ID   DBR1_DANRE              Reviewed;         568 AA.
AC   Q7T3E4;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Lariat debranching enzyme;
DE            EC=3.1.-.-;
GN   Name=dbr1; ORFNames=zgc:63930;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478 AND SER-568, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
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. Linked to its role in pre-mRNA processing mechanism, may also
CC       participate in retrovirus replication and have an antiviral cell-
CC       intrinsic defense function. {ECO:0000250|UniProtKB:Q9UK59}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; BC053153; AAH53153.1; -; mRNA.
DR   RefSeq; NP_955947.1; NM_199653.1.
DR   AlphaFoldDB; Q7T3E4; -.
DR   SMR; Q7T3E4; -.
DR   STRING; 7955.ENSDARP00000073957; -.
DR   iPTMnet; Q7T3E4; -.
DR   PaxDb; Q7T3E4; -.
DR   PRIDE; Q7T3E4; -.
DR   GeneID; 323746; -.
DR   KEGG; dre:323746; -.
DR   CTD; 51163; -.
DR   ZFIN; ZDB-GENE-030131-2466; dbr1.
DR   eggNOG; KOG2863; Eukaryota.
DR   InParanoid; Q7T3E4; -.
DR   OrthoDB; 1047278at2759; -.
DR   PhylomeDB; Q7T3E4; -.
DR   PRO; PR:Q7T3E4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008419; F:RNA lariat debranching enzyme activity; ISS:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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   Hydrolase; mRNA processing; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..568
FT                   /note="Lariat debranching enzyme"
FT                   /id="PRO_0000250361"
FT   REGION          388..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         478
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   MOD_RES         568
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   568 AA;  62889 MW;  ED592C5D4416C480 CRC64;
     MKVAVEGCCH GELDKIYESI SYLENKDGVK VDLLLCCGDF QAVRNEGDMK CMAVPAKYRH
     MQTFYKYYSG EKKAPVLTIF IGGNHEASNH LQELPYGGWV APNIYYLGYA GVIRYKGVRI
     GGLSGIFKSH DFKKGHFEFP PYNPETLRSV YHIRNIDVFK LKQIKMPIDI FMTHDWPRGI
     YHYGNTNALL RQKKFLRQEV ESSTLGSPAA ADLLEHLQPS YWFSAHLHVK FAALMQHEAK
     NNTAPKITKF LSLDKCLPHR DFLQIVEVAD RPGSSEQLEY DPEWLAILKA TDNLQKPTCN
     FWNPPQDNGL HSRWDFSASE EAMMEVVSDL SGDLCIPENF SLTVPPYDPS QPQPHALPAY
     STNPQTTELC ATLNLTDIYI LAGQSGQIYG ERGGKGATEE EDEEDSTGSA DEPSDFPSDT
     SGLSSSYNPD EITIEDEWEE EEDGGVGCGE GKGMDAVVPE GQVGSQDSDR DSSPQRETAK
     RLILPAPCAK PKTEAPLHSL PRLSLPPPSA CVSQGSSEEE GAFTAARVPK RTSGETTQSS
     AGQTGGTPQI KRRNQSIYTA VEDEESDS