ID   TET5B_RAT               Reviewed;         427 AA.
AC   B0BNK8;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Terminal nucleotidyltransferase 5B {ECO:0000305};
DE            EC=2.7.7.19 {ECO:0000250|UniProtKB:Q96A09};
DE   AltName: Full=Non-canonical poly(A) polymerase FAM46B;
GN   Name=Tent5b {ECO:0000312|RGD:1308967};
GN   Synonyms=Fam46b {ECO:0000312|RGD:1308967};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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).
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 in an ATP
CC       hydrolysis-dependent manner. May be involved in maintaining the
CC       translation efficiency of at least some genes through preventing
CC       degradation of their mRNAs. Prefers RNA molecules that are adenosine-
CC       rich close to 3'-end. In addition, may inhibit cell proliferation and
CC       cell cycle progression through ubiquitination of beta-catenin/CTNNB1.
CC       {ECO:0000250|UniProtKB:Q96A09}.
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:Q96A09};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC         Evidence={ECO:0000250|UniProtKB:Q96A09};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96A09}. Nucleus
CC       {ECO:0000250|UniProtKB:Q96A09}.
CC   -!- SIMILARITY: Belongs to the TENT family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; CH473968; EDL80668.1; -; Genomic_DNA.
DR   EMBL; BC158863; AAI58864.1; -; mRNA.
DR   RefSeq; NP_001101377.1; NM_001107907.2.
DR   AlphaFoldDB; B0BNK8; -.
DR   SMR; B0BNK8; -.
DR   STRING; 10116.ENSRNOP00000010487; -.
DR   PaxDb; B0BNK8; -.
DR   PRIDE; B0BNK8; -.
DR   Ensembl; ENSRNOT00000086144; ENSRNOP00000070098; ENSRNOG00000056153.
DR   GeneID; 313019; -.
DR   KEGG; rno:313019; -.
DR   UCSC; RGD:1308967; rat.
DR   CTD; 115572; -.
DR   RGD; 1308967; Tent5b.
DR   eggNOG; KOG3852; Eukaryota.
DR   GeneTree; ENSGT00940000160747; -.
DR   HOGENOM; CLU_008115_2_0_1; -.
DR   InParanoid; B0BNK8; -.
DR   OMA; TTVNYYV; -.
DR   OrthoDB; 612201at2759; -.
DR   PhylomeDB; B0BNK8; -.
DR   TreeFam; TF315239; -.
DR   PRO; PR:B0BNK8; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Proteomes; UP000234681; Chromosome 5.
DR   Bgee; ENSRNOG00000056153; Expressed in esophagus and 11 other tissues.
DR   Genevisible; B0BNK8; RN.
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; IBA:GO_Central.
DR   GO; GO:0048255; P:mRNA stabilization; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; 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; Nucleotidyltransferase; Nucleus; Reference proteome;
KW   Transferase.
FT   CHAIN           1..427
FT                   /note="Terminal nucleotidyltransferase 5B"
FT                   /id="PRO_0000351481"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   427 AA;  47016 MW;  22D759BBD6DE7065 CRC64;
     MMPSESGDES LEQPAAQVGT GAASAVATAG AAGGGPDLEA SSASLGRHQS RLSWPQVKRL
     DALLKEPIPI HGRGNFPTLS VQPQQIVQVV RSSLEEQGLH VHSVRLHGSA ASHVLHPESG
     LGYKDLDLVF QMDLQSEASF QLTKAVVLAC LLDFLPAGVS RAKITPLTLK EAYVQKLVKV
     CTDLDRWSLI SLSNKSGKNV ELKFVDSVRR QFEFSIDSFQ IILDSLLLFG QCSSTPMSEA
     FHPTVTGESL YGDFAEALEH LQHRVIATRS PEEIRGGGLL KYCHLLVRGF RPRPSTDVRA
     LQRYMCSRFF IDFPDPVEQR RILERYLEAH FGGAEAARRY ACLVTLHRVV NESTVCLMSH
     ERRQTLDLIT MLALQALAEQ GPAAMAALAW RRPGSDGVVP ATVNYYVTPM QPLLPRAHSY
     PTWLPCN