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Q6A548

- TERT_CANFA

UniProt

Q6A548 - TERT_CANFA

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
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      Previous versions | rss
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    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. RNA binding Source: InterPro
    4. telomeric template RNA reverse transcriptase activity Source: InterPro

    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-SubCell
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleolus Source: UniProtKB-SubCell
    4. PML body Source: UniProtKB-SubCell
    5. ribonucleoprotein complex Source: UniProtKB-KW

    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.

    Q6A548-1 [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: October 1, 2014
    This is version 67 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