DCP1B_PONAB
ID DCP1B_PONAB Reviewed; 609 AA.
AC Q5R413;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=mRNA-decapping enzyme 1B;
DE EC=3.6.1.62 {ECO:0000250|UniProtKB:Q9NPI6};
GN Name=DCP1B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the degradation of mRNAs, both in normal
CC mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-
CC methyl guanine cap structure from mRNA molecules, yielding a 5'-
CC phosphorylated mRNA fragment and 7m-GDP (By similarity).
CC {ECO:0000250|UniProtKB:Q9NPI6}.
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:0000250|UniProtKB:Q9NPI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000250|UniProtKB:Q9NPI6};
CC -!- SUBUNIT: Interacts with DCP1A. {ECO:0000250|UniProtKB:Q8IZD4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IZD4}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NPI6}.
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
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DR EMBL; CR861447; CAH93503.1; -; mRNA.
DR RefSeq; NP_001127672.1; NM_001134200.1.
DR AlphaFoldDB; Q5R413; -.
DR SMR; Q5R413; -.
DR STRING; 9601.ENSPPYP00000004723; -.
DR PRIDE; Q5R413; -.
DR GeneID; 100174754; -.
DR KEGG; pon:100174754; -.
DR CTD; 196513; -.
DR eggNOG; KOG2868; Eukaryota.
DR InParanoid; Q5R413; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 GO; GO:0043085; P:positive regulation of catalytic activity; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR031953; mRNA_decap_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290; PTHR16290; 1.
DR Pfam; PF06058; DCP1; 1.
DR Pfam; PF16741; mRNA_decap_C; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT CHAIN 2..609
FT /note="mRNA-decapping enzyme 1B"
FT /id="PRO_0000189635"
FT REGION 201..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 191
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
SQ SEQUENCE 609 AA; 66899 MW; FA342BEC2CD34BA3 CRC64;
MAAVAAGGLV GKGRDISLAA LQRHDPYINR IVDVASQVAL YTFGHRANEW EKTDVEGTLF
VYTRSASPKH GFTIMNRLSM ENRTEPITKD LDFQLQDPFL LYRNARLSIY GIWFYDKEEC
QRIAELMKNL TQYEQLKAHQ GTGAGISPMI LNSGEGKEVD ILRMLIKAKD EYTKCKTCSE
PKKITSSSAI YDNPNLIKPI PVKPSENQQQ RIPQPNQTLD PEPQHLSLTA LFGKQDKATC
QETVEPPQTL HQQQQQQQEK LPIRQGVVRS LSYEEPRRHS PPIEKQLCPA IQKLMVRSAD
LHPLSELPEN RPCENGSTHS AGEFFTGPVR PGSPHNIGTS RGVQNASRTQ NLFEKLQSTP
GAANKCDPST PAPASSAALN RSRAPTSVTP QAPGKGLAQP PQAYFNGSLP PQAHGREQST
LPRQTLPISG NQTGSSGVIS PQELLKKLQI VQQEQQLHAS NRPALAAKFP VLSQSSGTGK
PLESWINKTS STEQQTPLFQ VISPQRIPAT AAPSLLTSPM VFAQPTSVPP KERESGLLPV
GGQEPPAAAT SLLLPIQSPE PSMITSSPLT KLQLQEALLY LIQNDDNFLN IIYEAYLFSM
TQAAMKKSM
