DBR1_MOUSE
ID DBR1_MOUSE Reviewed; 550 AA.
AC Q923B1; Q8C1T9; Q8C7J7; Q99MT1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lariat debranching enzyme;
DE EC=3.1.-.-;
GN Name=Dbr1;
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 [MRNA], AND FUNCTION.
RX PubMed=11355701;
RA Kim H.-C., Kim G.-M., Yang J.-M., Ki J.W.;
RT "Cloning, expression, and complementation test of the RNA lariat
RT debranching enzyme cDNA from mouse.";
RL Mol. Cells 11:198-203(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-489; SER-491; SER-494
RP AND SER-505, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
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: Cleaves the 2'-5' phosphodiester linkage at the branch point
CC of excised lariat intron RNA and converts them into linear molecules
CC that can be subsequently degraded, thereby facilitating ribonucleotide
CC turnover (By similarity) (PubMed:11355701). Linked to its role in pre-
CC mRNA processing mechanism, may also participate in retrovirus
CC replication and have an antiviral cell-intrinsic defense function (By
CC similarity). {ECO:0000250|UniProtKB:Q9UK59,
CC ECO:0000269|PubMed:11355701}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK18789.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF300293; AAK18789.1; ALT_FRAME; mRNA.
DR EMBL; AK050090; BAC34064.1; -; mRNA.
DR EMBL; AK090351; BAC41182.1; -; mRNA.
DR EMBL; BC006661; AAH06661.1; -; mRNA.
DR CCDS; CCDS23435.1; -.
DR RefSeq; NP_113580.2; NM_031403.3.
DR AlphaFoldDB; Q923B1; -.
DR SMR; Q923B1; -.
DR BioGRID; 219967; 4.
DR STRING; 10090.ENSMUSP00000070991; -.
DR iPTMnet; Q923B1; -.
DR PhosphoSitePlus; Q923B1; -.
DR SwissPalm; Q923B1; -.
DR EPD; Q923B1; -.
DR jPOST; Q923B1; -.
DR MaxQB; Q923B1; -.
DR PaxDb; Q923B1; -.
DR PeptideAtlas; Q923B1; -.
DR PRIDE; Q923B1; -.
DR ProteomicsDB; 279278; -.
DR Antibodypedia; 33423; 161 antibodies from 19 providers.
DR DNASU; 83703; -.
DR Ensembl; ENSMUST00000066650; ENSMUSP00000070991; ENSMUSG00000032469.
DR GeneID; 83703; -.
DR KEGG; mmu:83703; -.
DR UCSC; uc009rei.1; mouse.
DR CTD; 51163; -.
DR MGI; MGI:1931520; Dbr1.
DR VEuPathDB; HostDB:ENSMUSG00000032469; -.
DR eggNOG; KOG2863; Eukaryota.
DR GeneTree; ENSGT00510000047481; -.
DR HOGENOM; CLU_005893_0_2_1; -.
DR InParanoid; Q923B1; -.
DR OMA; GIDDPLC; -.
DR OrthoDB; 1047278at2759; -.
DR PhylomeDB; Q923B1; -.
DR TreeFam; TF313221; -.
DR BioGRID-ORCS; 83703; 29 hits in 60 CRISPR screens.
DR PRO; PR:Q923B1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q923B1; protein.
DR Bgee; ENSMUSG00000032469; Expressed in optic fissure and 263 other tissues.
DR ExpressionAtlas; Q923B1; baseline and differential.
DR Genevisible; Q923B1; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008419; F:RNA lariat debranching enzyme activity; IDA:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; ISS:UniProtKB.
DR CDD; cd00844; MPP_Dbr1_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR007708; DBR1_C.
DR InterPro; IPR041816; Dbr1_N.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF05011; DBR1; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SMART; SM01124; DBR1; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Metal-binding; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..550
FT /note="Lariat debranching enzyme"
FT /id="PRO_0000250359"
FT REGION 390..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK59"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK59"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK59"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK59"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK59"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CONFLICT 48..49
FT /note="DL -> EV (in Ref. 1; AAK18789)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..244
FT /note="DQ -> GR (in Ref. 3; AAH06661)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> G (in Ref. 2; BAC41182)"
FT /evidence="ECO:0000305"
FT CONFLICT 434..436
FT /note="Missing (in Ref. 3; AAH06661)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="I -> V (in Ref. 2; BAC34064)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="K -> N (in Ref. 1; AAK18789)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="H -> P (in Ref. 1; AAK18789)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="P -> R (in Ref. 2; BAC41182)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="Q -> P (in Ref. 1; AAK18789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 62289 MW; 3496D481AB876545 CRC64;
MRVAVAGCCH GELDKIYETL ALAERRGSGP VDLLLCCGDF QAVRNEADLR CMAVPPKYRH
MQTFYRYYSG EKKAPVLTIF IGGNHEASNH LQELPYGGWV APNIYYLGLA GVVKYRGVRI
GGISGIFKSH DYRKGHFECP PYNSSTIRSI YHVRNIEVYK LKQLKQPVHI FLSHDWPRNI
YHYGNKKQLL KTKSFFRQEV ENSTLGSPAA SELLEHLQPA YWFSAHLHVK FAALMQHQAT
DKDQAGKETK FLALDKCLPH RDFLQVLEIE HDPSAPEYLE YDVEWLTVLR ATDDLINVTG
GLWNMPEDNG LHTRWDYSAT EETMKEVMEK LNHDPKVPCN FTMTAACYDP SKPQTQVKLV
HRINPQTTEF CAQLGITDIN VMIQKAREEE HHQCGEYEQQ GDPGTEESEE DRSEYNTDTS
ALSSINPDEI MLDEEEEEEE EEEEAVSAHS DMNTPSVEPA SDQASDLSTS FSDIRNLPSS
MFVSSDDASR SPASGEGKCG ETVESGDEKD LAKFPLKRLS DEHEPEQRKK IKRRNQAIYA
AVDDGDASAE
