TERT_RAT
ID TERT_RAT Reviewed; 1125 AA.
AC Q673L6; Q1LZ57; Q4U0V7; Q673L3; Q673L5; Q80SU5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Telomerase reverse transcriptase;
DE EC=2.7.7.49;
DE AltName: Full=Telomerase catalytic subunit;
GN Name=Tert {ECO:0000312|RGD:70494};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAT09124.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Brown Norway {ECO:0000312|EMBL:AAT09124.1};
RX PubMed=16454671; DOI=10.2174/092986606774502108;
RA Kaneko R., Esumi S., Yagi T., Hirabayashi T.;
RT "Predominant expression of rTERTb, an inactive TERT variant, in the adult
RT rat brain.";
RL Protein Pept. Lett. 13:59-65(2006).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAY40300.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58, AND INDUCTION.
RX PubMed=16205635; DOI=10.1038/sj.onc.1209140;
RA Hu B., Tack D.C., Liu T., Wu Z., Ullenbruch M.R., Phan S.H.;
RT "Role of Smad3 in the regulation of rat telomerase reverse transcriptase by
RT TGFbeta.";
RL Oncogene 25:1030-1041(2006).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAD29524.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 46-161, AND TISSUE SPECIFICITY.
RC STRAIN=Fischer {ECO:0000312|EMBL:CAD29524.1};
RX PubMed=12729609; DOI=10.1016/s0003-2697(03)00091-5;
RA Holzmann K., Berger W., Mejri D., Cerni C., Sasgary S.;
RT "Detection and quantification of transcripts for the catalytic subunit TERT
RT and the RNA component of telomerase in rat tissue.";
RL Anal. Biochem. 317:120-123(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:DAA01427.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway;
RA Kim M.H., Choi C.;
RT "The identification and characterization of rat telomerase catalytic
RT subunit rTERT mRNA from rat genomic sequence.";
RL Chonnam Med. J. 41:1-13(2005).
CC -!- FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the
CC replication of chromosome termini in most eukaryotes. Active in
CC progenitor and cancer cells. Inactive, or very low activity, in normal
CC somatic cells. Catalytic component of the teleromerase holoenzyme
CC complex whose main activity is the elongation of telomeres by acting as
CC a reverse transcriptase that adds simple sequence repeats to chromosome
CC ends by copying a template sequence within the RNA component of the
CC enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini
CC with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The
CC catalytic cycle involves primer binding, primer extension and release
CC of product once the template boundary has been reached or nascent
CC product translocation followed by further extension. More active on
CC substrates containing 2 or 3 telomeric repeats. Telomerase activity is
CC regulated by a number of factors including telomerase complex-
CC associated proteins, chaperones and polypeptide modifiers. Modulates
CC Wnt signaling. Plays important roles in aging and antiapoptosis (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- SUBUNIT: Catalytic component of the telomerase holoenzyme complex
CC composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two
CC molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2
CC and GAR1, and a telomerase RNA template component (TERC). The
CC telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and
CC POT1. The molecular chaperone HSP90/P23 complex is required for correct
CC assembly and stabilization of the active telomerase. Interacts directly
CC with HSP90A and PTGES3. Interacts with HSPA1A; the interaction occurs
CC in the absence of TERC and dissociates once the complex has formed.
CC Interacts with RAN; the interaction promotes nuclear export of TERT.
CC Interacts with XPO1. Interacts with PTPN11; the interaction retains
CC TERT in the nucleus. Interacts with NCL (via RRM1 and C-terminal
CC RRM4/Arg/Gly-rich domains); the interaction is important for nucleolar
CC localization of TERT (By similarity). Interacts with SMARCA4 (via the
CC bromodomain); the interaction regulates Wnt-mediated signaling (By
CC similarity). Interacts with MCRS1 (isoform MCRS2); the interaction
CC inhibits in vitro telomerase activity (By similarity). Interacts with
CC PIF1; the interaction has no effect on the elongation activity of TERT
CC (By similarity). Interacts with PML; the interaction recruits TERT to
CC PML bodies and inhibits telomerase activity (By similarity). Interacts
CC with GNL3L (By similarity). Interacts with isoform 1 and isoform 2 of
CC NVL (By similarity). Interacts with DHX36 (By similarity). Interacts
CC with ATF7 (By similarity). {ECO:0000250|UniProtKB:O14746,
CC ECO:0000250|UniProtKB:O70372}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O14746}. Nucleus, nucleoplasm {ECO:0000250}.
