ID   TET5C_DANRE             Reviewed;         388 AA.
AC   Q7ZUP1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Terminal nucleotidyltransferase 5C {ECO:0000305};
DE            EC=2.7.7.19 {ECO:0000250|UniProtKB:Q5VWP2};
GN   Name=tent5c {ECO:0000250|UniProtKB:Q5VWP2};
GN   Synonyms=fam46c {ECO:0000250|UniProtKB:Q5VWP2};
GN   ORFNames=zgc:55510 {ECO:0000303|Ref.1};
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   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of one adenosine molecule from an ATP
CC       to an mRNA poly(A) tail bearing a 3'-OH terminal group and enhances
CC       mRNA stability and gene expression. {ECO:0000250|UniProtKB:Q5VWP2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC         Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC         ChEBI:CHEBI:173115; EC=2.7.7.19;
CC         Evidence={ECO:0000250|UniProtKB:Q5VWP2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC         Evidence={ECO:0000250|UniProtKB:Q5VWP2};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VWP2}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q5VWP2}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q5VWP2}.
CC   -!- SIMILARITY: Belongs to the TENT family. {ECO:0000305}.
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DR   EMBL; BC048046; AAH48046.1; -; mRNA.
DR   RefSeq; NP_956801.2; NM_200507.2.
DR   AlphaFoldDB; Q7ZUP1; -.
DR   SMR; Q7ZUP1; -.
DR   STRING; 7955.ENSDARP00000114520; -.
DR   PaxDb; Q7ZUP1; -.
DR   GeneID; 327154; -.
DR   KEGG; dre:327154; -.
DR   CTD; 54855; -.
DR   ZFIN; ZDB-GENE-030131-5365; tent5c.
DR   eggNOG; KOG3852; Eukaryota.
DR   InParanoid; Q7ZUP1; -.
DR   OrthoDB; 612201at2759; -.
DR   PhylomeDB; Q7ZUP1; -.
DR   PRO; PR:Q7ZUP1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:1990817; F:RNA adenylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR012937; TET5.
DR   PANTHER; PTHR12974; PTHR12974; 1.
DR   Pfam; PF07984; NTP_transf_7; 1.
DR   SMART; SM01153; DUF1693; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; RNA-binding; Transferase.
FT   CHAIN           1..388
FT                   /note="Terminal nucleotidyltransferase 5C"
FT                   /id="PRO_0000259938"
SQ   SEQUENCE   388 AA;  44756 MW;  71C0C6E1BA6F88B2 CRC64;
     MASASTSSSN ESESQSVLTW EQVSRLNDVL TEAVPVHGRG NFPTLEVRLK DIVQMVRNRL
     ELRGIMVKDV RLNGSTASHV LVQDIGWSYK DLDVIFRVDL PREEEFQLIK DVVLSTLLDF
     LPEGVNKEKI TPMTLKEAYV QKLVKVYTDQ DRWSLISLSN NNGRNVELKF VDSIRRQFEF
     SVDSFQIILD SVLSYYDLSE NPMSQHFHPT VVGESMYGDF VEALGHLTNK TIATKRPEEI
     RGGGLLKYCN LLVREFKPTD PDEFKALERY MCSRFFIDFP DIVEQQRKLE AYLQSHFIGE
     ERNKYNYLMI LRRVVNESTV CLMGHERRQT LNLISLTAFR VLAEQNAIPD VSSVTCYYQP
     APYVKDLNFN NYYVASCNQS IPTWLPCN