TET5B_HUMAN
ID TET5B_HUMAN Reviewed; 425 AA.
AC Q96A09;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Terminal nucleotidyltransferase 5B {ECO:0000305};
DE EC=2.7.7.19 {ECO:0000269|PubMed:32009146, ECO:0000269|PubMed:34048638};
DE AltName: Full=Non-canonical poly(A) polymerase FAM46B;
GN Name=TENT5B {ECO:0000312|HGNC:HGNC:28273};
GN Synonyms=FAM46B {ECO:0000312|HGNC:HGNC:28273};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 FUNCTION.
RX PubMed=30532005; DOI=10.1038/s12276-018-0184-0;
RA Liang T., Ye X., Liu Y., Qiu X., Li Z., Tian B., Yan D.;
RT "FAM46B inhibits cell proliferation and cell cycle progression in prostate
RT cancer through ubiquitination of beta-catenin.";
RL Exp. Mol. Med. 50:1-12(2018).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-108; SER-109; LYS-124;
RP ASP-125; ASP-127; LYS-176; LYS-179; CYS-181; GLU-201; LYS-203; ARG-210;
RP GLU-213; ILE-216; ARG-269; GLU-272; ARG-275; LYS-281; ARG-303; ARG-321;
RP HIS-330 AND PHE-331, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
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).
RN [5]
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).
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 (PubMed:32009146, PubMed:34048638). May be
CC involved in maintaining the translation efficiency of at least some
CC genes through preventing degradation of their mRNAs (PubMed:32009146).
CC Prefers RNA molecules that are adenosine-rich close to 3'-end
CC (PubMed:32009146). In addition, may inhibit cell proliferation and cell
CC cycle progression through ubiquitination of beta-catenin/CTNNB1
CC (PubMed:30532005). {ECO:0000269|PubMed:30532005,
CC ECO:0000269|PubMed:32009146, 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:32009146, ECO:0000269|PubMed:34048638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC Evidence={ECO:0000305|PubMed:32009146};
CC -!- INTERACTION:
CC Q96A09; Q03154: ACY1; NbExp=3; IntAct=EBI-752030, EBI-742064;
CC Q96A09; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-752030, EBI-357530;
CC Q96A09; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-752030, EBI-11745576;
CC Q96A09; Q86V38: ATN1; NbExp=3; IntAct=EBI-752030, EBI-11954292;
CC Q96A09; P54253: ATXN1; NbExp=11; IntAct=EBI-752030, EBI-930964;
CC Q96A09; O14503: BHLHE40; NbExp=3; IntAct=EBI-752030, EBI-711810;
CC Q96A09; Q5SWW7: C10orf55; NbExp=5; IntAct=EBI-752030, EBI-12809220;
CC Q96A09; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-752030, EBI-18036948;
CC Q96A09; P55212: CASP6; NbExp=3; IntAct=EBI-752030, EBI-718729;
CC Q96A09; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-752030, EBI-12261896;
CC Q96A09; P28329-3: CHAT; NbExp=3; IntAct=EBI-752030, EBI-25837549;
CC Q96A09; P02489: CRYAA; NbExp=3; IntAct=EBI-752030, EBI-6875961;
CC Q96A09; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-752030, EBI-3867333;
CC Q96A09; Q15038: DAZAP2; NbExp=7; IntAct=EBI-752030, EBI-724310;
CC Q96A09; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-752030, EBI-744099;
CC Q96A09; A8MTA8-2: FAM166B; NbExp=3; IntAct=EBI-752030, EBI-12160437;
CC Q96A09; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-752030, EBI-12193763;
CC Q96A09; P22607: FGFR3; NbExp=3; IntAct=EBI-752030, EBI-348399;
CC Q96A09; P01100: FOS; NbExp=3; IntAct=EBI-752030, EBI-852851;
CC Q96A09; P53539: FOSB; NbExp=5; IntAct=EBI-752030, EBI-2806743;
CC Q96A09; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-752030, EBI-12018822;
CC Q96A09; P06396: GSN; NbExp=3; IntAct=EBI-752030, EBI-351506;
CC Q96A09; O00291: HIP1; NbExp=3; IntAct=EBI-752030, EBI-473886;
CC Q96A09; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-752030, EBI-7261162;
CC Q96A09; P52597: HNRNPF; NbExp=3; IntAct=EBI-752030, EBI-352986;
CC Q96A09; P04792: HSPB1; NbExp=3; IntAct=EBI-752030, EBI-352682;
CC Q96A09; P42858: HTT; NbExp=6; IntAct=EBI-752030, EBI-466029;
CC Q96A09; O60333-2: KIF1B; NbExp=3; IntAct=EBI-752030, EBI-10975473;
CC Q96A09; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-752030, EBI-6426443;
