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Q27ID4 (TERT_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Telomerase reverse transcriptase

EC=2.7.7.49
Alternative name(s):
Telomerase catalytic subunit
Gene names
Name:TERT
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1125 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis By similarity.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Subunit structure

Homodimer; dimerization is required to produce a functional complex. Oligomer; can form oligomers in the absence of the telomerase RNA template component (TERC). Catalytic subunit of the telomerase holoenzyme complex composed minimally of TERT and TERC. The telomerase complex is composed of TERT, DKC1, WDR79/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). The molecular chaperone HSP90/P23 complex is required for correct assembly and stabilization of the active telomerase. Interacts directly with HSP90A and PTGES3. Interacts with HSPA1A; the interaction occurs in the absence of TERC and dissociates once the complex has formed. Interacts with RAN; the interaction promotes nuclear export of TERT. Interacts with XPO1. Interacts with PTPN11; the interaction retains TERT in the nucleus. Interacts with NCL (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains); the interaction is important for nucleolar localization of TERT. Interacts with SMARCA4 (via the bromodomain); the interaction regulates Wnt-mediated signaling By similarity. Interacts with MCRS1 (isoform MCRS2);the interaction inhibits in vitro telomerase activity. Interacts with PIF1; the interaction has no effect on the elongation activity of TERT. Interacts with PML; the interaction recruits TERT to PML bodies and inhibits telomerase activity By similarity. Interacts with GNL3L By similarity.

Subcellular location

Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. Nucleus. Chromosometelomere. Cytoplasm By similarity. NucleusPML body By similarity. Note: Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage. Diffuse localization in the nucleoplasm. Enriched in nucleoli of certain cell types. Translocated to the cytoplasm via nuclear pores in a CRM1/RAN-dependent manner involving oxidative stress-mediated phosphorylation at Tyr-700. Dephosphorylation at this site by SHP2 retains TERT in the nucleus. Translocated to the nucleus by phosphorylation by AKT By similarity.

Domain

The primer grip sequence in the RT domain is required for telomerase activity and for stable association with short telomeric primers By similarity.

The RNA-interacting domain 1 (RD1)/N-terminal extension (NTE) is required for interaction with the pseudoknot-template domain of each of TERC dimers. It contains anchor sites that bind primer nucleotides upstream of the RNA-DNA hybrid and is thus an essential determinant of repeat addition processivity By similarity.

The RNA-interacting domain 2 (RD2) is essential for both interaction with the CR4-CR5 domain of TERC and for DNA sythesis By similarity.

Post-translational modification

Phosphorylation at Tyr-700 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation at Ser-231 by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-450 by DYRK2 promotes ubiquitination by the EDVP complex and degradation By similarity.

Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-450 by DYRK2. Ubiquitinated leads to proteasomal degradation By similarity.

Sequence similarities

Belongs to the reverse transcriptase family. Telomerase subfamily.

Contains 1 reverse transcriptase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11251125Telomerase reverse transcriptase
PRO_0000245166

Regions

Domain598 – 928331Reverse transcriptase
Region1 – 234234RNA-interacting domain 1 By similarity
Region58 – 199142GQ motif By similarity
Region137 – 1415Required for regulating specificity for telomeric DNA and for processivity for primer elongation By similarity
Region235 – 31278Linker By similarity
Region290 – 531242Required for oligomerization By similarity
Region313 – 543231RNA-interacting domain 2 By similarity
Region364 – 514151QFP motif By similarity
Region385 – 40521CP motif By similarity
Region907 – 92115Required for oligomerization By similarity
Region923 – 9275Primer grip sequence By similarity
Region929 – 1125197CTE By similarity
Motif226 – 24419Bipartite nuclear localization signal By similarity
Compositional bias180 – 1856Poly-Ala

Sites

Metal binding7051Magnesium; catalytic By similarity
Metal binding8611Magnesium; catalytic By similarity
Metal binding8621Magnesium; catalytic By similarity
Site1691Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template By similarity
Site8601Required for nucleotide incorporation and primer extension rate By similarity

Amino acid modifications

Modified residue2311Phosphoserine; by PKB/AKT1 By similarity
Modified residue4501Phosphoserine; by DYRK2 By similarity
Modified residue7001Phosphotyrosine; by SRC-type Tyr-kinases By similarity

Sequences

Sequence LengthMass (Da)Tools
Q27ID4 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 717F437B50BB747B

FASTA1,125124,447
        10         20         30         40         50         60 
MPRAPRCRAV RALLRASYRQ VLPLAAFVRR LRPQGHRLVR RGDPAAFRAL VAQCLVCVPW 