CC Nucleus {ECO:0000305}. Chromosome, telomere. Cytoplasm {ECO:0000250}.
CC Nucleus, PML body {ECO:0000250}. Note=Shuttling between nuclear and
CC cytoplasm depends on cell cycle, phosphorylation states, transformation
CC and DNA damage. Diffuse localization in the nucleoplasm. Enriched in
CC nucleoli of certain cell types. Translocated to the cytoplasm via
CC nuclear pores in a CRM1/RAN-dependent manner involving oxidative
CC stress-mediated phosphorylation at Tyr-697. Dephosphorylation at this
CC site by SHP2 retains TERT in the nucleus. Translocated to the nucleus
CC by phosphorylation by AKT (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:16454671};
CC IsoId=Q673L6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16454671}; Synonyms=a
CC {ECO:0000269|PubMed:16454671};
CC IsoId=Q673L6-2; Sequence=VSP_052083;
CC Name=3 {ECO:0000269|PubMed:16454671}; Synonyms=b
CC {ECO:0000269|PubMed:16454671}, c {ECO:0000269|PubMed:16454671};
CC IsoId=Q673L6-3; Sequence=VSP_052081, VSP_052082;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 expressed in thymus, liver,
CC spleen, lung, kidney and testis. High level of inactive isoform 3 in
CC adult hippocampus, low level in heart, cortex and cerebellum.
CC {ECO:0000269|PubMed:12729609, ECO:0000269|PubMed:16454671}.
CC -!- DEVELOPMENTAL STAGE: High activity in cortex at embryonic stage 16 and
CC postnatal day 2. Low activity in cortex from postnatal day 5.
CC {ECO:0000269|PubMed:16454671}.
CC -!- INDUCTION: Down-regulated by TGFbeta in fibroblasts. This inhibition is
CC mediated by SMAD3. {ECO:0000269|PubMed:16205635}.
CC -!- DOMAIN: The primer grip sequence in the RT domain is required for
CC telomerase activity and for stable association with short telomeric
CC primers. {ECO:0000250}.
CC -!- DOMAIN: The RNA-interacting domain 1 (RD1)/N-terminal extension (NTE)
CC is required for interaction with the pseudoknot-template domain of each
CC of TERC dimers. It contains anchor sites that bind primer nucleotides
CC upstream of the RNA-DNA hybrid and is thus an essential determinant of
CC repeat addition processivity (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The RNA-interacting domain 2 (RD2) is essential for both
CC interaction with the CR4-CR5 domain of TERC and for DNA synthesis.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at Tyr-697 under oxidative stress leads to
CC translocation of TERT to the cytoplasm and reduces its antiapoptotic
CC activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention.
CC Phosphorylation at the G2/M phase at Ser-447 by DYRK2 promotes
CC ubiquitination by the EDVP complex and degradation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the EDVP complex, a E3 ligase complex following
CC phosphorylation at Ser-447 by DYRK2. Ubiquitinated leads to proteasomal
CC degradation (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: Inactive form. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC subfamily. {ECO:0000255}.
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DR EMBL; AY539717; AAT09124.1; -; mRNA.
DR EMBL; AY539718; AAT09125.1; -; mRNA.
DR EMBL; AY539719; AAT09126.1; -; mRNA.
DR EMBL; AY539720; AAT09127.1; -; mRNA.
DR EMBL; AC123569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ021473; AAY40300.1; -; Genomic_DNA.
DR EMBL; AJ440965; CAD29524.1; -; mRNA.
DR EMBL; AJ440966; CAD29525.2; -; Genomic_DNA.
DR EMBL; BK000660; DAA01427.1; -; mRNA.
DR RefSeq; NP_445875.1; NM_053423.1. [Q673L6-1]
DR AlphaFoldDB; Q673L6; -.
DR SMR; Q673L6; -.
DR STRING; 10116.ENSRNOP00000022683; -.
DR BindingDB; Q673L6; -.
DR ChEMBL; CHEMBL3108654; -.
DR PaxDb; Q673L6; -.
DR PRIDE; Q673L6; -.
