TERT_ARATH
ID TERT_ARATH Reviewed; 1123 AA.
AC Q9SPU7; Q9SE99;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Telomerase reverse transcriptase;
DE Short=AtTERT;
DE EC=2.7.7.49;
GN Name=TERT; OrderedLocusNames=At5g16850; ORFNames=F5E19.190;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10471830; DOI=10.1016/s0014-5793(99)01083-2;
RA Oguchi K., Liu H., Tamura K., Takahashi H.;
RT "Molecular cloning and characterization of AtTERT, a telomerase reverse
RT transcriptase homolog in Arabidopsis thaliana.";
RL FEBS Lett. 457:465-469(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10611295; DOI=10.1073/pnas.96.26.14813;
RA Fitzgerald M.S., Riha K., Gao F., Ren S., McKnight T.D., Shippen D.E.;
RT "Disruption of the telomerase catalytic subunit gene from Arabidopsis
RT inactivates telomerase and leads to a slow loss of telomeric DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14813-14818(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP FUNCTION.
RX PubMed=11359612; DOI=10.1046/j.1365-313x.2001.01010.x;
RA Fitzgerald M.S., Shakirov E.V., Hood E.E., McKnight T.D., Shippen D.E.;
RT "Different modes of de novo telomere formation by plant telomerases.";
RL Plant J. 26:77-87(2001).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14579127; DOI=10.1007/s00412-003-0251-7;
RA Siroky J., Zluvova J., Riha K., Shippen D.E., Vyskot B.;
RT "Rearrangements of ribosomal DNA clusters in late generation telomerase-
RT deficient Arabidopsis.";
RL Chromosoma 112:116-123(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17448460; DOI=10.1016/j.ydbio.2007.03.023;
RA Grafi G., Ben-Meir H., Avivi Y., Moshe M., Dahan Y., Zemach A.;
RT "Histone methylation controls telomerase-independent telomere lengthening
RT in cells undergoing dedifferentiation.";
RL Dev. Biol. 306:838-846(2007).
RN [8]
RP INTERACTION WITH POT1A.
RX PubMed=17911168; DOI=10.1242/jcs.004119;
RA Rossignol P., Collier S., Bush M., Shaw P., Doonan J.H.;
RT "Arabidopsis POT1A interacts with TERT-V(I8), an N-terminal splicing
RT variant of telomerase.";
RL J. Cell Sci. 120:3678-3687(2007).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18212040; DOI=10.1128/mcb.01490-07;
RA Kannan K., Nelson A.D., Shippen D.E.;
RT "Dyskerin is a component of the Arabidopsis telomerase RNP required for
RT telomere maintenance.";
RL Mol. Cell. Biol. 28:2332-2341(2008).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=18239859; DOI=10.1007/s11103-008-9295-7;
RA Ruckova E., Friml J., Prochazkova Schrumpfova P., Fajkus J.;
RT "Role of alternative telomere lengthening unmasked in telomerase knock-out
RT mutant plants.";
RL Plant Mol. Biol. 66:637-646(2008).
CC -!- FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the
CC replication of chromosome termini in most eukaryotes. It elongates
CC telomeres. It is a reverse transcriptase that adds simple sequence
CC repeats to chromosome ends by copying a template sequence within the
CC RNA component of the enzyme. Required to prevent genome instability
CC induced by breakage-fusion-bridge (BFB) cycles. Can extend completely
CC non-telomeric sequences using RNA template in vitro.
CC {ECO:0000269|PubMed:10471830, ECO:0000269|PubMed:10611295,
CC ECO:0000269|PubMed:11359612, ECO:0000269|PubMed:14579127}.
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: Component of the telomerase ribonucleoprotein complex
CC (Probable). Interacts with POT1A. {ECO:0000269|PubMed:17911168,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q9SPU7; Q56Y52: POT1A; NbExp=4; IntAct=EBI-1606133, EBI-1606062;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18212040}.
CC Chromosome, telomere {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Low rates of telomere shortening at each
CC generation. Null mutant plants can survive up to 10 generations before
CC dying. Accelerated proliferation and cell death in dedifferentiated
CC cells. {ECO:0000269|PubMed:10611295, ECO:0000269|PubMed:14579127,
CC ECO:0000269|PubMed:17448460, ECO:0000269|PubMed:18239859}.
CC -!- MISCELLANEOUS: In the absence of telomerase, telomeres decline by
CC approximately 500 bp per generation, a rate 10 times slower than seen
CC in telomerase-deficient mice. This may be due to alternative telomere
CC lengthening, a process which is activated in early embryonic
CC development.
CC -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC subfamily. {ECO:0000305}.
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DR EMBL; AF135454; AAD54777.1; -; mRNA.
DR EMBL; AF172097; AAD54276.1; -; Genomic_DNA.
