TPZ1_SCHPO
ID TPZ1_SCHPO Reviewed; 508 AA.
AC O14246; B3A004;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protection of telomeres protein tpz1;
DE AltName: Full=Meiotically up-regulated gene 169 protein;
GN Name=tpz1; Synonyms=mug169; ORFNames=SPAC6F6.16c, SPAC6F6.18c;
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 POZ1; POT1 AND CCQ1.
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
CC -!- FUNCTION: Telomeric DNA-binding protein that is required to protect the
CC 3'-end telomeric overhang and involved in telomere length regulation.
CC recruits poz1 and ccq1 to telomeres, regulating telomere length
CC negatively and positively respectively. {ECO:0000269|PubMed:16303567,
CC ECO:0000269|PubMed:18535244}.
CC -!- SUBUNIT: Interacts with ccq1, pot1 and poz1.
CC {ECO:0000269|PubMed:18535244}.
CC -!- INTERACTION:
CC O14246; Q10432: ccq1; NbExp=2; IntAct=EBI-8802014, EBI-15953947;
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000269|PubMed:18535244}. Nucleus {ECO:0000269|PubMed:18535244}.
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DR EMBL; AB433170; BAG48200.1; -; mRNA.
DR EMBL; CU329670; CAB11738.2; -; Genomic_DNA.
DR PIR; T39049; T39049.
DR RefSeq; NP_593908.2; NM_001019338.3.
DR PDB; 5WE0; X-ray; 2.30 A; B/E/H/K=476-508.
DR PDB; 5WE1; X-ray; 3.20 A; B/D=476-508.
DR PDB; 5WE2; X-ray; 2.50 A; B/D=476-508.
DR PDB; 5XXE; X-ray; 2.50 A; C/D=477-508.
DR PDB; 5XXF; X-ray; 3.10 A; C/D=478-508.
DR PDB; 7CUI; X-ray; 2.60 A; B/D=164-240.
DR PDB; 7CUJ; X-ray; 2.40 A; C/D=426-470.
DR PDBsum; 5WE0; -.
DR PDBsum; 5WE1; -.
DR PDBsum; 5WE2; -.
DR PDBsum; 5XXE; -.
DR PDBsum; 5XXF; -.
DR PDBsum; 7CUI; -.
DR PDBsum; 7CUJ; -.
DR AlphaFoldDB; O14246; -.
DR SMR; O14246; -.
DR BioGRID; 278878; 14.
DR DIP; DIP-59445N; -.
DR IntAct; O14246; 3.
DR MINT; O14246; -.
DR STRING; 4896.SPAC6F6.16c.1; -.
DR iPTMnet; O14246; -.
DR MaxQB; O14246; -.
DR PaxDb; O14246; -.
DR PRIDE; O14246; -.
DR EnsemblFungi; SPAC6F6.16c.1; SPAC6F6.16c.1:pep; SPAC6F6.16c.
DR PomBase; SPAC6F6.16c; tpz1.
DR VEuPathDB; FungiDB:SPAC6F6.16c; -.
DR HOGENOM; CLU_536555_0_0_1; -.
DR OMA; HETRNIN; -.
DR Reactome; R-SPO-174437; Removal of the Flap Intermediate from the C-strand.
DR PRO; PR:O14246; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0070187; C:shelterin complex; IDA:PomBase.
DR GO; GO:0000782; C:telomere cap complex; IDA:PomBase.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; IGI:PomBase.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:PomBase.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IBA:GO_Central.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:PomBase.
DR GO; GO:0016233; P:telomere capping; IGI:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:PomBase.
DR GO; GO:1905324; P:telomere-telomerase complex assembly; IMP:PomBase.
DR InterPro; IPR028631; ACD.
DR PANTHER; PTHR14487; PTHR14487; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW Telomere.
FT CHAIN 1..508
FT /note="Protection of telomeres protein tpz1"
FT /id="PRO_0000304008"
FT REGION 2..223
FT /note="pot1-binding"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..508
FT /note="ccq1/poz1-binding"
FT COMPBIAS 252..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:7CUI"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:7CUI"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:7CUI"
FT HELIX 441..465
FT /evidence="ECO:0007829|PDB:7CUJ"
FT HELIX 480..484
FT /evidence="ECO:0007829|PDB:5WE0"
FT HELIX 490..505
FT /evidence="ECO:0007829|PDB:5WE0"
SQ SEQUENCE 508 AA; 57684 MW; A1A2F59238DACBF7 CRC64;
MSNCLKHPWL ENGLLNLIKN ADVLPIRVFK CQPLQIFEYI RYEHPIRCKL SDTEFYIEAE
FSSQSISDLN NFTEKRITSL RGGIVTLGNF LIHLIPSQSG IIPWIQVESF NFQGCEGAVF
GNPKAITTSA LFNALLQSPY LAALANEFNR SIKEGSSYQE ASLSQQEKPN DNTSNSRDIK
NNIQFHWKNM TSLSIEECII PKGQQLILEK ESEENTTHGI YLEERKMAQG LHNSVSETPE
VKQEDNDEDL DAYSWSSSTD SAGEIPSLPT NRKILEKIAE KPPPFESPLE DDETPDQTNE
HEANQVNVSQ LPLNPRGSGI SGRPVESTEQ LNSSLTIERS QSIQSTDSKQ RVETQSHRRS
KIEIFDAQDE LFDRSICTTI DDSTGKLLNA EETPIKTGDL HSTSASSVIS CTPPAINFTS
DICNEQIELE YKRKPIPDYD FMKGLETTLQ ELYVEHQSKK RRLELFQLTN NHQKNSEACE
MCRLGLPHGS FFELLRDWKK IEEFRNKS
