POT1_SCHPO
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 03-AUG-2022, entry version 147.
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; 4896.SPAC26H5.06.1; -.
DR MaxQB; O13988; -.
DR PaxDb; O13988; -.
DR PRIDE; O13988; -.
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; LWEPHAS; -.
DR PhylomeDB; O13988; -.
DR Reactome; R-SPO-174437; Removal of the Flap Intermediate from the C-strand.
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:0051974; P:negative regulation of telomerase activity; IBA:GO_Central.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:PomBase.
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 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 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
