POZ1_SCHPO
ID POZ1_SCHPO Reviewed; 249 AA.
AC O13852; B3A005;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protection of telomeres protein poz1;
DE AltName: Full=Pot1-associated protein poz1;
GN Name=poz1; ORFNames=SPAC19G12.13c;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH POT1; RAP1 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 [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Telomeric DNA-binding protein that negatively regulates
CC telomerase and telomere length. {ECO:0000269|PubMed:18535244}.
CC -!- SUBUNIT: Interacts with pot1, rap1 and tpz1.
CC {ECO:0000269|PubMed:18535244}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18535244}. Chromosome,
CC telomere {ECO:0000269|PubMed:18535244}.
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DR EMBL; AB433171; BAG48201.1; -; mRNA.
DR EMBL; CU329670; CAB10124.1; -; Genomic_DNA.
DR PIR; T38000; T38000.
DR RefSeq; NP_594428.1; NM_001019857.2.
DR PDB; 5WE0; X-ray; 2.30 A; A/D/G/J=2-249.
DR PDB; 5WE1; X-ray; 3.20 A; A/C=30-75, A/C=86-249.
DR PDB; 5WE2; X-ray; 2.50 A; A/C=2-249.
DR PDB; 5XXE; X-ray; 2.50 A; A/B=2-249.
DR PDB; 5XXF; X-ray; 3.10 A; A/B=2-247.
DR PDBsum; 5WE0; -.
DR PDBsum; 5WE1; -.
DR PDBsum; 5WE2; -.
DR PDBsum; 5XXE; -.
DR PDBsum; 5XXF; -.
DR AlphaFoldDB; O13852; -.
DR SMR; O13852; -.
DR BioGRID; 278714; 39.
DR IntAct; O13852; 1.
DR STRING; 4896.SPAC19G12.13c.1; -.
DR iPTMnet; O13852; -.
DR MaxQB; O13852; -.
DR PaxDb; O13852; -.
DR EnsemblFungi; SPAC19G12.13c.1; SPAC19G12.13c.1:pep; SPAC19G12.13c.
DR GeneID; 2542244; -.
DR KEGG; spo:SPAC19G12.13c; -.
DR PomBase; SPAC19G12.13c; poz1.
DR VEuPathDB; FungiDB:SPAC19G12.13c; -.
DR HOGENOM; CLU_1185616_0_0_1; -.
DR OMA; QACLENL; -.
DR PRO; PR:O13852; -.
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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0070187; C:shelterin complex; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:PomBase.
DR GO; GO:0016233; P:telomere capping; IGI:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR GO; GO:0032200; P:telomere organization; IMP:PomBase.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Telomere.
FT CHAIN 1..249
FT /note="Protection of telomeres protein poz1"
FT /id="PRO_0000116741"
FT HELIX 2..18
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:5WE0"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 93..115
FT /evidence="ECO:0007829|PDB:5WE0"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:5XXF"
FT HELIX 130..157
FT /evidence="ECO:0007829|PDB:5WE0"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5WE2"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 209..230
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:5WE0"
SQ SEQUENCE 249 AA; 29754 MW; 6051EE0973BC3971 CRC64;
MNEKIRSQSV LNTLETFFIK ENHYDMQREE SSIVNACLRY LGYSKSMCHE KMPIFMDIAF
IEYCFNLSLD PSSFQNLPIT QTQPDSQQIL WEYSLISNAL ERLENIELER QNCMREDGLV
KYTNELLLNK ETLNNEALKL YSCAKAGICR WMAFHFLEQE PIDHINFTKF LQDWGSHNEK
EMEALQRLSK HKIRKRLIYV SQHKKKMPWS KFNSVLSRYI QCTKLQLEVF CDYDFKQREI
VKMLTSNIN
