TET5B_MOUSE
ID TET5B_MOUSE Reviewed; 427 AA.
AC Q8C152; Q3TSC3; Q8CI10;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 115.
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|MGI:MGI:2140500};
GN Synonyms=Fam46b {ECO:0000312|MGI:MGI:2140500};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Vagina;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38001.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK028944; BAC26207.1; -; mRNA.
DR EMBL; AK135706; BAE22618.1; -; mRNA.
DR EMBL; AK137659; BAE23449.1; -; mRNA.
DR EMBL; AK162145; BAE36752.1; -; mRNA.
DR EMBL; BC038001; AAH38001.1; ALT_INIT; mRNA.
DR CCDS; CCDS18748.1; -.
DR RefSeq; NP_780516.1; NM_175307.6.
DR AlphaFoldDB; Q8C152; -.
DR SMR; Q8C152; -.
DR STRING; 10090.ENSMUSP00000056015; -.
DR iPTMnet; Q8C152; -.
DR PhosphoSitePlus; Q8C152; -.
DR PaxDb; Q8C152; -.
DR PRIDE; Q8C152; -.
DR ProteomicsDB; 271840; -.
DR Antibodypedia; 69553; 35 antibodies from 9 providers.
DR DNASU; 100342; -.
DR Ensembl; ENSMUST00000051676; ENSMUSP00000056015; ENSMUSG00000046694.
DR GeneID; 100342; -.
DR KEGG; mmu:100342; -.
DR UCSC; uc008vct.2; mouse.
DR CTD; 115572; -.
DR MGI; MGI:2140500; Tent5b.
DR VEuPathDB; HostDB:ENSMUSG00000046694; -.
DR eggNOG; KOG3852; Eukaryota.
DR GeneTree; ENSGT00940000160747; -.
DR HOGENOM; CLU_008115_2_0_1; -.
DR InParanoid; Q8C152; -.
DR OMA; TTVNYYV; -.
DR OrthoDB; 612201at2759; -.
DR PhylomeDB; Q8C152; -.
DR TreeFam; TF315239; -.
DR BioGRID-ORCS; 100342; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Tent5b; mouse.
DR PRO; PR:Q8C152; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8C152; protein.
DR Bgee; ENSMUSG00000046694; Expressed in secondary oocyte and 65 other tissues.
DR Genevisible; Q8C152; MM.
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_0000259932"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 138
FT /note="V -> A (in Ref. 2; AAH38001)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="F -> L (in Ref. 1; BAE36752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 46998 MW; BD4406CD3E66F9BD CRC64;
MMPSESGAES LEQPAAQVGT GAASAVATAG AAGGGPDPEA SSASLGRHQS RLSWPQVKRL
DALLKEPIPI HGRGNFPTLS VQPQQIVQVV RSSLEEHGLR VHSVRLHGSA ASHVLHPESG
LGYKDLDLVF QMDLRSEVSF QLTKAVVLAC LLDFLPAGVS RAKITPLTLK EAYVQKLVKV
CTDLDRWSLI SLSNKSGKNV ELKFVDSVRR QFEFSIDSFQ IILDSLLLFG QCSSTPMSEA
FHPTVTGESL YGDFAEALEH LQHRVIATRS PEEIRGGGLL KYCHLLVRGF RPRPSTDVRA
LQRYMCSRFF IDFPDLVEQR RILERYLEAH FGGAEAARRY ACLVTLHQVV NESTVCLMSH
ERRQTLDLIA MLALQALAEQ GPAAMAALAW RRPGSDGVVP ATVNYYVTPM QPLLPRAHSY
PTWLPCN
