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Q6A548

- TERT_CANFA

UniProt

Q6A548 - TERT_CANFA

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Protein

Telomerase reverse transcriptase

Gene
TERT
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei169 – 1691Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template By similarity
Metal bindingi702 – 7021Magnesium; catalytic By similarity
Sitei858 – 8581Required for nucleotide incorporation and primer extension rate By similarity
Metal bindingi859 – 8591Magnesium; catalytic By similarity
Metal bindingi860 – 8601Magnesium; catalytic By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. RNA binding Source: InterPro
  4. telomeric template RNA reverse transcriptase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Ribonucleoprotein, RNA-directed DNA polymerase, Transferase

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Telomerase reverse transcriptase (EC:2.7.7.49)
Alternative name(s):
Telomerase catalytic subunit
Gene namesi
Name:TERT
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

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-697. Dephosphorylation at this site by SHP2 retains TERT in the nucleus. Translocated to the nucleus by phosphorylation by AKT By similarity.

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleolus Source: UniProtKB-SubCell
  4. PML body Source: UniProtKB-SubCell
  5. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11231123Telomerase reverse transcriptasePRO_0000054924Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271Phosphoserine; by PKB/AKT1 By similarity
Modified residuei446 – 4461Phosphoserine; by DYRK2 By similarity
Modified residuei697 – 6971Phosphotyrosine; by SRC-type Tyr-kinases By similarity

Post-translational modificationi

Phosphorylation at Tyr-697 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-227 by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-446 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-446 by DYRK2. Ubiquitinated leads to proteasomal degradation By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ6A548.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini595 – 926332Reverse transcriptaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 230230RNA-interacting domain 1 By similarityAdd
BLAST
Regioni58 – 197140GQ motif By similarityAdd
BLAST
Regioni137 – 1415Required for regulating specificity for telomeric DNA and for processivity for primer elongation By similarity
Regioni231 – 30878Linker By similarityAdd
BLAST
Regioni309 – 539231RNA-interacting domain 2 By similarityAdd
BLAST
Regioni360 – 510151QFP motif By similarityAdd
BLAST
Regioni381 – 40121CP motif By similarityAdd
BLAST
Regioni905 – 91915Required for oligomerization By similarityAdd
BLAST
Regioni921 – 9255Primer grip sequence By similarity
Regioni927 – 1123197CTE By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi222 – 24019Bipartite nuclear localization signal By similarityAdd
BLAST

Domaini

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.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG276584.
HOGENOMiHOG000148780.
HOVERGENiHBG000460.
InParanoidiQ6A548.
KOiK11126.

Family and domain databases

InterProiIPR000477. RT_dom.
IPR021891. Telomerase_RBD.
IPR003545. Telomerase_RT.
[Graphical view]
PfamiPF00078. RVT_1. 1 hit.
PF12009. Telomerase_RBD. 1 hit.
[Graphical view]
PRINTSiPR01365. TELOMERASERT.
SMARTiSM00975. Telomerase_RBD. 1 hit.
[Graphical view]
PROSITEiPS50878. RT_POL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6A548-1 [UniParc]FASTAAdd to Basket

