; 008C30435FAD6AE1 CRC64;
MIEMSFDKET VLSCEGQTDP TSQEFNINDT SALHPPGNTT ENNLSKDAGS EASLEKSATT
DNNASSESAV LGAESSKQSH NGTKPQQQKV NKRRNTMSAG FKHPGYGKRR RRANSESESV
LPTNFLLGGN IFDPLNLNSL LDEEVNKALN AETPKSSPLP AKNRDPVEIL IPRDITDPLN
LNCLSTGDSL LVSPLKSGGG RRRHRNKHHG ANTGRVSTEG IGLTESNGCA AVKDDGTSLV
SMTNVHLEST IADQTLLDST LESSNKSSLT SNDNEVKEKT VDCSTAHLTA NPTNPPSSRQ
RKRRRAGSRT ENSSSSSEQH NESQGGNSRS GVSDRQQPYP NQWRPQYSNN NQNPQQPKKK
FQYGNYNKYY GYRNPGMSED PRIRVMNPDW FRGKDVLDLG CNTGHLTLFI AKNWRPASIV
GLDIDGSLIH AARQNIRHYL SEVQVQHSRR SGENTKADRG EVSGEEKDKD KTSKHSFPVS
LRISRGPIAG PPLPETNTHS LPPGDFPANV TFIKGNYVLE SDVLLQTQRE EYDVILCLSV
TKWVHLNWGD AGLKRFFHRV YKHLRPGGLF ILEPQPWSSY NKRKKLTEAI CKNYHSIRLK
PDQFSSFLTT EVGFSSYELI GTSQNYSKGF QRPISLYHKR PSSLK
