ID   MB211_DANRE             Reviewed;         359 AA.
AC   Q6NYB4; Q8JIW4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putative nucleotidyltransferase MAB21L1;
DE            EC=2.7.7.- {ECO:0000305};
DE   AltName: Full=Protein mab-21-like 1;
GN   Name=mab21l1;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=11960703; DOI=10.1016/s0925-4773(02)00012-6;
RA   Wong Y.-M., Chow K.L.;
RT   "Expression of zebrafish mab21 genes marks the differentiating eye,
RT   midbrain and neural tube.";
RL   Mech. Dev. 113:149-152(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative nucleotidyltransferase required for several aspects
CC       of embryonic development including normal development of the eye (By
CC       similarity). It is unclear whether it displays nucleotidyltransferase
CC       activity in vivo. Binds single-stranded RNA (ssRNA) (By similarity).
CC       {ECO:0000250|UniProtKB:O70299, ECO:0000250|UniProtKB:Q13394}.
CC   -!- SUBUNIT: Monomer. Homodecamer; composed of 2 back to back
CC       homopentamers. The protein may exist as monomer in solution and
CC       oiligomerizes upon ligand binding. {ECO:0000250|UniProtKB:Q13394}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O70299}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 8 hours post-fertilization (hpf).
CC       Expressed in the midbrain and the optic primordia from 14 hpf and
CC       around the eyes, the branchial pouches and the neural tube at 24 hpf.
CC       By 48 hpf, expression in the midbrain, branchial pouches and the neural
CC       tube was reduced to a very low level. {ECO:0000269|PubMed:11960703}.
CC   -!- SIMILARITY: Belongs to the mab-21 family. {ECO:0000305}.
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DR   EMBL; AY048747; AAL09173.1; -; mRNA.
DR   EMBL; BC057249; AAH57249.1; -; mRNA.
DR   EMBL; BC066667; AAH66667.1; -; mRNA.
DR   RefSeq; NP_694506.2; NM_152974.2.
DR   AlphaFoldDB; Q6NYB4; -.
DR   SMR; Q6NYB4; -.
DR   STRING; 7955.ENSDARP00000071872; -.
DR   PaxDb; Q6NYB4; -.
DR   Ensembl; ENSDART00000164928; ENSDARP00000138318; ENSDARG00000102047.
DR   GeneID; 246091; -.
DR   KEGG; dre:246091; -.
DR   CTD; 4081; -.
DR   ZFIN; ZDB-GENE-020516-1; mab21l1.
DR   eggNOG; KOG3963; Eukaryota.
DR   GeneTree; ENSGT01050000244827; -.
DR   HOGENOM; CLU_045315_0_0_1; -.
DR   InParanoid; Q6NYB4; -.
DR   OMA; AVDKCKY; -.
DR   OrthoDB; 771781at2759; -.
DR   PhylomeDB; Q6NYB4; -.
DR   TreeFam; TF315012; -.
DR   PRO; PR:Q6NYB4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 15.
DR   Bgee; ENSDARG00000102047; Expressed in camera-type eye and 32 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR024810; Mab-21_dom.
DR   Pfam; PF03281; Mab-21; 1.
DR   SMART; SM01265; Mab-21; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..359
FT                   /note="Putative nucleotidyltransferase MAB21L1"
FT                   /id="PRO_0000312784"
FT   BINDING         23..24
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000250|UniProtKB:Q13394"
FT   BINDING         63..66
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000250|UniProtKB:Q13394"
FT   BINDING         73
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N884"
FT   BINDING         75
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N884"
FT   BINDING         248
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000250|UniProtKB:Q13394"
FT   BINDING         252..255
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000250|UniProtKB:Q13394"
FT   CONFLICT        179
FT                   /note="I -> V (in Ref. 1; AAL09173)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   359 AA;  41035 MW;  E41DF65D2E2C7345 CRC64;
     MIAAQAKLVY HLNKYYNEKC QSRKAAISKT IREVCKVVSD VLKEVEVQEP RFISSLNEMD
     NRFEGLEVIS PTEFEVVLYL NQMGVFNFVD DGSLPGCAVL KLSDGRKRSM SLWVEFITAS
     GYLSARKIRS RFQTLVAQAV DKCSYRDVVK MVADTSEVKL RIRDRYVVQI TPAFKCTGIW
     PRSAAHWPLP HIPWPGPNRV AEVKAEGFNL LSKECYSLNG KQSSAESDAW VLQFAEAENR
     LLLGGCRKKC LSLLKTLRDR HLELPGQPLN NYHMKTLVSY ECEKHPRESD WDENCLGDRL
     NGILLQLISC LQCRRCPHYF LPNLDLFQGK PHSALENAAK QTWRLAREIL TNPKSLEKL