TELO2_DANRE
ID TELO2_DANRE Reviewed; 822 AA.
AC Q7T006; A0JMI8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Telomere length regulation protein TEL2 homolog;
GN Name=telo2; ORFNames=si:ch211-153c20.2, zgc:153824;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=WIK; TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT
CC complex that is required to stabilize protein levels of the
CC phosphatidylinositol 3-kinase-related protein kinase (PIKK) family
CC proteins. Promotes assembly, stabilizes and maintains the activity of
CC TORC complexes, which regulate cell growth and survival in response to
CC nutrient and hormonal signals. May be involved in telomere length
CC regulation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TEL2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE30387.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL772148; CAE30387.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC125895; AAI25896.1; -; mRNA.
DR RefSeq; NP_001071209.1; NM_001077741.1.
DR AlphaFoldDB; Q7T006; -.
DR SMR; Q7T006; -.
DR STRING; 7955.ENSDARP00000114983; -.
DR PaxDb; Q7T006; -.
DR PRIDE; Q7T006; -.
DR GeneID; 777634; -.
DR KEGG; dre:777634; -.
DR CTD; 9894; -.
DR ZFIN; ZDB-GENE-061103-523; telo2.
DR eggNOG; KOG4346; Eukaryota.
DR InParanoid; Q7T006; -.
DR OrthoDB; 355610at2759; -.
DR PhylomeDB; Q7T006; -.
DR TreeFam; TF313925; -.
DR PRO; PR:Q7T006; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070209; C:ASTRA complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR Gene3D; 1.25.40.720; -; 2.
DR InterPro; IPR038528; TEL2_C_sf.
DR InterPro; IPR019337; Telomere_length_regulation_dom.
DR Pfam; PF10193; Telomere_reg-2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..822
FT /note="Telomere length regulation protein TEL2 homolog"
FT /id="PRO_0000318517"
FT REGION 442..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 19
FT /note="K -> R (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..138
FT /note="VS -> AG (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> S (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="F -> S (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="M -> L (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="N -> H (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..466
FT /note="PVS -> SVL (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="R -> C (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="V -> L (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="V -> L (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="F -> L (in Ref. 2; AAI25896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 822 AA; 91669 MW; 5B1F5CBC37CF4959 CRC64;
MGTFGTESPL RLQVSSCLKT LSTSRDSGEI VHALRTLMRC LDDGEFTRIH HTHALQVLVS
AQSSHWFSRS HDEDEEEMKK LWGEIIIRGP AEQTLLTLLD TISSTGESEA LDRCVSALEM
FLSAARLQVL LWSRCEVSGA SADSPQLTET VIGHLAALPS ITSNHLHTNT PDIFLPQQYY
PLLAASILDT LEKTCHALRA GRDCSLGFVS QVLGKVCIQG YSSQMFETLG PRLSFVTRED
ALYQRVTQKL MENVPERCTE SVITGLIRSL SGAAAVSRLM GNLVLTNKKA QFVLTHKLIL
QQYQHPTRLL KSVLGYLAVD SSRRPLLKQV LRSVCQVWCN SSAVKHTCVE QQLYVSKALL
LCVALLDDSE IQELRQEMLQ CMLGGVQCRL DSNVERIRRM GMVVGECLSH RLDTPGSQLK
FQYGADEEIG ELKSLMESLA VNDDEEEQPD ASNSLQPEPK VEAPVSSQSV ASDPGNGSES
ELDSDDDLTP YDMSADQEKK KSAPPRYVRD CLEGLMSSDD AERFELSLQV AETLLRKNVK
ATQEVSVQFS KVLLHLEDRY NTALFLSLRQ NAMVALTVTD IKPVVDYWTT EFYALNYSLR
QRLDILEVLA LAAQELSEPV TNKHTGAEPI TAVTPLGQSD DITHWRQIVD KRIQSKTRRI
SKGVTQPVKA VPNRYAPVAG FFFFPLFRSY DRPQTTFDLL GGDHLVLGRL LHTLGLLMHL
AVNAPVVSQM GRALLDFVWA VRFHTDQMVR RGVMFAVCAV FLSMPSENLL TELGDDLMET
RAWLADVAES DCDSDCRSLA VQSLMLMDKN LKSQLQIPDM ET