DR EMBL; AL391147; CAC01849.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92349.1; -; Genomic_DNA.
DR PIR; T51517; T51517.
DR RefSeq; NP_197187.1; NM_121691.4.
DR AlphaFoldDB; Q9SPU7; -.
DR SMR; Q9SPU7; -.
DR BioGRID; 16824; 68.
DR IntAct; Q9SPU7; 1.
DR STRING; 3702.AT5G16850.1; -.
DR PaxDb; Q9SPU7; -.
DR PRIDE; Q9SPU7; -.
DR EnsemblPlants; AT5G16850.1; AT5G16850.1; AT5G16850.
DR GeneID; 831548; -.
DR Gramene; AT5G16850.1; AT5G16850.1; AT5G16850.
DR KEGG; ath:AT5G16850; -.
DR Araport; AT5G16850; -.
DR TAIR; locus:2148975; AT5G16850.
DR eggNOG; KOG1005; Eukaryota.
DR HOGENOM; CLU_001996_1_0_1; -.
DR InParanoid; Q9SPU7; -.
DR OMA; GHISSTF; -.
DR OrthoDB; 1297956at2759; -.
DR PhylomeDB; Q9SPU7; -.
DR PRO; PR:Q9SPU7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SPU7; baseline and differential.
DR Genevisible; Q9SPU7; AT.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000333; C:telomerase catalytic core complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003720; F:telomerase activity; IDA:TAIR.
DR GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IDA:TAIR.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:TAIR.
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; 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 1: Evidence at protein level;
KW Chromosome; DNA-binding; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Reference proteome; RNA-directed DNA polymerase; Telomere;
KW Transferase.
FT CHAIN 1..1123
FT /note="Telomerase reverse transcriptase"
FT /id="PRO_0000412607"
FT DOMAIN 596..929
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 191..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 691
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 860
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 CONFLICT 1107
FT /note="R -> K (in Ref. 2; AAD54276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1123 AA; 130580 MW; 5645B8295817B7F6 CRC64;
MPRKPRHRVP EILWRLFGNR ARNLNDAIVD LIPNRNIQPE QCRCRGQGCL GCSSDKPAFL
LRSDDPIHYR KLLHRCFVVL HEQTPPLLDF SPTSWWSQRE IVERIIEMMQ SGCDCQNVIC
ARYDKYDQSS PILELLTSSS WEFLLKRVGH DVMVYLLQQT SIFLPLLGKK HQQVSGPPLC
IKHKRTLSVH ENKRKRDDNV QPPTKRQWLS SAVDDCPKDD SATITPIVGE DVDQHREKKT
TKRSRIYLKR RRKQRKVNFK KVDCNAPCIT PSTNGKVSTG NDEMNLHIGI NGSLTDFVKQ
AKQVKRNKNF KFGLSETYSV IPPNHILKTL RPNCSDSKLL MNHIFGEVNV WSTTPSHGKG
NCPSGSICLY HSLLKSLKNL IGKTKSSHLK MLLDKHCPVL LLQEDALKSG TTSQSSRRQK
ADKLPHGSSS SQTGKPKCPS VEERKLYCTN DQVVSFIWAI CRYIVPESLL GTTHQMRVLR
KNIAWFVSRR RNEKCTVNQF LHKVKPSDFP FFARKELCCM VNGHELQSES IRSTQQMLCT
KWISWLFLEI VKKLVHFNFY ATESQGGRLN IYYYRKRSWE RLISKEISKA LDGYVLVDDA
EAESSRKKLS KFRFLPKANG VRMVLDFSSS SRSQSLRDTH AVLKDIQLKE PDVLGSSVFD
HDDFYRNLCP YLIHLRSQSG ELPPLYFVVA DVFKAFDSVD QGKLLHVIQS FLKDEYILNR
CRLVCCGKRS NWVNKILVSS DKNSNFSRFT STVPYNALQS IVVDKGENHR VRKKDLMVWI
GNMLKNNMLQ LDKSFYVQIA GIPQGHRLSS LLCCFYYGHL ERTLIYPFLE EASKDVSSKE
CSREEELIIP TSYKLLRFID DYLFVSTSRD QASSFYHRLK HGFKDYNCFM NETKFCINFE
DKEEHRCSSN RMFVGDNGVP FVRWTGLLIN SRTFEVQVDY TRYLSGHISS TFSVAWQNKP
VRNLRQKLCY FLVPKCHPIL FDSNINSGEI VRLNIYQIFL LAAMKFHCYV YEVSRFWKLH
PQTLFKFITI SVRYMFRLIN RRVRRINTGS SFRPVLKLYK EEVIWLGLDA YIQVLKKKNS
RYRMLLIYLK SALSKHSLSQ QLSSELRYAT DRSNSSSLWK LNY
