TAZ1_SCHPO
ID TAZ1_SCHPO Reviewed; 663 AA.
AC P79005; O00049;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=Telomere length regulator taz1;
GN Name=taz1; Synonyms=myb, myb1; ORFNames=SPAC16A10.07c;
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].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9034194; DOI=10.1038/385744a0;
RA Cooper J.P., Nimmo E.R., Allshire R.C., Cech T.R.;
RT "Regulation of telomere length and function by a Myb-domain protein in
RT fission yeast.";
RL Nature 385:744-747(1997).
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 INTERACTION WITH TAF1.
RX PubMed=11270572; DOI=10.1007/s002940000168;
RA Ueno M., Kurokawa R., Renauld H., Watanabe K., Ushimaru T., Uritani M.,
RA Yoshinaga K., Hiraoka Y.;
RT "Schizosaccharomyces pombe taf1+ is required for nitrogen starvation-
RT induced sexual development and for entering the dormant GO state.";
RL Curr. Genet. 38:307-313(2001).
RN [4]
RP INTERACTION WITH CCQ1, AND SUBCELLULAR LOCATION.
RX PubMed=15546621; DOI=10.1016/j.molcel.2004.10.027;
RA Flory M.R., Carson A.R., Muller E.G., Aebersold R.;
RT "An SMC-domain protein in fission yeast links telomeres to the meiotic
RT centrosome.";
RL Mol. Cell 16:619-630(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16615890; DOI=10.1016/j.cell.2006.01.048;
RA Chikashige Y., Tsutsumi C., Yamane M., Okamasa K., Haraguchi T.,
RA Hiraoka Y.;
RT "Meiotic proteins bqt1 and bqt2 tether telomeres to form the bouquet
RT arrangement of chromosomes.";
RL Cell 125:59-69(2006).
RN [6]
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Regulates telomere length and function. Required for the
CC repression of telomere-adjacent gene expression and for normal meiosis
CC or sporulation. It may be a negative regulator of the telomere-
CC replicating enzyme, telomerase, or may protect against activation of
CC telomerase-independent pathways of telomere elongation. It may be
CC involved in the interactions between chromosomes and spindle proteins,
CC disruption of these interactions would lead to defective meiosis.
CC -!- SUBUNIT: Interacts with taf1 via the Myb domain, and ccq1.
CC {ECO:0000269|PubMed:11270572, ECO:0000269|PubMed:15546621}.
CC -!- INTERACTION:
CC P79005; Q96TL7: rap1; NbExp=5; IntAct=EBI-15903288, EBI-929794;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, telomere.
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DR EMBL; Y09406; CAA70568.1; -; mRNA.
DR EMBL; CU329670; CAB10000.1; -; Genomic_DNA.
DR PIR; T37772; T37772.
DR RefSeq; NP_594047.1; NM_001019472.2.
DR PDB; 2L3N; NMR; -; A=362-395.
DR PDB; 4ZMI; X-ray; 2.30 A; A=127-361.
DR PDB; 4ZMK; X-ray; 1.50 A; A=408-478.
DR PDBsum; 2L3N; -.
DR PDBsum; 4ZMI; -.
DR PDBsum; 4ZMK; -.
DR AlphaFoldDB; P79005; -.
DR SMR; P79005; -.
DR BioGRID; 278779; 49.
DR DIP; DIP-59072N; -.
DR IntAct; P79005; 1.
DR STRING; 4896.SPAC16A10.07c.1; -.
DR iPTMnet; P79005; -.
DR MaxQB; P79005; -.
DR PaxDb; P79005; -.
DR PRIDE; P79005; -.
DR EnsemblFungi; SPAC16A10.07c.1; SPAC16A10.07c.1:pep; SPAC16A10.07c.
DR GeneID; 2542313; -.
DR KEGG; spo:SPAC16A10.07c; -.
DR PomBase; SPAC16A10.07c; taz1.
DR VEuPathDB; FungiDB:SPAC16A10.07c; -.
DR HOGENOM; CLU_422819_0_0_1; -.
DR OMA; PAYCEIH; -.
DR EvolutionaryTrace; P79005; -.
DR PRO; PR:P79005; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0110092; C:nucleus leading edge; IDA:PomBase.
DR GO; GO:0070187; C:shelterin complex; IDA:PomBase.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:PomBase.
DR GO; GO:0060090; F:molecular adaptor activity; EXP:PomBase.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:PomBase.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; IMP:PomBase.
DR GO; GO:0032121; P:meiotic attachment of telomeric heterochromatin to spindle pole body; IMP:PomBase.
DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; IGI:PomBase.
DR GO; GO:0044820; P:mitotic telomere tethering at nuclear periphery; IMP:PomBase.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IMP:PomBase.
DR GO; GO:0101017; P:regulation of mitotic DNA replication initiation from late origin; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IGI:PomBase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR Pfam; PF08558; TRF; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Telomere.
FT CHAIN 1..663
FT /note="Telomere length regulator taz1"
FT /id="PRO_0000197124"
FT DOMAIN 556..612
FT /note="Myb-like"
FT REGION 15..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 131..161
FT /evidence="ECO:0007829|PDB:4ZMI"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 263..280
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 340..355
FT /evidence="ECO:0007829|PDB:4ZMI"
FT HELIX 376..389
FT /evidence="ECO:0007829|PDB:2L3N"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:4ZMK"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:4ZMK"
FT HELIX 427..447
FT /evidence="ECO:0007829|PDB:4ZMK"
FT HELIX 451..477
FT /evidence="ECO:0007829|PDB:4ZMK"
SQ SEQUENCE 663 AA; 74647 MW; 5852F21518031152 CRC64;
MISVQSTETI QKVLENEGDQ QFDKEVVQNS DSNIETGQIS DSLTKAVEER AETESSSNLS
NFTTSESESS KPAYCFNSHS QNMAEGSISI PVISHSMNVE NEVSTAEGQD SRTGESENDQ
NAMIVRSIWD IEKASLLVND CQNIANMAEQ KVMMVSAIFS ESSKDIVNPE SFSERLGKET
VKDLYEFNEQ LTTKYGLEFR TIFFSYIRKY DAYWCLFEDL EKPLKSIQFF TGLIDLLDNT
NKHLTLRSIV LDALLSADEE DSFYGDALVL FEELVIRYFG TDSNPSIDAS EFILSCLPYT
SLDALNVVCG QVWKSQKICD FLKSTIGNTS NSPLQLRASF PAFVNAVIHF LLEFKNVRRL
ERKDLSVKGM LYDSDSQQIL NRLRERVSGS TAQSADEASG HESDASEDTF SERTLGLNSI
DNTEISEVVS LGLVSSALDK ITGLLSADNL SETVSQARDF SHTLSKSLKS RAKSLSQKEA
ANRSKLIAKR GDNLRREASL SSEQDDLSED FPPVRESDEQ ESRSGGRSSA MRVSIERSAA
RSGTRRSQGN PYEGYRTRRK WTDEEENELY EMISQHGCCW SKIIHIQKLE NGPLKTFGPT
QIKDKARLIK ARFMKQNRLQ ELYSKSLNWK NVTVGQAYCE LHKIPYIEAT PPLLREELVN
YQS