CC Q96A09; Q92876: KLK6; NbExp=3; IntAct=EBI-752030, EBI-2432309;
CC Q96A09; O76011: KRT34; NbExp=3; IntAct=EBI-752030, EBI-1047093;
CC Q96A09; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-752030, EBI-12805508;
CC Q96A09; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-752030, EBI-12111050;
CC Q96A09; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-752030, EBI-11962084;
CC Q96A09; Q13064: MKRN3; NbExp=3; IntAct=EBI-752030, EBI-2340269;
CC Q96A09; Q96HR8: NAF1; NbExp=3; IntAct=EBI-752030, EBI-2515597;
CC Q96A09; Q9BSH3: NICN1; NbExp=3; IntAct=EBI-752030, EBI-13324229;
CC Q96A09; Q6NSM0: NR1D2; NbExp=3; IntAct=EBI-752030, EBI-10250949;
CC Q96A09; P32243-2: OTX2; NbExp=3; IntAct=EBI-752030, EBI-9087860;
CC Q96A09; O00444: PLK4; NbExp=3; IntAct=EBI-752030, EBI-746202;
CC Q96A09; Q16633: POU2AF1; NbExp=3; IntAct=EBI-752030, EBI-943588;
CC Q96A09; P78424: POU6F2; NbExp=3; IntAct=EBI-752030, EBI-12029004;
CC Q96A09; O75360: PROP1; NbExp=3; IntAct=EBI-752030, EBI-9027467;
CC Q96A09; P60891: PRPS1; NbExp=3; IntAct=EBI-752030, EBI-749195;
CC Q96A09; P28062-2: PSMB8; NbExp=3; IntAct=EBI-752030, EBI-372312;
CC Q96A09; Q92530: PSMF1; NbExp=3; IntAct=EBI-752030, EBI-945916;
CC Q96A09; P62826: RAN; NbExp=3; IntAct=EBI-752030, EBI-286642;
CC Q96A09; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-752030, EBI-11987469;
CC Q96A09; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-752030, EBI-746118;
CC Q96A09; Q9BQY4: RHOXF2; NbExp=4; IntAct=EBI-752030, EBI-372094;
CC Q96A09; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-752030, EBI-10182375;
CC Q96A09; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-752030, EBI-396669;
CC Q96A09; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-752030, EBI-6257312;
CC Q96A09; Q9NP31: SH2D2A; NbExp=3; IntAct=EBI-752030, EBI-490630;
CC Q96A09; Q16348: SLC15A2; NbExp=3; IntAct=EBI-752030, EBI-12806032;
CC Q96A09; Q6P1M0-2: SLC27A4; NbExp=3; IntAct=EBI-752030, EBI-12898981;
CC Q96A09; Q8WU79: SMAP2; NbExp=3; IntAct=EBI-752030, EBI-2822515;
CC Q96A09; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-752030, EBI-12288855;
CC Q96A09; P35711: SOX5; NbExp=3; IntAct=EBI-752030, EBI-3505701;
CC Q96A09; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-752030, EBI-11959123;
CC Q96A09; O95947: TBX6; NbExp=3; IntAct=EBI-752030, EBI-2824328;
CC Q96A09; Q08117-2: TLE5; NbExp=6; IntAct=EBI-752030, EBI-11741437;
CC Q96A09; Q63HR2: TNS2; NbExp=3; IntAct=EBI-752030, EBI-949753;
CC Q96A09; Q15645: TRIP13; NbExp=3; IntAct=EBI-752030, EBI-358993;
CC Q96A09; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-752030, EBI-2514383;
CC Q96A09; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-752030, EBI-947187;
CC Q96A09; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-752030, EBI-11975223;
CC Q96A09; O76024: WFS1; NbExp=3; IntAct=EBI-752030, EBI-720609;
CC Q96A09; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-752030, EBI-2515601;
CC Q96A09; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-752030, EBI-742550;
CC Q96A09; Q96F45: ZNF503; NbExp=3; IntAct=EBI-752030, EBI-8832437;
CC Q96A09; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-752030, EBI-4395669;
CC Q96A09; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-752030, EBI-4395732;
CC Q96A09; Q9Y649; NbExp=3; IntAct=EBI-752030, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32009146}. Nucleus
CC {ECO:0000269|PubMed:32009146}.
CC -!- DEVELOPMENTAL STAGE: Uniquely and highly expressed in pre-implantation
CC embryos and pluripotent stem cells, but sharply down-regulated
CC following differentiation. {ECO:0000269|PubMed:32009146}.
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=AAH12790.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH14160.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL356390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012790; AAH12790.1; ALT_INIT; mRNA.
DR EMBL; BC014160; AAH14160.1; ALT_INIT; mRNA.
DR CCDS; CCDS294.2; -.
DR RefSeq; NP_443175.2; NM_052943.3.
DR AlphaFoldDB; Q96A09; -.
DR SMR; Q96A09; -.
