PAT1_SCHPO
ID PAT1_SCHPO Reviewed; 754 AA.
AC O42958;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=DNA topoisomerase 2-associated protein pat1;
DE AltName: Full=Decapping activator and translational repressor pat1;
DE AltName: Full=Topoisomerase II-associated protein pat1;
GN ORFNames=SPBC19G7.10c;
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 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: Activator of decapping that functions as a general and active
CC mechanism of translational repression and required for P-body
CC formation. Stabilizes the 3' terminus of mRNAs and modulates the rates
CC of mRNA-decapping that occur following deadenylation. Might be required
CC for promoting the formation or the stabilization of the preinitiation
CC translation complexes. Necessary for accurate chromosome transmission
CC during cell division (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Cytoplasm, P-body {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the PAT1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17064.2; -; Genomic_DNA.
DR PIR; T39841; T39841.
DR RefSeq; NP_595976.2; NM_001021884.3.
DR AlphaFoldDB; O42958; -.
DR SMR; O42958; -.
DR BioGRID; 277297; 25.
DR STRING; 4896.SPBC19G7.10c.1; -.
DR iPTMnet; O42958; -.
DR MaxQB; O42958; -.
DR PaxDb; O42958; -.
DR EnsemblFungi; SPBC19G7.10c.1; SPBC19G7.10c.1:pep; SPBC19G7.10c.
DR GeneID; 2540778; -.
DR KEGG; spo:SPBC19G7.10c; -.
DR PomBase; SPBC19G7.10c; -.
DR VEuPathDB; FungiDB:SPBC19G7.10c; -.
DR eggNOG; KOG4592; Eukaryota.
DR HOGENOM; CLU_012622_1_0_1; -.
DR InParanoid; O42958; -.
DR OMA; DFITRYQ; -.
DR PhylomeDB; O42958; -.
DR Reactome; R-SPO-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:O42958; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000932; C:P-body; IPI:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR InterPro; IPR039900; Pat1-like.
DR InterPro; IPR019167; PAT1_dom.
DR PANTHER; PTHR21551; PTHR21551; 1.
DR Pfam; PF09770; PAT1; 2.
PE 3: Inferred from homology;
KW Cytoplasm; mRNA processing; Reference proteome; Repressor; RNA-binding;
KW Translation regulation.
FT CHAIN 1..754
FT /note="DNA topoisomerase 2-associated protein pat1"
FT /id="PRO_0000372628"
SQ SEQUENCE 754 AA; 84117 MW; EB226989F3D8E53A CRC64;
MSFFGFNTTL PKENMFPNEG QLEEDGIDFE ETYDDLGNQL NEAGDELNDE TFGVSAGSIG
RDFDFSGTTA QASAQLEDEQ YQINQQNIFA KPVKPASSEL PQVSRLNGAS QFPSREPAST
AINKLSDLQP MASIWENIVP EKPAIIPPEV ASLQDRLGAQ PSEKVFSLQE LEEQLLNSMT
APKPPSQPAI PIVPSEMAAQ VTRENISSLD PAISAASIGN VTFGQPNIPS TTTDFAGLAA
PNMVHPSQAI PNPVMQPSLV PQMPYPQNGM YNPSVAPPAS LVNLFQQEQL IQNQNLDEKR
QKLERDHMLM AQCAGLMTRS DKSFIARIQI SQLMSEDPES DDFYYRVYSI IRGRKPSEEE
ASHFIQTYLG PSNNRRRGRR SENPMQKLQQ QLQRLVSSAK ERPKATQLSL EGALGKIAVN
TVRTPRQLLN VKRPTEPASS NSSLNNFSGF STKKDVLHAI EKVYDLLLDF EQALRKASTL
ETTDQEQIDT WKTTLSEKLE SIWKALYINE SLEASSKTRP PFISIISHPK GMRLLPRLFP
HLSKEQQISI LKVVVYNFDS LDIVLRGTFD VNGELPLDVV SEMSSFTQFI IPPLLTIVNE
LDLETINNLF SQLLNRTNAV YLIQTKIGLS FLTLFISRAE ILKQSGTVNQ NEKEEWENTF
NVMFNRVKGH FSTVFPPPNA RAYADESYPW EFLAACATAA SSEQHFTLVS ETRDRVLDNI
ITSKRAPSEI AVVRISNVNL FLNAMGLDAR QLSA