DCP1B_MOUSE
ID DCP1B_MOUSE Reviewed; 578 AA.
AC Q3U564; B2RUI2; Q3V333;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=mRNA-decapping enzyme 1B;
DE EC=3.6.1.62 {ECO:0000250|UniProtKB:Q9NPI6};
GN Name=Dcp1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pancreas, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U564-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U564-2; Sequence=VSP_025609;
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
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DR EMBL; AK050548; BAE20676.1; -; mRNA.
DR EMBL; AK153860; BAE32216.1; -; mRNA.
DR EMBL; BC141163; AAI41164.1; -; mRNA.
DR CCDS; CCDS39610.1; -. [Q3U564-1]
DR AlphaFoldDB; Q3U564; -.
DR SMR; Q3U564; -.
DR STRING; 10090.ENSMUSP00000108397; -.
DR iPTMnet; Q3U564; -.
DR PhosphoSitePlus; Q3U564; -.
DR EPD; Q3U564; -.
DR jPOST; Q3U564; -.
DR MaxQB; Q3U564; -.
DR PaxDb; Q3U564; -.
DR PRIDE; Q3U564; -.
DR ProteomicsDB; 279506; -. [Q3U564-1]
DR ProteomicsDB; 279507; -. [Q3U564-2]
DR Antibodypedia; 22113; 171 antibodies from 25 providers.
DR Ensembl; ENSMUST00000073909; ENSMUSP00000073568; ENSMUSG00000041477. [Q3U564-2]
DR UCSC; uc009dly.2; mouse. [Q3U564-2]
DR MGI; MGI:2442404; Dcp1b.
DR VEuPathDB; HostDB:ENSMUSG00000041477; -.
DR eggNOG; KOG2868; Eukaryota.
DR GeneTree; ENSGT00940000158409; -.
DR HOGENOM; CLU_030030_2_0_1; -.
DR InParanoid; Q3U564; -.
DR PhylomeDB; Q3U564; -.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR ChiTaRS; Dcp1b; mouse.
DR PRO; PR:Q3U564; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3U564; protein.
DR Bgee; ENSMUSG00000041477; Expressed in seminiferous tubule of testis and 192 other tissues.
DR ExpressionAtlas; Q3U564; baseline and differential.
DR Genevisible; Q3U564; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0097398; P:cellular response to interleukin-17; IDA:MGI.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
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 GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR GO; GO:0110012; P:protein localization to P-body; IDA:MGI.
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; 2.
DR Pfam; PF06058; DCP1; 1.
DR Pfam; PF16741; mRNA_decap_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Hydrolase;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT CHAIN 2..578
FT /note="mRNA-decapping enzyme 1B"
FT /id="PRO_0000287718"
FT REGION 187..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..265
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD4"
FT VAR_SEQ 495..527
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025609"
SQ SEQUENCE 578 AA; 62720 MW; 14194466EDA5B1CD CRC64;
MAAAAAGGLP GKGHDISLAA LRRHDPYISR IVDVASQVAL YTFGHRANEW EKTGVEGTLF
VYTRSASPKH GFTIMNRLSM ENRTEPITKD LDFQLQNPFL LYRNGTLSIY GIWFYDKEEC
QRIAKLMKNL TQSEQLKACH GAGSSPVTLS SGEGQEVDIL QMLTKAKDEY TKCKTCSEPK
QMTNSSAICD NPKLIKPVPV RPSSSQRLQG PAPSKTSDPE PQHLSLTALF GKQDKAPCQE
TVKPSRTFAH HHHHHHQQQQ ETRPVHHGVA CSLSCEEPRK LSLPVEKQLC PAIQKLMLGS
PGLHPLPQHP EQWSCKSGSP SPAGGILPGP VQLGSPWNGR VAHCTQSTCR GHKLLEQLQG
APGAVHKYNP CAPTGPAVAT QVAPGQSVAQ SQLVYFSGPL QPPAPGHQAL RKEQGALPAQ
AVSLSGSQES SPTVLPTQEL LRKLQVVHQE QQAAPRPALA ARFPVSAQGS GTEKPLEAWV
SKTASMEKQA PLLQSTCAPL RETDNGLMAL GGQELPAASS NLLLPLQNWE SSTVASRPLT
RLQLQEALLN LIQNDDNFLS IIYEAYLFSV TQAAMRTT
