TET5C_MOUSE
ID TET5C_MOUSE Reviewed; 391 AA.
AC Q5SSF7; Q0P629; Q80XL2; Q9CUN7;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Terminal nucleotidyltransferase 5C {ECO:0000305};
DE EC=2.7.7.19 {ECO:0000269|PubMed:34048638};
GN Name=Tent5c {ECO:0000250|UniProtKB:Q5VWP2};
GN Synonyms=Fam46c {ECO:0000312|MGI:MGI:1921895};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, Mammary tumor, and Olfactory epithelium;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-391.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INDUCTION BY IL4 AND
RP LPS, AND TISSUE SPECIFICITY.
RX PubMed=28931820; DOI=10.1038/s41467-017-00578-5;
RA Mroczek S., Chlebowska J., Kulinski T.M., Gewartowska O., Gruchota J.,
RA Cysewski D., Liudkovska V., Borsuk E., Nowis D., Dziembowski A.;
RT "The non-canonical poly(A) polymerase FAM46C acts as an onco-suppressor in
RT multiple myeloma.";
RL Nat. Commun. 8:619-619(2017).
RN [6] {ECO:0007744|PDB:7CQZ}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-349, CATALYTIC ACTIVITY,
RP FUNCTION, AND MUTAGENESIS OF ASN-72; GLY-73; SER-74; GLY-77; ASP-90;
RP ASP-92; CYS-146; GLU-166; ARG-175; ARG-240; SER-248; ARG-268; THR-290;
RP HIS-295 AND ASP-298.
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).
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 (PubMed:34048638). Can also elongate
CC RNA oligos ending with uridine molecule, provided that the sequence is
CC adenosine-rich (By similarity). Mainly targets mRNAs encoding
CC endoplasmic reticulum-targeted protein (PubMed:28931820).
CC {ECO:0000250|UniProtKB:Q5VWP2, ECO:0000269|PubMed:28931820,
CC 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:0000269|PubMed:34048638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC Evidence={ECO:0000305|PubMed:34048638};
CC -!- SUBUNIT: Interacts with BCCIP and PABPC1; the interaction has no effect
CC on TENT5C poly(A) polymerase function. Interacts with PLK4; this
CC interaction leads to the TENT5C recruitment into the centrosome.
CC {ECO:0000250|UniProtKB:Q5VWP2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VWP2}. Cytoplasm
CC {ECO:0000269|PubMed:28931820}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q5VWP2}.
CC Note=Recruited into the centrosome through its interaction with PLK4.
CC {ECO:0000250|UniProtKB:Q5VWP2}.
CC -!- TISSUE SPECIFICITY: Expressed by splenocytes, expression is increased
CC in activated splenocytes. {ECO:0000269|PubMed:28931820}.
CC -!- INDUCTION: In splenocytes, expression is highly induced after
CC yctivation by IL4 and LPS. {ECO:0000269|PubMed:28931820}.
CC -!- DISRUPTION PHENOTYPE: Animals do not display major developmental
CC phenotypes. They suffer from anemia with lower hemoglobin levels
CC compared to controls. They have increased proliferation of B cells.
CC {ECO:0000269|PubMed:28931820}.
CC -!- SIMILARITY: Belongs to the TENT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37072.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH46309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL663099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037072; AAH37072.1; ALT_INIT; mRNA.
DR EMBL; BC046309; AAH46309.1; ALT_INIT; mRNA.
DR EMBL; BC120717; AAI20718.1; -; mRNA.
DR EMBL; BC120719; AAI20720.1; -; mRNA.
DR EMBL; AK015259; BAB29768.1; -; mRNA.
DR CCDS; CCDS51017.1; -.
DR RefSeq; NP_001136424.1; NM_001142952.1.
DR RefSeq; XP_006502275.1; XM_006502212.3.
DR PDB; 7CQZ; X-ray; 2.35 A; A=1-349.
DR PDBsum; 7CQZ; -.
DR AlphaFoldDB; Q5SSF7; -.
DR SMR; Q5SSF7; -.
DR STRING; 10090.ENSMUSP00000056872; -.
