Overview
| Uniprot ID | Q5VYS8 |
| Protein Name | Terminal uridylyltransferase 7 |
| Gene Name | TUT7 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 130 |
PVINRQRKDSFQENE |
Function
Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:19703396, PubMed:25480299). Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth (By similarity). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets (PubMed:25480299). Also functions as an integral regulator of microRNA biogenesiS using 3 different uridylation mechanisms (PubMed:25979828). Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7). Uridylated pre-let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7 uridylation is strongly enhanced in the presence of LIN28A (PubMed:22898984). In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing (PubMed:25979828, PubMed:28671666). Add oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (PubMed:25979828). Does not play a role in replication-dependent histone mRNA degradation (PubMed:18172165). Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult (PubMed:18172165, PubMed:19703396, PubMed:22898984, PubMed:25480299, PubMed:25979828, PubMed:28671666). TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (PubMed:30122351)
Protein Sequence
10
MGDTAKPYFV
20
KRTKDRGTMD
30
DDDFRRGHPQ
40
QDYLIIDDHA
50
KGHGSKMEKG
60
LQKKKITPGN
70
YGNTPRKGPC
80
AVSSNPYAFK
90
NPIYSQPAWM
100
NDSHKDQSKR
110
WLSDEHTGNS
120
DNWREFKPGP
130
RIPVINRQRK
140
DSFQENEDGY
150
RWQDTRGCRT
160
VRRLFHKDLT
170
SLETTSEMEA
180
GSPENKKQRS
190
RPRKPRKTRN
200
EENEQDGDLE
210
GPVIDESVLS
220
TKELLGLQQA
230
EERLKRDCID
240
RLKRRPRNYP
250
TAKYTCRLCD
260
VLIESIAFAH
270
KHIKEKRHKK
280
NIKEKQEEEL
290
LTTLPPPTPS
300
QINAVGIAID
310
KVVQEFGLHN
320
ENLEQRLEIK
330
RIMENVFQHK
340
LPDCSLRLYG
350
SSCSRLGFKN
360
SDVNIDIQFP
370
AIMSQPDVLL
380
LVQECLKNSD
390
SFIDVDADFH
400
ARVPVVVCRE
410
KQSGLLCKVS
420
AGNENACLTT
430
KHLTALGKLE
440
PKLVPLVIAF
450
RYWAKLCSID
460
RPEEGGLPPY
470
VFALMAIFFL
480
QQRKEPLLPV
490
YLGSWIEGFS
500
LSKLGNFNLQ
510
DIEKDVVIWE
520
HTDSAAGDTG
530
ITKEEAPRET
540
PIKRGQVSLI
550
LDVKHQPSVP
560
VGQLWVELLR
570
FYALEFNLAD
580
LVISIRVKEL
590
VSRELKDWPK
600
KRIAIEDPYS
610
VKRNVARTLN
620
SQPVFEYILH
630
CLRTTYKYFA
640
LPHKITKSSL
650
LKPLNAITCI
660
SEHSKEVINH
670
HPDVQTKDDK
680
LKNSVLAQGP
690
GATSSAANTC
700
KVQPLTLKET
710
AESFGSPPKE
720
EMGNEHISVH
730
PENSDCIQAD
740
VNSDDYKGDK
750
VYHPETGRKN
760
EKEKVGRKGK
770
HLLTVDQKRG
780
EHVVCGSTRN
790
NESESTLDLE
800
GFQNPTAKEC
810
EGLATLDNKA
820
DLDGESTEGT
830
EELEDSLNHF
840
THSVQGQTSE
850
MIPSDEEEED
860
DEEEEEEEEP
870
RLTINQREDE
880
DGMANEDELD
890
NTYTGSGDED
900
ALSEEDDELG
910
EAAKYEDVKE
920
CGKHVERALL
930
VELNKISLKE
940
ENVCEEKNSP
950
VDQSDFFYEF
960
SKLIFTKGKS
970
PTVVCSLCKR
980
EGHLKKDCPE
990
DFKRIQLEPL
1000
PPLTPKFLNI
1010
LDQVCIQCYK
1020
DFSPTIIEDQ
1030
AREHIRQNLE
1040
SFIRQDFPGT
1050
KLSLFGSSKN
1060
GFGFKQSDLD
1070
VCMTINGLET
1080
AEGLDCVRTI
1090
EELARVLRKH
1100
SGLRNILPIT
1110
TAKVPIVKFF
1120
HLRSGLEVDI
1130
SLYNTLALHN
1140
TRLLSAYSAI
1150
DPRVKYLCYT
1160
MKVFTKMCDI
1170
GDASRGSLSS
1180
YAYTLMVLYF
1190
LQQRNPPVIP
1200
VLQEIYKGEK
1210
KPEIFVDGWN
1220
IYFFDQIDEL
1230
PTYWSECGKN
1240
TESVGQLWLG
1250
LLRFYTEEFD
1260
FKEHVISIRR
1270
KSLLTTFKKQ
1280
WTSKYIVIED
1290
PFDLNHNLGA
1300
GLSRKMTNFI
1310
MKAFINGRRV
1320
FGIPVKGFPK
1330
DYPSKMEYFF
1340
DPDVLTEGEL
1350
APNDRCCRIC
1360
GKIGHFMKDC
1370
PMRRKVRRRR
1380
DQEDALNQRY
1390
PENKEKRSKE
1400
DKEIHNKYTE
1410
REVSTKEDKP
1420
IQCTPQKAKP
1430
MRAAADLGRE
1440
KILRPPVEKW
1450
KRQDDKDLRE
1460
KRCFICGREG
1470
HIKKECPQFK
1480
GSSGSLSSKY
1490
MTQGKASAKR
TQQES
Gene Ontology
| Classification |
GO ID |
Description |
| Biological Process |
GO:0031123 |
RNA 3'-end processing |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0035198 |
miRNA binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0050265 |
RNA uridylyltransferase activity |
| Molecular Function |
GO:0070569 |
uridylyltransferase activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0010586 |
miRNA metabolic process |
| Biological Process |
GO:0001556 |
oocyte maturation |
| Biological Process |
GO:1990074 |
polyuridylation-dependent mRNA catabolic process |
| Biological Process |
GO:0031054 |
pre-miRNA processing |
| Biological Process |
GO:0141008 |
transposable element silencing by mRNA destabilization |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.