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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).By similarity

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

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 templateBy similarity
Metal bindingi702 – 7021Magnesium; catalyticPROSITE-ProRule annotation
Sitei858 – 8581Required for nucleotide incorporation and primer extension rateBy similarity
Metal bindingi859 – 8591Magnesium; catalyticPROSITE-ProRule annotation
Metal bindingi860 – 8601Magnesium; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. 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).By similarity

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
  4. 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/AKT1By similarity
Modified residuei446 – 4461Phosphoserine; by DYRK2By similarity
Modified residuei697 – 6971Phosphotyrosine; by SRC-type Tyr-kinasesBy 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).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).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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6A548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini595 – 926332Reverse transcriptasePROSITE-ProRule annotationAdd
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi222 – 24019Bipartite nuclear localization signalBy 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).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

Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation

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 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MPRAPRCRAV RALLRGRYRE VLPLATFLRR LGPPGRLLVR RGDPAAFRAL
60 70 80 90 100
VAQCLVCVPW GARPPPAAPC FRQVSCLKEL VARVVQRLCE RGARNVLAFG
110 120 130 140 150
FALLDGARGG PPVAFTTSVR SYLPNTVTET LRGSGAWGLL LRRVGDDVLT
160 170 180 190 200
HLLARCALYL LVAPSCAYQV CGPPLYDLCA PASLPLPAPG LPGLPGLPGL
210 220 230 240 250
GAGAGASADL RPTRQAQNSG ARRRRGSPGS GVPLAKRPRR SVASEPERGA
260 270 280 290 300
HRSFPRAQQP PVSEAPAVTP AVAASPAASW EGGPPGTRPT TPAWHPYPGP
310 320 330 340 350
QGVPHDPAHP ETKRFLYCSG GRERLRPSFL LSALPPTLSG ARKLVETIFL
360 370 380 390 400
GSAPQKPGAA RRMRRLPARY WRMRPLFQEL LGNHARCPYR ALLRTHCPLR
410 420 430 440 450
AMAAKEGSGN QAHRGVGICP LERPVAAPQE QTDSTRLVQL LRQHSSPWQV
460 470 480 490 500
YAFLRACLCW LVPTGLWGSR HNQRRFLRNV KKFISLGKHA KLSLQELTWK
510 520 530 540 550
MKVRDCTWLH GNPGACCVPA AEHRRREEIL ARFLVLVDGH IYVVKLLRSF
560 570 580 590 600
FYVTETTFQK NRLFFYRKSV WSQLQSIGIR QLFNSVHLRE LSEAEVRRHR
610 620 630 640 650
EARPALLTSR LRFLPKPSGL RPIVNMDYIM GARTFHRDKK VQHLTSQLKT
660 670 680 690 700
LFSVLNYERA RRPSLLGASM LGMDDIHRAW RTFVLRIRAQ NPAPQLYFVK
710 720 730 740 750
VDVTGAYDAL PQDRLVEVIA NVIRPQESTY CVRHYAVVQR TARGHVRKAF
760 770 780 790 800
KRHVSTFADL QPYMRQFVER LQETSLLRDA VVIEQSSSLN EAGSSLFHLF
810 820 830 840 850
LRLVHNHVVR IGGKSYIQCQ GVPQGSILST LLCSLCYGDM ERRLFPGIEQ
860 870 880 890 900
DGVLLRLVDD FLLVTPHLTQ AQAFLRTLVK GVPEYGCRAN LQKTAVNFPV
910 920 930 940 950
EDGALGSAAP LQLPAHCLFP WCGLLLDTRT LEVSCDYSSY AHTSIRASLT
960 970 980 990 1000
FSQGAKPGRN MRRKLLAVLR LKCCALFLDL QVNGIHTVYM NVYKIFLLQA
1010 1020 1030 1040 1050
YRFHACVLQL PFNQPVRKNP SFFLRVIADT ASCCYSLLKA RNAGLSLGAK
1060 1070 1080 1090 1100
GASGLFPSEA ARWLCLHAFL LKLAHHSGTY RCLLGALQAA KAHLSRQLPR
1110 1120
GTLAALEAAA DPSLTADFKT ILD
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: October 29, 2014
This is version 68 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