DR BioGRID; 125440; 68.
DR IntAct; Q96A09; 74.
DR STRING; 9606.ENSP00000289166; -.
DR iPTMnet; Q96A09; -.
DR PhosphoSitePlus; Q96A09; -.
DR BioMuta; FAM46B; -.
DR DMDM; 294862433; -.
DR EPD; Q96A09; -.
DR jPOST; Q96A09; -.
DR MassIVE; Q96A09; -.
DR MaxQB; Q96A09; -.
DR PaxDb; Q96A09; -.
DR PeptideAtlas; Q96A09; -.
DR PRIDE; Q96A09; -.
DR ProteomicsDB; 75890; -.
DR Antibodypedia; 69553; 35 antibodies from 9 providers.
DR DNASU; 115572; -.
DR Ensembl; ENST00000289166.6; ENSP00000289166.5; ENSG00000158246.8.
DR GeneID; 115572; -.
DR KEGG; hsa:115572; -.
DR MANE-Select; ENST00000289166.6; ENSP00000289166.5; NM_052943.4; NP_443175.2.
DR UCSC; uc010ofj.3; human.
DR CTD; 115572; -.
DR DisGeNET; 115572; -.
DR GeneCards; TENT5B; -.
DR HGNC; HGNC:28273; TENT5B.
DR HPA; ENSG00000158246; Tissue enhanced (esophagus, skin).
DR MIM; 619069; gene.
DR neXtProt; NX_Q96A09; -.
DR OpenTargets; ENSG00000158246; -.
DR PharmGKB; PA134962922; -.
DR VEuPathDB; HostDB:ENSG00000158246; -.
DR eggNOG; KOG3852; Eukaryota.
DR GeneTree; ENSGT00940000160747; -.
DR HOGENOM; CLU_008115_2_0_1; -.
DR InParanoid; Q96A09; -.
DR OMA; TTVNYYV; -.
DR OrthoDB; 612201at2759; -.
DR PhylomeDB; Q96A09; -.
DR TreeFam; TF315239; -.
DR BRENDA; 2.7.7.19; 2681.
DR PathwayCommons; Q96A09; -.
DR SignaLink; Q96A09; -.
DR BioGRID-ORCS; 115572; 7 hits in 1082 CRISPR screens.
DR ChiTaRS; FAM46B; human.
DR GenomeRNAi; 115572; -.
DR Pharos; Q96A09; Tdark.
DR PRO; PR:Q96A09; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96A09; protein.
DR Bgee; ENSG00000158246; Expressed in skin of leg and 114 other tissues.
DR Genevisible; Q96A09; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA: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; IMP:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP: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 Cytoplasm; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..425
FT /note="Terminal nucleotidyltransferase 5B"
FT /id="PRO_0000259931"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 108
FT /note="G->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 109
FT /note="S->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 124
FT /note="K->A: Does not affect polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 125
FT /note="D->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 127
FT /note="D->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 176
FT /note="K->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 179
FT /note="K->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 181
FT /note="C->A: Reduces polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 201
FT /note="E->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 203
FT /note="K->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 210
FT /note="R->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 213
FT /note="E->A: Substantially reduces polyadenylation
FT activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 216
FT /note="I->S: Substantially reduces polyadenylation
FT activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 269
FT /note="R->A: Substantially reduces polyadenylation
FT activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 272
FT /note="E->A: Substantially reduces polyadenylation
FT activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 275
FT /note="R->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 281
FT /note="K->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 303
FT /note="R->A: Does not affect polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 321
FT /note="R->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 330
FT /note="H->A: Loss of polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
FT MUTAGEN 331
FT /note="F->A: Does not affect polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:32009146"
SQ SEQUENCE 425 AA; 46688 MW; A0FD17359AF2C6DD CRC64;
MMPSESGAER RDRAAAQVGT AAATAVATAA PAGGGPDPEA LSAFPGRHLS GLSWPQVKRL
DALLSEPIPI HGRGNFPTLS VQPRQIVQVV RSTLEEQGLH VHSVRLHGSA ASHVLHPESG
LGYKDLDLVF RVDLRSEASF QLTKAVVLAC LLDFLPAGVS RAKITPLTLK EAYVQKLVKV
CTDSDRWSLI SLSNKSGKNV ELKFVDSVRR QFEFSIDSFQ IILDSLLLFG QCSSTPMSEA
FHPTVTGESL YGDFTEALEH LRHRVIATRS PEEIRGGGLL KYCHLLVRGF RPRPSTDVRA
LQRYMCSRFF IDFPDLVEQR RTLERYLEAH FGGADAARRY ACLVTLHRVV NESTVCLMNH
ERRQTLDLIA ALALQALAEQ GPAATAALAW RPPGTDGVVP ATVNYYVTPV QPLLAHAYPT
WLPCN
