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Database: UniProt
Entry: G1PKR5_MYOLU
LinkDB: G1PKR5_MYOLU
Original site: G1PKR5_MYOLU 
ID   G1PKR5_MYOLU            Unreviewed;      1096 AA.
AC   G1PKR5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Telomerase reverse transcriptase {ECO:0000256|ARBA:ARBA00016182, ECO:0000256|RuleBase:RU365061};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493, ECO:0000256|RuleBase:RU365061};
DE   AltName: Full=Telomerase catalytic subunit {ECO:0000256|ARBA:ARBA00032044, ECO:0000256|RuleBase:RU365061};
GN   Name=TERT {ECO:0000313|Ensembl:ENSMLUP00000011412.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000011412.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000011412.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000011412.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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.
CC       {ECO:0000256|RuleBase:RU365061}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00024557,
CC         ECO:0000256|RuleBase:RU365061};
CC   -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC       {ECO:0000256|ARBA:ARBA00004574, ECO:0000256|RuleBase:RU365061}.
CC       Nucleus, nucleolus {ECO:0000256|RuleBase:RU365061}. Nucleus,
CC       nucleoplasm {ECO:0000256|RuleBase:RU365061}. Nucleus
CC       {ECO:0000256|RuleBase:RU365061}. Cytoplasm
CC       {ECO:0000256|RuleBase:RU365061}. Nucleus, PML body
CC       {ECO:0000256|RuleBase:RU365061}. 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. Dephosphorylation at this site
CC       by SHP2 retains TERT in the nucleus. Translocated to the nucleus by
CC       phosphorylation by AKT. {ECO:0000256|RuleBase:RU365061}.
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. {ECO:0000256|RuleBase:RU365061}.
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:0000256|RuleBase:RU365061}.
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:0000256|RuleBase:RU365061}.
CC   -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC       subfamily. {ECO:0000256|ARBA:ARBA00008001,
CC       ECO:0000256|RuleBase:RU365061}.
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DR   EMBL; AAPE02000919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02000920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02000921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1PKR5; -.
DR   STRING; 59463.ENSMLUP00000011412; -.
DR   Ensembl; ENSMLUT00000012542.2; ENSMLUP00000011412.2; ENSMLUG00000012533.2.
DR   eggNOG; KOG1005; Eukaryota.
DR   GeneTree; ENSGT00390000018531; -.
DR   HOGENOM; CLU_001996_2_0_1; -.
DR   InParanoid; G1PKR5; -.
DR   OMA; LAAMKFH; -.
DR   TreeFam; TF329048; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0000333; C:telomerase catalytic core complex; IEA:Ensembl.
DR   GO; GO:1990572; C:TERT-RMRP complex; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:Ensembl.
DR   GO; GO:0070034; F:telomerase RNA binding; IEA:Ensembl.
DR   GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IEA:Ensembl.
DR   GO; GO:0098680; F:template-free RNA nucleotidyltransferase; IEA:Ensembl.
DR   GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR   GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0022616; P:DNA strand elongation; IEA:Ensembl.
DR   GO; GO:0070200; P:establishment of protein localization to telomere; IEA:Ensembl.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR   GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
DR   GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0042635; P:positive regulation of hair cycle; IEA:Ensembl.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR   GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IEA:Ensembl.
DR   GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR   GO; GO:0090399; P:replicative senescence; IEA:Ensembl.
DR   GO; GO:0030422; P:siRNA processing; IEA:Ensembl.
DR   GO; GO:0140745; P:siRNA transcription; IEA:Ensembl.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IEA:Ensembl.
DR   CDD; cd01648; TERT; 1.
DR   Gene3D; 1.10.132.70; -; 1.
DR   Gene3D; 1.10.357.90; -; 1.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR021891; Telomerase_RBD.
DR   InterPro; IPR003545; Telomerase_RT.
DR   InterPro; IPR049139; TERT_C.
DR   PANTHER; PTHR12066; TELOMERASE REVERSE TRANSCRIPTASE; 1.
DR   PANTHER; PTHR12066:SF0; TELOMERASE REVERSE TRANSCRIPTASE; 1.
DR   Pfam; PF12009; Telomerase_RBD; 1.
DR   Pfam; PF21399; TERT_C; 1.
DR   PRINTS; PR01365; TELOMERASERT.
DR   SMART; SM00975; Telomerase_RBD; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU365061};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU365061};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365061};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU365061};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365061};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   RNA-directed DNA polymerase {ECO:0000256|RuleBase:RU365061};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365061};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
FT   DOMAIN          568..880
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          190..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1096 AA;  122650 MW;  36E957C8EE76D704 CRC64;
     MPRAPRCRAV RALLRGHYRE VLPLDTFVRR LGPQGRCLVQ PGDPMAFRAL VTQCLVCVPW
     DAQPLPVAPD FRQVSCLKEL VARVVQRLCE RGARNVLAFG FALLDGARGG PPMAFTTNVR
     SYLPNTVTET LRGSGAWGLL LRRVGDDVLT HLLARCALYL LVPPNCAYQV CGPPLYDLCT
     PRHAGGSLTR LGPTRQAWNG GGGGEAGVPL GCRRRPRRSS AGGSPPQAKR PRHGPISEPY
     RGPSASGPRV VTPTKAAAEA SPGEGEPRRP RRPLPLLGRE REAGCPSSRP SHPQAAPGPR
     VVAETKQFLY CSGGRERLRS SFLLNSLQPS LTGAQRLVET IFLDSKPLQR GTPRRTRRLP
     TRYWRMRPLF QELLGNHARC PYGALLREHC PLRDSATPAT PAAEDTGPPR LVQLLRQHSS
     PKHVYGLLRA CLRRLVPARL WGSRHNERRF LKNVKKFISL GKFAKLLSQE LTWKMKVQDC
     AWLSQSPGGR CVPATEHRLR EAVLTKFLCW LMGTYVVELL KSFFYVTETT FQKNQLFFFR
     KSIWSQLQSI GIRQHFDRVQ LRELSVAEVK RYQEARPALL TSRLRFLPKP SGLRPIVNMD
     YVVGARTFHG DKKVQHLTSK VKTLFSVLNY EREQRPGLLG ASVLGMDDIY RAWRAFVLRM
     RAQDPVPQLY FVKVDVMGAY DALPQDRLVE VIANVIQPQE HTYCLRQYAV VQRTARGRVR
     KSFKRHVSTF TDLQPYMKQF VQQLQKSSLR DAVVIEQSCS LNEASSDLFD VFLHLVYNHI
     VRIGGKFYIQ CQGIPQGSIL STLLCSLCYG DMESRVFPGL QQDGVLLRLV DDFLLVTPHL
     TQAKAFLRTL SRGVPEYGCK ELAKTVVNFS QKVRGLGAIS PSRVGACHSC VGQGTGQVLL
     DTRLFADVMC CSYAQTSIRA SLAFSQGSKP GRSMRRKLFA VLRLKCHSLL LDLQVNGLQT
     VCTNVYKIFL LQAYRFHACV LQLPFNQHVR KNPSFFLRVI SDTASRCHTL LKAKNPGMPL
     GTKGAAGPFP SEAARWLCFH AFLLKLSRHS ATYRCLLGAL QTAQAQLCRQ LPRATLATLE
     AAADPALTTD FRTILD
//
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