DR EPD; Q5SSF7; -.
DR PaxDb; Q5SSF7; -.
DR PRIDE; Q5SSF7; -.
DR ProteomicsDB; 271841; -.
DR Antibodypedia; 33893; 111 antibodies from 20 providers.
DR Ensembl; ENSMUST00000061455; ENSMUSP00000056872; ENSMUSG00000044468.
DR GeneID; 74645; -.
DR KEGG; mmu:74645; -.
DR UCSC; uc008qqu.2; mouse.
DR CTD; 54855; -.
DR MGI; MGI:1921895; Tent5c.
DR VEuPathDB; HostDB:ENSMUSG00000044468; -.
DR eggNOG; KOG3852; Eukaryota.
DR GeneTree; ENSGT00940000158856; -.
DR HOGENOM; CLU_008115_2_0_1; -.
DR InParanoid; Q5SSF7; -.
DR OMA; NTRDCMS; -.
DR OrthoDB; 612201at2759; -.
DR PhylomeDB; Q5SSF7; -.
DR TreeFam; TF315239; -.
DR BRENDA; 2.7.7.19; 3474.
DR BioGRID-ORCS; 74645; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Fam46c; mouse.
DR PRO; PR:Q5SSF7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q5SSF7; protein.
DR Bgee; ENSMUSG00000044468; Expressed in blood and 210 other tissues.
DR Genevisible; Q5SSF7; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0048255; P:mRNA stabilization; IMP: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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Nucleotidyltransferase; Nucleus;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..391
FT /note="Terminal nucleotidyltransferase 5C"
FT /id="PRO_0000259935"
FT MUTAGEN 72
FT /note="N->A: Does not affect polynucleotide
FT adenylyltransferase activity. Increases cell apoptosis."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 72
FT /note="N->H: Significantly increases polynucleotide
FT adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 73
FT /note="G->A: Loss of polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 74
FT /note="S->A: Loss of polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 77
FT /note="G->S: Increases polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 90
FT /note="D->A: Loss of polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 92
FT /note="D->A: Loss of polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 146
FT /note="C->A: Significantly reduces polynucleotide
FT adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 166
FT /note="E->A: Loss of polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 175
FT /note="R->A: Loss of polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 240
FT /note="R->A: Loss of polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 248
FT /note="S->A: Does not affect polynucleotide
FT adenylyltransferase activity. Increases cell apoptosis."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 268
FT /note="R->A: Significantly reduces polynucleotide
FT adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 290
FT /note="T->R: Increases polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 295
FT /note="H->A: Loss of polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT MUTAGEN 298
FT /note="D->G: Increases polynucleotide adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:34048638"
FT CONFLICT 185
FT /note="Q -> H (in Ref. 3; BAB29768)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="R -> G (in Ref. 3; BAB29768)"
FT /evidence="ECO:0000305"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:7CQZ"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:7CQZ"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 300..317
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:7CQZ"
FT HELIX 323..342
FT /evidence="ECO:0007829|PDB:7CQZ"
SQ SEQUENCE 391 AA; 44797 MW; 78B23DD6F1CD7751 CRC64;
MAEEGSSTKD SESFSVLNWD QVSRLHEVLT EVVPIHGRGN FPTLEITLKD IVQTVRGRLE
EAGINVQDVR LNGSAAGHVL VKDNGLGCKD LDLIFHVALP TEAEFQLVRD VVLCSLLNFL
PEGVNKLKIS PVTLKEAYVQ KLVKVCTDTD RWSLISLSNK NGRNVELKFV DSIRRQFEFS
VDSFQIILDS LLFFYDCSGN PISEHFHPTV IGESMYGDFE EAFDHLQNRL IATKNPEEIR
GGGLLKYSNL LVRDFRPADQ EEIKTLERYM CSRFFIDFPD ILEQQRKLET YLQNHFSDEE
RSKYDYLMIL RRVVNESTVC LMGHERRQTL NLISLLALRV LAEQNIIPSA TNVTCYYQPA
PYVSDGNFNN YYIAHPPITY SQPYPTWLPC N
