ID   TLS1_PONAB              Reviewed;         289 AA.
AC   Q5RC87;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Telomere length and silencing protein 1 homolog {ECO:0000250|UniProtKB:Q10148};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the regulation of telomeric heterochromatin
CC       assembly and control of telomere length.
CC       {ECO:0000250|UniProtKB:Q10148}.
CC   -!- SIMILARITY: Belongs to the TLS1 family.
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DR   EMBL; CR858393; CAH90620.1; -; mRNA.
DR   RefSeq; NP_001125335.1; NM_001131863.1.
DR   AlphaFoldDB; Q5RC87; -.
DR   STRING; 9601.ENSPPYP00000022064; -.
DR   GeneID; 100172237; -.
DR   KEGG; pon:100172237; -.
DR   CTD; 101170595; -.
DR   eggNOG; KOG3345; Eukaryota.
DR   OrthoDB; 1493869at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   InterPro; IPR010756; Tls1.
DR   PANTHER; PTHR13486; PTHR13486; 1.
DR   Pfam; PF07052; Hep_59; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..289
FT                   /note="Telomere length and silencing protein 1 homolog"
FT                   /id="PRO_0000227525"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ63"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ63"
FT   MOD_RES         147
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ63"
FT   MOD_RES         253
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ63"
FT   MOD_RES         261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ63"
SQ   SEQUENCE   289 AA;  33703 MW;  FD34A8B67A737F25 CRC64;
     MPVVRKIFRR RRGDSESEED EQDSEEVRLK LEETREVQNL RKRPNGVSAV ALLVGEKVQE
     ETTLVDDPFQ MKTGGMVDMK KLKERGKDKI SEEEDLHLGT SFSAETNRRD EDADMMKYIE
     TELKKRKGIV EHEEQKVKPK NAEDCLYELP ENIRVSSAKK TEEMLSNQML SGIPEVDQGI
     DAKIKNIIST EDAKARLLAE QQNKKKDSET SFVPTNMAVN YVQHNRFYHE ELNAPIRRNK
     EEPKARPLRV GDTEKPEPER SPPNRKRPAN EKATDDYHYE KFKKMNRRY