TET5C_MACFA
ID TET5C_MACFA Reviewed; 391 AA.
AC Q4R8X4;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Terminal nucleotidyltransferase 5C {ECO:0000305};
DE EC=2.7.7.19 {ECO:0000250|UniProtKB:Q5VWP2};
GN Name=TENT5C {ECO:0000250|UniProtKB:Q5VWP2};
GN Synonyms=FAM46C {ECO:0000250|UniProtKB:Q5VWP2};
GN ORFNames=QtsA-11212 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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. Can also elongate RNA oligos ending
CC with uridine molecule, provided that the sequence is adenosine-rich.
CC Mainly targets mRNAs encoding endoplasmic reticulum-targeted protein.
CC {ECO:0000250|UniProtKB:Q5VWP2}.
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:Q5VWP2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC Evidence={ECO:0000250|UniProtKB:Q5VWP2};
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:0000250|UniProtKB:Q5VWP2}. 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 -!- SIMILARITY: Belongs to the TENT family. {ECO:0000305}.
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DR EMBL; AB168323; BAE00447.1; -; mRNA.
DR RefSeq; NP_001271000.1; NM_001284071.1.
DR AlphaFoldDB; Q4R8X4; -.
DR SMR; Q4R8X4; -.
DR STRING; 9541.XP_005542241.1; -.
DR GeneID; 101926532; -.
DR CTD; 54855; -.
DR eggNOG; KOG3852; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; ISS: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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Nucleotidyltransferase; Nucleus;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..391
FT /note="Terminal nucleotidyltransferase 5C"
FT /id="PRO_0000259934"
SQ SEQUENCE 391 AA; 44963 MW; FBD90E1F28CD5F5F CRC64;
MAEESSCTRD CMSFSVLNWD QVSRLHEVLT EVVPIHGRGN FPTLEITLKD IVQTVRSRLE
EAGIKVQDVR LNGSAAGHVL VKDNGLGCKD LDLIFHVALP TEAEFQLVRD VVLCSLLNFL
PEGVNKLKIS PVTLKEAYVQ KLVKVCTDTD RWSLISLSNK NGKNVELKFV DSIRRQFEFS
VDSFQIILDS LLFFYDCSNN PISEHFHPTV IGESMYGDFE EAFDHLQNRL IATKNPEEIR
GGGLLKYSNL LVRDFRPTDQ EEIETLERYM CSRFFIDFPD ILEQQRKLET YLQNHFAEEE
RSKYDYLMIL RRVVNESTVC LMGHERRQTL NLISLLALRV LAEQNIIPNA TNVTCYYQPA
PYVSDGNFSN YYVAHPPVTY SQPYPTWLPC N