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MPRAPRCRAV RALLRGRYRE VLPLATFLRR LGPPGRLLVR RGDPAAFRAL     50
VAQCLVCVPW GARPPPAAPC FRQVSCLKEL VARVVQRLCE RGARNVLAFG 100
FALLDGARGG PPVAFTTSVR SYLPNTVTET LRGSGAWGLL LRRVGDDVLT 150
HLLARCALYL LVAPSCAYQV CGPPLYDLCA PASLPLPAPG LPGLPGLPGL 200
GAGAGASADL RPTRQAQNSG ARRRRGSPGS GVPLAKRPRR SVASEPERGA 250
HRSFPRAQQP PVSEAPAVTP AVAASPAASW EGGPPGTRPT TPAWHPYPGP 300
QGVPHDPAHP ETKRFLYCSG GRERLRPSFL LSALPPTLSG ARKLVETIFL 350
GSAPQKPGAA RRMRRLPARY WRMRPLFQEL LGNHARCPYR ALLRTHCPLR 400
AMAAKEGSGN QAHRGVGICP LERPVAAPQE QTDSTRLVQL LRQHSSPWQV 450
YAFLRACLCW LVPTGLWGSR HNQRRFLRNV KKFISLGKHA KLSLQELTWK 500
MKVRDCTWLH GNPGACCVPA AEHRRREEIL ARFLVLVDGH IYVVKLLRSF 550
FYVTETTFQK NRLFFYRKSV WSQLQSIGIR QLFNSVHLRE LSEAEVRRHR 600
EARPALLTSR LRFLPKPSGL RPIVNMDYIM GARTFHRDKK VQHLTSQLKT 650
LFSVLNYERA RRPSLLGASM LGMDDIHRAW RTFVLRIRAQ NPAPQLYFVK 700
VDVTGAYDAL PQDRLVEVIA NVIRPQESTY CVRHYAVVQR TARGHVRKAF 750
KRHVSTFADL QPYMRQFVER LQETSLLRDA VVIEQSSSLN EAGSSLFHLF 800
LRLVHNHVVR IGGKSYIQCQ GVPQGSILST LLCSLCYGDM ERRLFPGIEQ 850
DGVLLRLVDD FLLVTPHLTQ AQAFLRTLVK GVPEYGCRAN LQKTAVNFPV 900
EDGALGSAAP LQLPAHCLFP WCGLLLDTRT LEVSCDYSSY AHTSIRASLT 950
FSQGAKPGRN MRRKLLAVLR LKCCALFLDL QVNGIHTVYM NVYKIFLLQA 1000
YRFHACVLQL PFNQPVRKNP SFFLRVIADT ASCCYSLLKA RNAGLSLGAK 1050
GASGLFPSEA ARWLCLHAFL LKLAHHSGTY RCLLGALQAA KAHLSRQLPR 1100
GTLAALEAAA DPSLTADFKT ILD 1123
Length:1,123
Mass (Da):124,825
Last modified:September 13, 2004 - v1
Checksum:iF5F55D791106C1A3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF380351 mRNA. Translation: AAQ02791.1.
RefSeqiNP_001026800.1. NM_001031630.1.
UniGeneiCfa.114.

Genome annotation databases

GeneIDi403412.
KEGGicfa:403412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF380351 mRNA. Translation: AAQ02791.1 .
RefSeqi NP_001026800.1. NM_001031630.1.
UniGenei Cfa.114.

3D structure databases

ProteinModelPortali Q6A548.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 403412.
KEGGi cfa:403412.

Organism-specific databases

CTDi 7015.

Phylogenomic databases

eggNOGi NOG276584.
HOGENOMi HOG000148780.
HOVERGENi HBG000460.
InParanoidi Q6A548.
KOi K11126.

Miscellaneous databases

NextBioi 20816932.

Family and domain databases

InterProi IPR000477. RT_dom.
IPR021891. Telomerase_RBD.
IPR003545. Telomerase_RT.
[Graphical view ]
Pfami PF00078. RVT_1. 1 hit.
PF12009. Telomerase_RBD. 1 hit.
[Graphical view ]
PRINTSi PR01365. TELOMERASERT.
SMARTi SM00975. Telomerase_RBD. 1 hit.
[Graphical view ]
PROSITEi PS50878. RT_POL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and expression of the reverse transcriptase component of the Canis familiaris telomerase ribonucleoprotein (dogTERT)."
    Nasir L., Gault E., Campbell S., Veeramalai M., Gilbert D., McFarlane R., Munro A., Argyle D.J.
    Gene 336:105-113(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
    Tissue: Kidney.

Entry informationi

Entry nameiTERT_CANFA
AccessioniPrimary (citable) accession number: Q6A548
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: September 13, 2004
Last modified: March 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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