STS5_SCHPO
ID STS5_SCHPO Reviewed; 1066 AA.
AC O74454; O13452;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein sts5;
GN Name=sts5; ORFNames=SPCC16C4.09;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8886983; DOI=10.1242/jcs.109.9.2331;
RA Toda T., Niwa H., Nemoto T., Dhut S., Eddison M., Matsusaka T.,
RA Yanagida M., Hirata D.;
RT "The fission yeast sts5+ gene is required for maintenance of growth
RT polarity and functionally interacts with protein kinase C and an
RT osmosensing MAP-kinase pathway.";
RL J. Cell Sci. 109:2331-2342(1996).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157; THR-262; SER-264 AND
RP THR-377, AND IDENTIFICATION BY 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: Required for the maintenance of cell shape during interphase.
CC Required for localization of cortical actin to the growing tips before
CC mitosis. {ECO:0000269|PubMed:8886983}.
CC -!- SUBUNIT: Interacts with serine/threonine phosphatase ppe1, protein
CC kinase C and an osmosensing MAP kinase.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8886983}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; D58421; BAA23619.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20748.1; -; Genomic_DNA.
DR PIR; T41099; T41099.
DR PIR; T45283; T45283.
DR RefSeq; NP_587919.1; NM_001022910.2.
DR AlphaFoldDB; O74454; -.
DR SMR; O74454; -.
DR BioGRID; 275751; 320.
DR STRING; 4896.SPCC16C4.09.1; -.
DR iPTMnet; O74454; -.
DR MaxQB; O74454; -.
DR PaxDb; O74454; -.
DR PRIDE; O74454; -.
DR EnsemblFungi; SPCC16C4.09.1; SPCC16C4.09.1:pep; SPCC16C4.09.
DR GeneID; 2539180; -.
DR KEGG; spo:SPCC16C4.09; -.
DR PomBase; SPCC16C4.09; sts5.
DR VEuPathDB; FungiDB:SPCC16C4.09; -.
DR eggNOG; KOG2102; Eukaryota.
DR HOGENOM; CLU_282442_0_0_1; -.
DR InParanoid; O74454; -.
DR OMA; PCLTVRT; -.
DR PhylomeDB; O74454; -.
DR PRO; PR:O74454; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000932; C:P-body; ISS:PomBase.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; ISM:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; ISO:PomBase.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR041093; Dis3l2_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR Pfam; PF17877; Dis3l2_C_term; 1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Exonuclease; Hydrolase; Nuclease; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1066
FT /note="Protein sts5"
FT /id="PRO_0000166422"
FT REGION 18..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 5
FT /note="F -> C (in Ref. 1; BAA23619)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="V -> G (in Ref. 1; BAA23619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1066 AA; 117604 MW; 077187800B330C15 CRC64;
MDEEFENDFP YKVMLNQQQD PSDAQSSPTF VPSANPSLTT PWLQTTPSAN RPTWLPLQQH
MHQLRHTGLL PAVESSFVHG HRRSASAGVG MGNFSNQATI PSNSPAVSNM QPPTQGGQPL
YPTNFFTTSV SASSDSFPNS PTVPSKFSLN PSVATSTNIS PRRHAKSHSV ASVSSPNSHN
AVPFTPHAFV PPVNNASPLP ALNTLPQLLR PRNLDAQWRP SSLSQTNSPT HAANPSFPGT
IVTHNTSNFR PEGGGHRHRR STGSLSVGSS GSGFSSGGSG NPRKNLFSPY LPQSSIPALL
AERRLVTGIL IVSKKNRSDA FVSVDGLDAE VFICGSKDRN RALEGDVVAI ELLDVDEVWA
GKLEKEENRR RKDPISTRGS FDNLRIDAVP FEVPQRSAIK ARDDEQVEGQ TLFLLDQKQL
GADEKPKYAG HVVAVLQRAP GQVFSGTLGI LRPSSAANKE RQTSSGNQGS SNNSGNDKPK
IVWFKPSDKR VPLIAIPTEQ APTDFLGNDQ AYAQRLFLAS IKRWPVTSLH PFGMLVGELG
SMDSMSAQVS ALLHDTGVHS EPWEGSAATS AVTALNALSD NFLNVAGCAD YRSEDVFLFV
KNDVSKAAVS EVKQHESNIN SSSATDFVSS AFHIRPTSTG YHVGIHVTDV SRVIEPGSPL
DRELQRRSIA VNLCQKSVPL FPTTLGEALS LREDKDCYTM SLLLDVSSTG KIRGTWIGWA
VIRPRKAYTM KEADELLQTD ARLRLFHTVS SRLRTHHLGT DVPLSRYCRL VRRWDEESCS
FDPNETNLFI SSAVEVLRET LLDAANRAVA SHLRQEFREN AFLRTQRLPS RENCRILQSM
AIQMGCVLDL SSTKSLLRSL SLIEDDTVRN ILQLYYYKVT PRAVYEMQKY KGNLASQMMS
LGIEDESDDL THFTAPLERY GDIVVHYQLQ LLLRGELASE KRLRVWSQAA NDASRRLVIS
KFAQETSIHI KIFSDWAESQ VWQDGLVCFV APSYFDVFFP SLGMEKRVHL DLLNLTHVRF
EEDQGILSLY DESGAVTVVK LLTSVKVKLF VQLSTPPLIN VSNVEF
