TERT_TAKRU
ID TERT_TAKRU Reviewed; 1074 AA.
AC Q4KTA7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Telomerase reverse transcriptase {ECO:0000303|PubMed:15961261};
DE EC=2.7.7.49 {ECO:0000269|PubMed:18039659, ECO:0000269|PubMed:24055314};
DE AltName: Full=Telomerase catalytic subunit {ECO:0000305};
GN Name=tert {ECO:0000312|EMBL:AAX59693.1};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000312|EMBL:AAX59693.1};
RN [1] {ECO:0000312|EMBL:AAX59693.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Gill {ECO:0000303|PubMed:15961261}, and
RC Testis {ECO:0000303|PubMed:15961261};
RX PubMed=15961261; DOI=10.1016/j.gene.2005.04.038;
RA Yap W.H., Yeoh E., Brenner S., Venkatesh B.;
RT "Cloning and expression of the reverse transcriptase component of
RT pufferfish (Fugu rubripes) telomerase.";
RL Gene 353:207-217(2005).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND RECONSTITUTION OF THE TELOMERASE
RP HOLOENZYME COMPLEX.
RX PubMed=18039659; DOI=10.1074/jbc.m708032200;
RA Xie M., Mosig A., Qi X., Li Y., Stadler P.F., Chen J.J.;
RT "Structure and function of the smallest vertebrate telomerase RNA from
RT teleost fish.";
RL J. Biol. Chem. 283:2049-2059(2008).
RN [3] {ECO:0007744|PDB:4LMO}
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 294-544, CATALYTIC ACTIVITY,
RP RECONSTITUTION OF THE TELOMERASE HOLOENZYME COMPLEX, SUBUNIT, AND
RP MUTAGENESIS OF 300-THR--TYR-305; TYR-305; TYR-512; THR-514 AND GLU-515.
RX PubMed=24055314; DOI=10.1016/j.str.2013.08.013;
RA Harkisheimer M., Mason M., Shuvaeva E., Skordalakes E.;
RT "A motif in the vertebrate telomerase N-terminal linker of TERT contributes
RT to RNA binding and telomerase activity and processivity.";
RL Structure 21:1870-1878(2013).
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. {ECO:0000269|PubMed:18039659,
CC ECO:0000269|PubMed:24055314}.
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, ECO:0000269|PubMed:18039659,
CC ECO:0000269|PubMed:24055314};
CC -!- SUBUNIT: Catalytic subunit of the telomerase holoenzyme complex
CC composed minimally of TERT and the telomerase RNA template component
CC (TERC). {ECO:0000269|PubMed:18039659, ECO:0000269|PubMed:24055314}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14746}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:O14746}.
CC -!- TISSUE SPECIFICITY: Detected at highest levels in gill, ovary and
CC testis, and at lower levels in brain, eye, heart, skin, spleen and
CC stomach. {ECO:0000269|PubMed:15961261}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher levels in actively dividing
CC cells. {ECO:0000269|PubMed:15961261}.
CC -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC subfamily. {ECO:0000305}.
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DR EMBL; AY861384; AAX59693.1; -; Genomic_DNA.
DR PDB; 4LMO; X-ray; 2.37 A; A/B/C/D=294-544.
DR PDBsum; 4LMO; -.
DR AlphaFoldDB; Q4KTA7; -.
DR SMR; Q4KTA7; -.
DR STRING; 31033.ENSTRUP00000036305; -.
DR eggNOG; KOG1005; Eukaryota.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000333; C:telomerase catalytic core complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:UniProtKB.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IDA:UniProtKB.
DR GO; GO:0022616; P:DNA strand elongation; IDA:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Chromosome; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW RNA-directed DNA polymerase; Telomere; Transferase.
FT CHAIN 1..1074
FT /note="Telomerase reverse transcriptase"
FT /id="PRO_0000433392"
FT DOMAIN 552..877
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 240..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..360
FT /note="Interaction with RNA template"
FT /evidence="ECO:0000250|UniProtKB:Q1PS67"
FT REGION 461..486
FT /note="Interaction with RNA template"
FT /evidence="ECO:0000250|UniProtKB:Q1PS67"
FT MOTIF 300..305
FT /note="TFLY; involved in RNA binding"
FT /evidence="ECO:0000269|PubMed:24055314"
FT COMPBIAS 248..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 649
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 810
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 811
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT MUTAGEN 300..305
FT /note="Missing: Reduced RNA template binding."
