DCP1B_BOVIN
ID DCP1B_BOVIN Reviewed; 581 AA.
AC Q3SZL6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=mRNA-decapping enzyme 1B;
DE EC=3.6.1.62 {ECO:0000250|UniProtKB:Q9NPI6};
GN Name=DCP1B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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; BC102799; AAI02800.1; -; mRNA.
DR RefSeq; NP_001029639.1; NM_001034467.2.
DR AlphaFoldDB; Q3SZL6; -.
DR SMR; Q3SZL6; -.
DR STRING; 9913.ENSBTAP00000003353; -.
DR iPTMnet; Q3SZL6; -.
DR PaxDb; Q3SZL6; -.
DR GeneID; 514548; -.
DR KEGG; bta:514548; -.
DR CTD; 196513; -.
DR eggNOG; KOG2868; Eukaryota.
DR InParanoid; Q3SZL6; -.
DR OrthoDB; 1509316at2759; -.
DR Proteomes; UP000009136; 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 Cytoplasm; Hydrolase; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..581
FT /note="mRNA-decapping enzyme 1B"
FT /id="PRO_0000287717"
FT REGION 181..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 366
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
SQ SEQUENCE 581 AA; 62880 MW; 4EACD820E7193196 CRC64;
MAVAGGPAGK GRDISLAALR RHDPYISRIV DVASQVALYT FGHRANEWEK TDVEGTLFVY
SRSASPKHGF TIMNRLSMEN RTEPITKDLD FLLQDPFLLY RNARLSIYGI WFYDKEECQR
IAELMKNLTQ YEQLKAHHGT GAGASPVSLG SGEGKEADIL RMLTKAKDEY TKCKTCSEPK
QISSSSAIHD NPNLIKPIPV KPSGSRQQRG PRPGQTSDPE PQHLSLTALF GKQDKAPCQE
ATGPPQTLPL QQQQPEKFPM RQGVVRSLSY EEPRRPSPPV DKQLCPAIQK LMVRSMDLQP
LAELPESRPC TDALRAACAG PAQTGSPRSH ALAAPGTQKL LQVQSIPGAE NRCEPGAPAP
ASSATTPVSL AQPTRLSSAL PPQTPGPRAL PRPAPPGPGP GHQPVTGPGE VSPRELLRRL
QAVQQEQQLP APGRPALAAK FPTATLSTRA RNPLEPWRDP PPSTEQPAPL LQVLSPQRIP
AAATPPPLMS PLVFAQPSWA PPQERSRAPL PPGNQDPAAT PTGLLLPLRT PEPPGTPGSA
LSKLQLQEAL LHLIQNDDNF LNIIYEAYLF SLTQAAVKKT L
