PIR2_SCHPO
ID PIR2_SCHPO Reviewed; 609 AA.
AC O94326;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=NURS complex subunit pir2 {ECO:0000305};
GN Name=pir2 {ECO:0000312|PomBase:SPBC725.08};
GN Synonyms=ars2 {ECO:0000312|PomBase:SPBC725.08};
GN ORFNames=SPBC725.08 {ECO:0000312|PomBase:SPBC725.08};
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-30, AND
RP 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).
RN [4]
RP INTERACTION WITH CCR4, AND MUTAGENESIS OF PHE-165 AND SER-316.
RX PubMed=26942678; DOI=10.1016/j.molcel.2016.01.029;
RA Sugiyama T., Thillainadesan G., Chalamcharla V.R., Meng Z.,
RA Balachandran V., Dhakshnamoorthy J., Zhou M., Grewal S.I.S.;
RT "Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors
RT to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly.";
RL Mol. Cell 61:747-759(2016).
CC -!- SUBUNIT: Interacts with ccr4. {ECO:0000269|PubMed:26942678}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22180.1; -; Genomic_DNA.
DR PIR; T40660; T40660.
DR RefSeq; NP_595488.1; NM_001021399.2.
DR AlphaFoldDB; O94326; -.
DR SMR; O94326; -.
DR BioGRID; 277658; 265.
DR IntAct; O94326; 3.
DR STRING; 4896.SPBC725.08.1; -.
DR iPTMnet; O94326; -.
DR MaxQB; O94326; -.
DR PaxDb; O94326; -.
DR PRIDE; O94326; -.
DR EnsemblFungi; SPBC725.08.1; SPBC725.08.1:pep; SPBC725.08.
DR GeneID; 2541143; -.
DR KEGG; spo:SPBC725.08; -.
DR PomBase; SPBC725.08; -.
DR VEuPathDB; FungiDB:SPBC725.08; -.
DR eggNOG; KOG2295; Eukaryota.
DR HOGENOM; CLU_031224_0_0_1; -.
DR InParanoid; O94326; -.
DR OMA; CPGGHIR; -.
DR PhylomeDB; O94326; -.
DR PRO; PR:O94326; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:1990477; C:MTREC complex; IDA:PomBase.
DR GO; GO:0016604; C:nuclear body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; ISO:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR InterPro; IPR039727; SE/Ars2.
DR InterPro; IPR007042; SERRATE/Ars2_C.
DR InterPro; IPR021933; SERRATE/Ars2_N.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13165; PTHR13165; 1.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..609
FT /note="NURS complex subunit pir2"
FT /id="PRO_0000352817"
FT ZN_FING 474..499
FT /note="C2H2-type"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 165
FT /note="F->L: Decreases cell population growth at high
FT temperature; when associated with P-316."
FT /evidence="ECO:0000269|PubMed:26942678"
FT MUTAGEN 316
FT /note="S->P: Decreases cell population growth at high
FT temperature; when associated with L-165."
FT /evidence="ECO:0000269|PubMed:26942678"
SQ SEQUENCE 609 AA; 70865 MW; B132313AB9BD75C4 CRC64;
MSEVHQESEV EYSRWKRERS PERSQRRSQS PPGEQSAYHR ERSPLRKRGN YYDDRTRASG
PYPTFTKPLI DPYTQTNAVS YERFIRWYSK ENHISATTED LYNSLHGTYN NYKQDLYART
ARSFVESHCD EAWFEDSYWV DESQGRVLEV SENEKSYRRA LYDKFMDRLD AGYYDDFQLP
TAEDVIEKPS IPDNDTDDSI LPSNDPQLSK WNQDSRNDAM ENTLLVSHVL PNISVAQIHN
ALDGISFVQH FSLSTINLIK NDERSLWVHF KAGTNMDGAK EAVDGIQLDS NFTIESENPK
IPTHTHPIPI FEIASSEQTC KNLLEKLIRF IDRASTKYSL PNDAAQRIED RLKTHASMKD
DDDKPTNFHD IRLSDLYAEY LRQVATFDFW TSKEYESLIA LLQDSPAGYS RKKFNPSKEV
GQEENIWLSD LENNFACLLE PENVDIKAKG ALPVEDFINN ELDSVIMKED EQKYRCHVGT
CAKLFLGPEF VRKHINKKHK DWLDHIKKVA ICLYGYVLDP CRAMDPKVVS TSYVSLQILN
KPYVGFRNIN ANYTFPTTSY SRRNDEEITS GASSQKSYSR QEPMIHRREF YRTYQDLDAP
NQEVPELDY