DR Ensembl; ENSRNOT00000022683; ENSRNOP00000022683; ENSRNOG00000025327. [Q673L6-3]
DR Ensembl; ENSRNOT00000100559; ENSRNOP00000076971; ENSRNOG00000025327. [Q673L6-1]
DR GeneID; 301965; -.
DR KEGG; rno:301965; -.
DR UCSC; RGD:70494; rat. [Q673L6-1]
DR CTD; 7015; -.
DR RGD; 70494; Tert.
DR eggNOG; KOG1005; Eukaryota.
DR GeneTree; ENSGT00390000018531; -.
DR HOGENOM; CLU_001996_2_0_1; -.
DR InParanoid; Q673L6; -.
DR OMA; FWLMDTY; -.
DR OrthoDB; 1297956at2759; -.
DR PhylomeDB; Q673L6; -.
DR TreeFam; TF329048; -.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR PRO; PR:Q673L6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000025327; Expressed in liver and 15 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0031379; C:RNA-directed RNA polymerase complex; ISO:RGD.
DR GO; GO:0000333; C:telomerase catalytic core complex; ISO:RGD.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:1990572; C:TERT-RMRP complex; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; ISO:RGD.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; ISO:RGD.
DR GO; GO:0003720; F:telomerase activity; ISS:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; ISO:RGD.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0098680; F:template-free RNA nucleotidyltransferase; ISO:RGD.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071897; P:DNA biosynthetic process; ISO:RGD.
DR GO; GO:0022616; P:DNA strand elongation; ISO:RGD.
DR GO; GO:0062103; P:double-stranded RNA biosynthetic process; ISO:RGD.
DR GO; GO:0070200; P:establishment of protein localization to telomere; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:RGD.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:RGD.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:1903704; P:negative regulation of siRNA production; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:RGD.
DR GO; GO:0042635; P:positive regulation of hair cycle; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISO:RGD.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:RGD.
DR GO; GO:1903620; P:positive regulation of transdifferentiation; IMP:RGD.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0090399; P:replicative senescence; ISO:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0006278; P:RNA-templated DNA biosynthetic process; ISO:RGD.
DR GO; GO:0030422; P:siRNA processing; ISO:RGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
DR GO; GO:0001172; P:transcription, RNA-templated; ISO:RGD.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR021891; Telomerase_RBD.
DR InterPro; IPR003545; Telomerase_RT.
DR PANTHER; PTHR12066; PTHR12066; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF12009; Telomerase_RBD; 1.
DR PRINTS; PR01365; TELOMERASERT.
DR SMART; SM00975; Telomerase_RBD; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromosome; Cytoplasm; DNA-binding; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-directed DNA polymerase;
KW Telomere; Transferase; Ubl conjugation.
FT CHAIN 1..1125
FT /note="Telomerase reverse transcriptase"
FT /id="PRO_0000245165"
FT DOMAIN 595..928
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 1..239
FT /note="RNA-interacting domain 1"
FT /evidence="ECO:0000250"
FT REGION 58..205
FT /note="GQ motif"
FT /evidence="ECO:0000250"
FT REGION 137..141
FT /note="Required for regulating specificity for telomeric
FT DNA and for processivity for primer elongation"
FT /evidence="ECO:0000250"
FT REGION 206..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..328
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 306..528