        70         80         90        100        110        120 
DAQPPPAAPS FRQVSCLKEL VARVVQRLCE RGARNVLAFG FTLLAGARGG PPVAFTTSVR 

       130        140        150        160        170        180 
SYLPNTVTDT LRGSGAWGLL LHRVGDDVLT HLLSRCALYL LVPPTCAYQV CGPPLYDLRA 

       190        200        210        220        230        240 
AAAAARRPTR QVGGTRAGFG LPRPASSNGG HGEAEGLLEA RAQGARRRRS SARGRLPPAK 

       250        260        270        280        290        300 
RPRRGLEPGR DLEGQVARSP PRVVTPTRDA AEAKSRKGDV PGPCRLFPGG ERGVGSASWR 

       310        320        330        340        350        360 
LSPSEGEPGA GACAETKRFL YCSGGGEQLR RSFLLCSLPP SLAGARTLVE TIFLDSKPGP 

       370        380        390        400        410        420 
PGAPRRPRRL PARYWQMRPL FRKLLGNHAR SPYGALLRAH CPLPASAPRA GPDHQKCPGV 

       430        440        450        460        470        480 
GGCPSERPAA APEGEANSGR LVQLLRQHSS PWQVYGLLRA CLRRLVPAGL WGSRHNERRF 

       490        500        510        520        530        540 
LRNVKKLLSL GKHGRLSQQE LTWKMKVQDC AWLRASPGAR CVPAAEHRQR EAVLGRFLHW 

       550        560        570        580        590        600 
LMGAYVVELL RSFFYVTETT FQKNRLFFFR KRIWSQLQRL GVRQHLDRVR LRELSEAEVR 

       610        620        630        640        650        660 
QHQEARPALL TSRLRFVPKP GGLRPIVNVG CVEGAPAPPR DKKVQHLSSR VKTLFAVLNY 

       670        680        690        700        710        720 
ERARRPGLLG ASVLGMDDIH RAWRAFVLPL RARGPAPPLY FVKVDVVGAY DALPQDKLAE 

       730        740        750        760        770        780 
VIANVLQPQE NTYCVRHCAM VRTARGRMRK SFKRHVSTFS DFQPYLRQLV EHLQAMGSLR 

       790        800        810        820        830        840 
DAVVIEQSCS LNEPGSSLFN LFLHLVRSHV IRIGGRSYIQ CQGIPQGSIL STLLCSFCYG 

       850        860        870        880        890        900 
DMENKLFPGV QQDGVLLRLV DDFLLVTPHL TRARDFLRTL VRGVPEYGCQ VNLRKTVVNF 

       910        920        930        940        950        960 
PVEPGALGGA APLQLPAHCL FPWCGLLLDT RTLEVHGDHS SYARTSIRAS LTFTQGFKPG 

       970        980        990       1000       1010       1020 
RNMRRKLLAV LQLKCHGLFL DLQVNSLQTV FTNVYKIFLL QAYRFHACVL QLPFSQPVRS 

      1030       1040       1050       1060       1070       1080 
SPAFFLQVIA DTASRGYALL KARNAGASLG ARGAAGLFPS EAAQWLCLHA FLLKLARHRV 

      1090       1100       1110       1120 
TYSRLLGALR TARARLHRQL PGPTRAALEA AADPALTADF KTILD 

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References

[1]"Cloning and expression of the reverse transcriptase component of Bos taurus telomerase."
Zhao D., Du Z., Li N.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ399842 Genomic DNA. Translation: ABD61652.2.
RefSeqNP_001039707.1. NM_001046242.1.
UniGeneBt.60929.

3D structure databases

ProteinModelPortalQ27ID4.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ27ID4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID518884.
KEGGbta:518884.

Organism-specific databases

CTD7015.

Phylogenomic databases

eggNOGNOG276584.
HOGENOMHOG000148780.
HOVERGENHBG000460.
InParanoidQ27ID4.
KOK11126.

Family and domain databases

InterProIPR000477. RT_dom.
IPR021891. Telomerase_RBD.
IPR003545. Telomerase_RT.
[Graphical view]
PfamPF00078. RVT_1. 1 hit.
PF12009. Telomerase_RBD. 1 hit.
[Graphical view]
PRINTSPR01365. TELOMERASERT.
SMARTSM00975. Telomerase_RBD. 1 hit.
[Graphical view]
PROSITEPS50878. RT_POL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20872758.

Entry information

Entry nameTERT_BOVIN
AccessionPrimary (citable) accession number: Q27ID4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 2, 2006
Last modified: March 19, 2014
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families