ID   POT1_SCHPO              Reviewed;         555 AA.
AC   O13988;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Protection of telomeres protein 1;
GN   Name=pot1; ORFNames=SPAC26H5.06;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION.
RX   PubMed=11349150; DOI=10.1126/science.1060036;
RA   Baumann P., Cech T.R.;
RT   "Pot1, the putative telomere end-binding protein in fission yeast and
RT   humans.";
RL   Science 292:1171-1175(2001).
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=12463756; DOI=10.1021/bi026674z;
RA   Lei M., Baumann P., Cech T.R.;
RT   "Cooperative binding of single-stranded telomeric DNA by the Pot1 protein
RT   of Schizosaccharomyces pombe.";
RL   Biochemistry 41:14560-14568(2002).
RN   [4]
RP   SELF-ASSOCIATION, AND SUBCELLULAR LOCATION.
RX   PubMed=17715303; DOI=10.1073/pnas.0705497104;
RA   Martin V., Du L.-L., Rozenzhak S., Russell P.;
RT   "Protection of telomeres by a conserved Stn1-Ten1 complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:14038-14043(2007).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCQ1; POZ1 AND TPZ1.
RX   PubMed=18535244; DOI=10.1126/science.1154819;
RA   Miyoshi T., Kanoh J., Saito M., Ishikawa F.;
RT   "Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere
RT   length.";
RL   Science 320:1341-1344(2008).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-185, AND TELOMERIC
RP   SINGLE-STRANDED DNA-BINDING.
RX   PubMed=14614509; DOI=10.1038/nature02092;
RA   Lei M., Podell E.R., Baumann P., Cech T.R.;
RT   "DNA self-recognition in the structure of Pot1 bound to telomeric single-
RT   stranded DNA.";
RL   Nature 426:198-203(2003).
CC   -!- FUNCTION: Single-stranded telomeric DNA-binding protein that is
CC       required to protect the 3'-end telomeric overhang. It binds the
CC       consensus sequence 5'-GGTTAC-3'. Regulates telomerase and telomere
CC       length. {ECO:0000269|PubMed:11349150, ECO:0000269|PubMed:12463756,
CC       ECO:0000269|PubMed:18535244}.
CC   -!- SUBUNIT: Self-associates. Interacts with ccq1, poz1 and tpz1.
CC       {ECO:0000269|PubMed:12463756, ECO:0000269|PubMed:18535244}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere.
CC   -!- SIMILARITY: Belongs to the telombin family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16192.2; -; Genomic_DNA.
DR   PIR; T38425; T38425.
DR   RefSeq; NP_594453.1; NM_001019882.2.
DR   PDB; 1QZG; X-ray; 1.90 A; A/B=2-185.
DR   PDB; 1QZH; X-ray; 2.40 A; A/B/C/D/E/F=2-185.
DR   PDB; 4HID; X-ray; 1.82 A; A=198-339.
DR   PDB; 4HIK; X-ray; 1.64 A; A=198-339.
DR   PDB; 4HIM; X-ray; 1.75 A; A=198-339.
DR   PDB; 4HIO; X-ray; 1.75 A; A=198-339.
DR   PDB; 4HJ5; X-ray; 2.04 A; A=198-339.
DR   PDB; 4HJ7; X-ray; 1.78 A; A=198-339.
DR   PDB; 4HJ8; X-ray; 2.04 A; A=198-339.
DR   PDB; 4HJ9; X-ray; 1.85 A; A=198-339.
DR   PDB; 4HJA; X-ray; 2.10 A; A=198-339.
DR   PDB; 5USB; X-ray; 1.61 A; A=200-337.
DR   PDB; 5USN; X-ray; 1.90 A; A=200-339.
DR   PDB; 5USO; X-ray; 2.00 A; A=200-337.
DR   PDB; 6BWY; X-ray; 2.90 A; A/B/E/G=5-174.
DR   PDB; 7CUH; X-ray; 3.00 A; A=1-339.
DR   PDB; 7CUI; X-ray; 2.60 A; A/C=357-555.
DR   PDBsum; 1QZG; -.
DR   PDBsum; 1QZH; -.
DR   PDBsum; 4HID; -.
DR   PDBsum; 4HIK; -.
DR   PDBsum; 4HIM; -.
DR   PDBsum; 4HIO; -.
DR   PDBsum; 4HJ5; -.
DR   PDBsum; 4HJ7; -.
DR   PDBsum; 4HJ8; -.
DR   PDBsum; 4HJ9; -.
DR   PDBsum; 4HJA; -.
DR   PDBsum; 5USB; -.
DR   PDBsum; 5USN; -.
DR   PDBsum; 5USO; -.
DR   PDBsum; 6BWY; -.
DR   PDBsum; 7CUH; -.
DR   PDBsum; 7CUI; -.
DR   AlphaFoldDB; O13988; -.
