TET5B_XENTR
ID TET5B_XENTR Reviewed; 395 AA.
AC F7E7M3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 3.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Terminal nucleotidyltransferase 5B {ECO:0000250|UniProtKB:Q96A09};
DE EC=2.7.7.19 {ECO:0000250|UniProtKB:Q96A09};
DE AltName: Full=Non-canonical poly(A) polymerase FAM46B;
GN Name=tent5b {ECO:0000250|UniProtKB:Q96A09};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=34048638; DOI=10.1002/cac2.12163;
RA Zhang H., Zhang S.H., Hu J.L., Wu Y.T., Ma X.Y., Chen Y., Yu B., Liao S.,
RA Huang H., Gao S.;
RT "Structural and functional characterization of multiple myeloma associated
RT cytoplasmic poly(A) polymerase FAM46C.";
RL Cancer Commun. (Lond) 41:615-630(2021).
RN [3] {ECO:0007744|PDB:6JYJ}
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
RX PubMed=32009146; DOI=10.1093/nar/gkaa049;
RA Hu J.L., Liang H., Zhang H., Yang M.Z., Sun W., Zhang P., Luo L.,
RA Feng J.X., Bai H., Liu F., Zhang T., Yang J.Y., Gao Q., Long Y., Ma X.Y.,
RA Chen Y., Zhong Q., Yu B., Liao S., Wang Y., Zhao Y., Zeng M.S., Cao N.,
RA Wang J., Chen W., Yang H.T., Gao S.;
RT "FAM46B is a prokaryotic-like cytoplasmic poly(A) polymerase essential in
RT human embryonic stem cells.";
RL Nucleic Acids Res. 48:2733-2748(2020).
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 and participates in cytoplasmic
CC polyadenylation (PubMed:34048638). May be involved in maintaining the
CC translation efficiency of at least some genes through preventing
CC degradation of their mRNAs (By similarity).
CC {ECO:0000250|UniProtKB:Q96A09, ECO:0000269|PubMed:34048638}.
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}.
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DR EMBL; AAMC02005713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001017206.1; NM_001017206.2.
DR PDB; 6JYJ; X-ray; 2.69 A; A/B/C=1-395.
DR PDBsum; 6JYJ; -.
DR SMR; F7E7M3; -.
DR PaxDb; F7E7M3; -.
DR GeneID; 549960; -.
DR KEGG; xtr:549960; -.
DR CTD; 115572; -.
DR Xenbase; XB-GENE-952160; tent5b.
DR eggNOG; KOG3852; Eukaryota.
DR HOGENOM; CLU_008115_2_0_1; -.
DR InParanoid; F7E7M3; -.
DR OMA; QPFLPCN; -.
DR OrthoDB; 612201at2759; -.
DR PhylomeDB; F7E7M3; -.
DR TreeFam; TF315239; -.
DR BRENDA; 2.7.7.19; 8483.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000020683; Expressed in blastula and 15 other tissues.
DR ExpressionAtlas; F7E7M3; differential.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="Terminal nucleotidyltransferase 5B"
FT /id="PRO_0000454712"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 140..150
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:6JYJ"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 261..278
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 303..318
FT /evidence="ECO:0007829|PDB:6JYJ"
FT HELIX 324..342
FT /evidence="ECO:0007829|PDB:6JYJ"
SQ SEQUENCE 395 AA; 45300 MW; CEA73489C957162B CRC64;
MSSALSQASP TAPRFSVLSW PQVRRLDAIL CESVPIHGRG NFPTLSCRPR DLVQVVRSRL
EQKGILVHNV RLNGSAASYV LHHDSGLGYK DLDLIFMVDL KGPDAFQVVK HAVLNCLLDF
LPSGVNKEKI TPMTLKEAYV QKLVKVCTES DRWSLISLSN NSGKNMELKF VDSLRRQFEF
SVDSFQIILD SMLMFSQCSE NPMSQSFHPT VTGESMYGDF EEAMDHLRNR IIATRNPEEI
RGGGLLKYCN LLVRGFRPKS EVDMKTMQRY MCSRYFIDFP DIREQQRKLK CYLQDHFVGM
EDKRYDYLMT LHQVVNESTV CLMGHERRQT LALIASLAVH VLSEQNHPQA VPTFTCYYQP
APYIGEVNYN SYYFTPVQPL MSCSHSYQTW LPCCN
