ID A0A3P8Y2L4_ESOLU Unreviewed; 632 AA.
AC A0A3P8Y2L4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase {ECO:0000256|ARBA:ARBA00026102};
DE EC=3.6.1.62 {ECO:0000256|ARBA:ARBA00026102};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000010892.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000010892.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000010892.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461;
CC EC=3.6.1.62; Evidence={ECO:0000256|ARBA:ARBA00024496};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000256|ARBA:ARBA00024496};
CC -!- SIMILARITY: Belongs to the DCP1 family.
CC {ECO:0000256|ARBA:ARBA00008778}.
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DR AlphaFoldDB; A0A3P8Y2L4; -.
DR SMR; A0A3P8Y2L4; -.
DR STRING; 8010.ENSELUP00000010892; -.
DR Ensembl; ENSELUT00000001386.2; ENSELUP00000010892.2; ENSELUG00000011344.2.
DR GeneTree; ENSGT00940000158409; -.
DR InParanoid; A0A3P8Y2L4; -.
DR OMA; LPMRQGV; -.
DR Proteomes; UP000265140; LG18.
DR Bgee; ENSELUG00000011344; Expressed in head kidney and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR CDD; cd09804; Dcp1; 1.
DR Gene3D; 6.10.140.2030; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR031953; mRNA_decap_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290:SF0; DECAPPING PROTEIN 1, ISOFORM A; 1.
DR PANTHER; PTHR16290; TRANSCRIPTION FACTOR SMIF DECAPPING ENZYME DCP1; 1.
DR Pfam; PF06058; DCP1; 1.
DR Pfam; PF16741; mRNA_decap_C; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140}.
FT DOMAIN 592..631
FT /note="mRNA-decapping enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16741"
FT REGION 141..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..579
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 68678 MW; 09825B2E3CF01E74 CRC64;
MTASSSGGNT CLTAKGLDIS LAALQRQDPY INNIVDVASQ VALYTFNNRS NEWEKTDVEG
TLFVYTRLAS PRHGFTIMNR LSMENLTEPI TKDLDFQLQD PFLLYRNARL AIYGIWFYDK
VDCQRIAELM KNLTKQEQAL AQQSRSGWES PGDLEAAEDP GKTRGVDILQ MLTKARDEYD
KGGKPEPKEI GRSVLQDNPN LIKPIPVKPM DRHPQPGLQE RPVQDQGEPR PLSLATLFGV
QQASRGPVSP MSGYGAPGSQ PQAKPAGVRP AVARSLSYED PSQSRLQAQP GAPAPGSGPQ
QHCPAFQKLM REASTQPGLQ RGGPMELLQP VSESPENRLL ENGAPSTLHH QAQQDPIQRL
FQNQPTSATL SLTSCSSTAS CCSRPSPLQQ PPHLLPGLQP AQPLLVDPAG FHHHPNLVPH
QSQPIFFTPT KASQMQASLP SKSLPPSPHL PPYLQQQVSV PRGSPSHLAL QPQPGHPQPG
QLAGVVPPGE LLQRLQLVQQ EQGLVPVTAR PASNLAPRFH EKLSAGSAAQ KFQVISPQRI
PATVAPTLLL SPSVFSQAKP PQVQPKAPGD PPGPPTALLS PRAPDETQSW GLTKSQLQAT
LLHLIQNDSS FLDTIYKAYT QSFSSKTNTD KF
//