DR   SMR; O13988; -.
DR   BioGRID; 279156; 33.
DR   DIP; DIP-38935N; -.
DR   IntAct; O13988; 2.
DR   STRING; 284812.O13988; -.
DR   iPTMnet; O13988; -.
DR   MaxQB; O13988; -.
DR   PaxDb; 4896-SPAC26H5-06-1; -.
DR   EnsemblFungi; SPAC26H5.06.1; SPAC26H5.06.1:pep; SPAC26H5.06.
DR   GeneID; 2542703; -.
DR   KEGG; spo:SPAC26H5.06; -.
DR   PomBase; SPAC26H5.06; pot1.
DR   VEuPathDB; FungiDB:SPAC26H5.06; -.
DR   eggNOG; KOG4757; Eukaryota.
DR   HOGENOM; CLU_016663_1_0_1; -.
DR   InParanoid; O13988; -.
DR   OMA; WEPHASF; -.
DR   PhylomeDB; O13988; -.
DR   EvolutionaryTrace; O13988; -.
DR   PRO; PR:O13988; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000783; C:nuclear telomere cap complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0070187; C:shelterin complex; IC:PomBase.
DR   GO; GO:0000782; C:telomere cap complex; IDA:PomBase.
DR   GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:PomBase.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:PomBase.
DR   GO; GO:0010521; F:telomerase inhibitor 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; IDA:PomBase.
DR   GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR   CDD; cd04497; hPOT1_OB1_like; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; PROTECTION OF TELOMERES 1; 1.
DR   PANTHER; PTHR14513:SF0; PROTECTION OF TELOMERES PROTEIN 1; 1.
DR   Pfam; PF02765; POT1; 1.
DR   Pfam; PF16686; POT1PC; 1.
DR   SMART; SM00976; Telo_bind; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW   Telomere.
FT   CHAIN           1..555
FT                   /note="Protection of telomeres protein 1"
FT                   /id="PRO_0000121732"
FT   HELIX           8..16
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   STRAND          41..57
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:1QZH"
FT   STRAND          83..93
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   STRAND          104..115
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   STRAND          118..131
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:7CUH"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:7CUH"
FT   HELIX           156..173
FT                   /evidence="ECO:0007829|PDB:1QZG"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   STRAND          212..224
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   TURN            247..249
FT                   /evidence="ECO:0007829|PDB:4HIO"
FT   STRAND          258..260
FT                   /evidence="ECO:0007829|PDB:5USN"
FT   STRAND          263..267
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   HELIX           270..275
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   TURN            276..278
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   STRAND          284..294
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   STRAND          300..304
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   HELIX           310..312
FT                   /evidence="ECO:0007829|PDB:4HJ7"
FT   STRAND          315..319
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   HELIX           324..326
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   HELIX           327..336
FT                   /evidence="ECO:0007829|PDB:5USB"
FT   STRAND          378..380
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           390..394
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   STRAND          405..419
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           421..423
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   STRAND          424..429
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   TURN            430..432
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   STRAND          433..443
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   STRAND          449..455
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           456..463
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           473..475
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           477..491
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           494..504
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           508..510
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           511..514
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   STRAND          519..527
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   HELIX           542..544
FT                   /evidence="ECO:0007829|PDB:7CUI"
FT   STRAND          546..554
FT                   /evidence="ECO:0007829|PDB:7CUI"
SQ   SEQUENCE   555 AA;  64111 MW;  A79DAA95A0C4F803 CRC64;
     MGEDVIDSLQ LNELLNAGEY KIGELTFQSI RSSQELQKKN TIVNLFGIVK DFTPSRQSLH
     GTKDWVTTVY LWDPTCDTSS IGLQIHLFSK QGNDLPVIKQ VGQPLLLHQI TLRSYRDRTQ
     GLSKDQFRYA LWPDFSSNSK DTLCPQPMPR LMKTGDKEEQ FALLLNKIWD EQTNKHKNGE
     LLSTSSARQN QTGLSYPSVS FSLLSQITPH QRCSFYAQVI KTWYSDKNFT LYVTDYTENE
     LFFPMSPYTS SSRWRGPFGR FSIRCILWDE HDFYCRNYIK EGDYVVMKNV RTKIDHLGYL
     ECILHGDSAK RYNMSIEKVD SEEPELNEIK SRKRLYVQNC QNGIEAVIEK LSQSQQSENP
     FIAHELKQTS VNEITAHVIN EPASLKLTTI STILHAPLQN LLKPRKHRLR VQVVDFWPKS
     LTQFAVLSQP PSSYVWMFAL LVRDVSNVTL PVIFFDSDAA ELINSSKIQP CNLADHPQMT
     LQLKERLFLI WGNLEERIQH HISKGESPTL AAEDVETPWF DIYVKEYIPV IGNTKDHQSL
     TFLQKRWRGF GTKIV
//