FT /note="Required for oligomerization"
FT /evidence="ECO:0000250"
FT REGION 329..540
FT /note="RNA-interacting domain 2"
FT /evidence="ECO:0000250"
FT REGION 381..511
FT /note="QFP motif"
FT /evidence="ECO:0000250"
FT REGION 402..422
FT /note="CP motif"
FT /evidence="ECO:0000250"
FT REGION 907..921
FT /note="Required for oligomerization"
FT /evidence="ECO:0000250"
FT REGION 923..927
FT /note="Primer grip sequence"
FT /evidence="ECO:0000250"
FT REGION 929..1125
FT /note="CTE"
FT /evidence="ECO:0000250"
FT MOTIF 332..337
FT /note="TFLY; involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q4KTA7"
FT COMPBIAS 230..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 861
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 862
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT SITE 169
FT /note="Required for optimal binding of telomeric ssDNA and
FT incorporation of nucleotides at the second position of the
FT template"
FT /evidence="ECO:0000250"
FT SITE 860
FT /note="Required for nucleotide incorporation and primer
FT extension rate"
FT /evidence="ECO:0000250"
FT MOD_RES 447
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:O14746"
FT MOD_RES 697
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:O14746"
FT VAR_SEQ 515..615
FT /note="EKDTVPAAEHRLRERILAMFLFWLMDTYVVQLLRSFFYITETTFQKNRLFFY
FT RKSVWSKLQSIGIRQQLERVQLRELSQEEVKHHQDTWLAMPICRLRFIP -> ACTSFW
FT DSPSPSQVSFIFITAGKPSFPWIRRPLRYLETHRVELTHPAWQEGHCPCRRAPSEGEDP
FT CHVPVLANGHICGTAAEVILLHHRDHVPEEPPFLLP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16454671"
FT /id="VSP_052081"
FT VAR_SEQ 616..1125
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16454671"
FT /id="VSP_052082"
FT VAR_SEQ 641..646
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16454671"
FT /id="VSP_052083"
FT CONFLICT 521
FT /note="A -> V (in Ref. 2; DAA01427)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="E -> V (in Ref. 2; DAA01427)"
FT /evidence="ECO:0000305"
FT CONFLICT 550..551
FT /note="FF -> LL (in Ref. 2; DAA01427)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="L -> P (in Ref. 2; DAA01427)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="M -> L (in Ref. 2; DAA01427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1125 AA; 126934 MW; B8B2A11C914372DF CRC64;
MPRAPRCPAV RSLLRSRYRE VWPLATFVRR LGLEGSRLVQ PGDPKVFRTL VAQCLVCVPW
GSQPPPADLS FHQVSSLKEL VSRVVQKLCE RGERNVLAFG FALLNGARGG PPMAFTTSVH
SYLPNSVTES LCVSGAWMLL LSRVGDDLLV YLLSHCALYL LVPPSCAYQV CGSPLYQICA
TTDTWSSVPA GYRPTRPVGG NFTNLGSAHQ IKNSGHQEAP KPQALPSRGT KRLLSLTSTN
VPSAKKARFE PALRVDKGPH RQVVPTPSGK TWAPSPAASP KVPPAAKNLS LKGKASDPSL
SGSVCCKHKP SSSSLLSSPP QDAEKLRPFT ETRHFLYSRG GGQEELNPSF LLNSLPPSLT
GARRLVEIIF LGSRPRTSGP FCRTRRLPRR YWQMRPLFQQ LLMNHAKCQY VRFLRSHCRF
RTANQRVPDA MDTSPSHLTS LLRLHSSPWQ VYGFLRACLR ELVPAGLWGT RHNERRFLKN
VKKFISLGKY AKLSLQELMW RVKVEDCHWL RSSPEKDTVP AAEHRLRERI LAMFLFWLMD
TYVVQLLRSF FYITETTFQK NRLFFYRKSV WSKLQSIGIR QQLERVQLRE LSQEEVKHHQ
DTWLAMPICR LRFIPKLNGL RPIVNMSYGM DTRAFGKKKQ TQCFTQSLKT LFSVLNYERT
KHPNLMGASV LGTSDSYRIW RTFVLRVRAL DQTPRMYFVK ADVTGAYDAI PQDKLVEIVA
NIIRRSESMY CIRQYAVVQK DSQGQVHKSF RRQVSTLSDL QPYMGQFTKH LQDSDASALR
NSVVIEQSIS MNETGSSLLH FFLRFVRHSV VKIDGRFYVQ CQGIPQGSSL STLLCSLCFG
DMENKLFAEV QQDGLLLRFV DDFLLVTPHL AHAKAFLSTL VHGVPEYGCM INLQKTVVNF
PVETGALGGA APHQLPAHCL FPWCGLLLDT RTLEVFCDYS GYGRTSIKMS LTFQGVSRAG
KTMRYKLLSV LRLKCHGLFL DLQVNSLQTV CINIYKIFLL QAYRFHACVI RLPFGQHVRK
NHAFFLGIIS NLASCCYAIL KVKNPGVSLR AKGAPGSFPP EATRWLCYQA FLLKLAAHSV
TYKCLLGPLR TAQKQLCRKL PEATMTLLKT AADPALSTDF QTILD
