ID   POTE1_CHICK             Reviewed;         778 AA.
AC   P62597;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Protection of telomeres protein 1;
DE            Short=cPot1;
DE   AltName: Full=POT1-like telomere end-binding protein;
GN   Name=POT1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, SUBUNIT, AND
RP   SINGLE-STRANDED TELOMERE DNA-BINDING.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=14966288; DOI=10.1128/mcb.24.5.2091-2102.2004;
RA   Wei C., Price C.M.;
RT   "Cell cycle localization, dimerization, and binding domain architecture of
RT   the telomere protein cPot1.";
RL   Mol. Cell. Biol. 24:2091-2102(2004).
CC   -!- FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex
CC       that is essential for the replication of chromosome termini. Is a
CC       component of the double-stranded telomeric DNA-binding TRF1 complex
CC       that is involved in the regulation of telomere length by cis-inhibition
CC       of telomerase. Also acts as a single-stranded telomeric DNA-binding
CC       protein and thus may act as a downstream effector of the TRF1 complex
CC       and may transduce information about telomere maintenance and/or length
CC       to the telomere terminus. Binds to at least two telomeric single-
CC       stranded 5'-TTAGGG-3' repeats (G-strand). Its activity is TERT
CC       dependent but it does not increase TERT activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer or homooligomer. Component of the telomerase
CC       ribonucleoprotein complex. Binds single-stranded telomeric DNA as a
CC       monomer (By similarity). Found in a complex with TERF1, TINF2 and
CC       TNKS1. Interacts with TNKS1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NUX5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14966288}.
CC       Chromosome, telomere {ECO:0000269|PubMed:14966288}. Note=Colocalizes
CC       with telomeric DNA.
CC   -!- SIMILARITY: Belongs to the telombin family. {ECO:0000305}.
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DR   EMBL; AY555718; AAS64745.1; -; mRNA.
DR   RefSeq; NP_996875.1; NM_206992.1.
DR   AlphaFoldDB; P62597; -.
DR   SMR; P62597; -.
DR   STRING; 9031.ENSGALP00000030079; -.
DR   PaxDb; P62597; -.
DR   GeneID; 404538; -.
DR   KEGG; gga:404538; -.
DR   CTD; 25913; -.
DR   VEuPathDB; HostDB:geneid_404538; -.
DR   eggNOG; KOG4757; Eukaryota.
DR   InParanoid; P62597; -.
DR   OrthoDB; 940962at2759; -.
DR   PhylomeDB; P62597; -.
DR   Reactome; R-GGA-418124; Telomere maintenance.
DR   PRO; PR:P62597; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR   GO; GO:0000783; C:nuclear telomere cap complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0098505; F:G-rich strand telomeric DNA binding; IBA:GO_Central.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; ISS:UniProtKB.
DR   GO; GO:0010521; F:telomerase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0051974; P:negative regulation of telomerase activity; IBA:GO_Central.
DR   GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IBA:GO_Central.
DR   GO; GO:0016233; P:telomere capping; IBA:GO_Central.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
DR   Gene3D; 2.40.50.140; -; 2.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR028389; POT1.
DR   InterPro; IPR032042; POT1PC.
DR   InterPro; IPR011564; Telomer_end-bd_POT1/Cdc13.
DR   PANTHER; PTHR14513; PTHR14513; 1.
DR   Pfam; PF02765; POT1; 1.
DR   Pfam; PF16686; POT1PC; 1.
DR   SMART; SM00976; Telo_bind; 1.
DR   SUPFAM; SSF50249; SSF50249; 2.
PE   1: Evidence at protein level;
KW   Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere.
FT   CHAIN           1..778
FT                   /note="Protection of telomeres protein 1"
FT                   /id="PRO_0000121731"
SQ   SEQUENCE   778 AA;  87484 MW;  BD11397FAC6D0A53 CRC64;
     MPVQVLKIIK GKPETQLPSH LQREDLKHLQ TGLDHTNKYF QGIVILSYPL TKLGDGTDFF
     KIVLQDDTCS RINSINVLMY GKMAEDCAKL IRNGDTFIVA GFKVAESPTA REDGRHACHL
     QVSEESGSAI FICTQPSITP FSEATSPSVA PKYVYTPLNC LKDGTVVNLY GIVKFFKPPY
     ISKGTDYCSV VTLVDQSNVK LTCTLFNGNL DSLPKIYKNG DIVRFHRVKI REYNGQMQGI
     TSAGFASLTF DGTVGAPVVP RASSKVYTFV DEEQKTVEEL RIWAASNLSV SGPEAKLSDV
     KPMMFFDLTC QLVGKAKVDG SSFLLKVWDG TKCPYPTWKV PVEAKELEGD RVLLHHLRNL
     TVDVLVYDNH VQLAKSLKTG SFLRIYSIHT KQASAKNEDM SSHIEFHLHG GTCYGRGIGI
     LPENNPDVEE LKSFLECVEL TDSQNMESVS SLELGDTFDS YTDLESPLQR CQQLSATVLT
     DHQDMSNTVL KTVLNSSAPQ QYRIRAKLRS FKPQKLYQSV KLHCSKCNTL QEVPNGDAID
     FILQGCAATA PNPELQSMSW YESVVWTTEE DQGRKITIHF VKHYEMLQRP ENTLLMIEGG
     TLKEIWKLTR RFKCVIPVKS KEDDLELLDL SAPFLLQGNI KYYGCKKCST PKSIKNLSSL
     AEKREPSWEP TEIAQVLGIE PLQYVFVMKF TLVDGTGVLN AYLFDYEKFF QIPASEILTN
     SFLQQKMEMT MNTLSPPGRK LDDLPWLECF IKSYNVADGM KHQVYYQIFD TTVAEDVV