FT /evidence="ECO:0000269|PubMed:24055314"
FT MUTAGEN 305
FT /note="Y->A: Reduced RNA template binding and moderately
FT impaired telomerase activity."
FT /evidence="ECO:0000269|PubMed:24055314"
FT MUTAGEN 512
FT /note="Y->A: Reduced RNA template binding and strongly
FT impaired telomerase activity."
FT /evidence="ECO:0000269|PubMed:24055314"
FT MUTAGEN 514
FT /note="T->A: Reduced RNA template binding and strongly
FT impaired telomerase activity."
FT /evidence="ECO:0000269|PubMed:24055314"
FT MUTAGEN 515
FT /note="E->A: Reduced RNA template binding and strongly
FT impaired telomerase activity."
FT /evidence="ECO:0000269|PubMed:24055314"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:4LMO"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 363..375
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:4LMO"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 432..448
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 481..500
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 502..510
FT /evidence="ECO:0007829|PDB:4LMO"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:4LMO"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:4LMO"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:4LMO"
FT HELIX 528..541
FT /evidence="ECO:0007829|PDB:4LMO"
SQ SEQUENCE 1074 AA; 122505 MW; 7F88945ADC76C36D CRC64;
MSITDLSPTL GILRSLYPHV QVLVDFADDI VFREGHKATL IEESDTSHFK SFVRGIFVCF
HKELQQVPSC NQICTLPELL AFVLNSVKRK RKRNVLAHGY NFQSLAQEER DADQFKLQGD
VTQSAAYVHG SDLWRKVSMR LGTDITRYLF ESCSVFVAVP PSCLFQVCGI PIYDCFSLAT
ASLGFSLQSR GCRERCLGVN SMKRRAFNVK RYLRKRKTET DQKDEARVCS GKRRRVMEED
KVSCETMQDG ESGKTTLVQK QPGSKKRSEM EATLLPLEGG PSWRSGTFPP LPPSQSFMRT
LGFLYGGRGM RSFLLNRKKK TAEGFRKIQG RDLIRIVFFE GVLYLNGLER KPKKLPRRFF
NMVPLFSQLL RQHRRCPYSR LLQKTCPLVG IKDAGQAELS SFLPQHCGSH RVYLFVRECL
LAVIPQELWG SEHNRLLYFA RVRFFLRSGK FERLSVAELM WKIKVNNCDW LKISKTGRVP
PSELSYRTQI LGQFLAWLLD GFVVGLVRAC FYATESMGQK NAIRFYRQEV WAKLQDLAFR
SHISKGQMVE LTPDQVAALP KSTIISRLRF IPKTDGMRPI TRVIGADAKT RLYQSHVRDL
LDMLRACVCS TPSLLGSTVW GMTDIHKVLS SIAPAQKEKP QPLYFVKMDV SGAYESLPHN
KLIEVINQVL TPVLNEVFTI RRFAKIWADS HEGLKKAFIR QADFLEANMG SINMKQFLTS
LQKKGKLHHS VLVEQIFSSD LEGKDALQFF TQILKGSVIQ FGKKTYRQCQ GVPQGSAVSS
VLCCLCYGHM ENVLFKDIIN KKSCLMRLVD DFLLITPNLH DAQTFLKILL AGVPQYGLVV
NPQKVVVNFE DYGSTDSCPG LRVLPLRCLF PWCGLLLDTH TLDIYKDYSS YADLSLRYSL
TLGSCHSAGH QMKRKLMGIL RLKCHALFLD LKTNSLEAIY KNIYKLLLLH ALRFHVCAQS
LPFGQSVAKN PAYFLLMIWD MVEYTNYLIR LSNNGLISGS TSQTGSVQYE AVELLFCLSF
LLVLSKHRRL YKDLLLHLHK RKRRLEQCLG DLRLARVRQA ANPRNPLDFL AIKT
