ID   LAS1_SCHPO              Reviewed;         470 AA.
AC   O42936;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Pre-rRNA-processing protein las1;
GN   Name=las1; ORFNames=SPBC16C6.12c;
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   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CRB3, GRC3 AND RIX1,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=21385875; DOI=10.1074/jbc.m110.201343;
RA   Kitano E., Hayashi A., Kanai D., Shinmyozu K., Nakayama J.;
RT   "Roles of fission yeast Grc3 protein in ribosomal RNA processing and
RT   heterochromatic gene silencing.";
RL   J. Biol. Chem. 286:15391-15402(2011).
CC   -!- FUNCTION: Required for both pre-rRNA processing and heterochromatic
CC       gene silencing. {ECO:0000269|PubMed:21385875}.
CC   -!- SUBUNIT: Interacts with crb3, gcr3 and eix1.
CC       {ECO:0000269|PubMed:21385875}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Cytoplasm, cytoskeleton,
CC       spindle pole.
CC   -!- SIMILARITY: Belongs to the LAS1 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA16919.1; -; Genomic_DNA.
DR   PIR; T39563; T39563.
DR   RefSeq; NP_596810.1; NM_001023831.2.
DR   AlphaFoldDB; O42936; -.
DR   SMR; O42936; -.
DR   BioGRID; 276576; 3.
DR   STRING; 4896.SPBC16C6.12c.1; -.
DR   SwissPalm; O42936; -.
DR   MaxQB; O42936; -.
DR   PaxDb; O42936; -.
DR   EnsemblFungi; SPBC16C6.12c.1; SPBC16C6.12c.1:pep; SPBC16C6.12c.
DR   GeneID; 2540034; -.
DR   KEGG; spo:SPBC16C6.12c; -.
DR   PomBase; SPBC16C6.12c; las1.
DR   VEuPathDB; FungiDB:SPBC16C6.12c; -.
DR   eggNOG; KOG2425; Eukaryota.
DR   HOGENOM; CLU_581602_0_0_1; -.
DR   InParanoid; O42936; -.
DR   OMA; WSTRGRI; -.
DR   Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:O42936; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR   GO; GO:0090730; C:Las1 complex; ISO:PomBase.
DR   GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IC:PomBase.
DR   GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR   GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IMP:PomBase.
DR   InterPro; IPR007174; Las1.
DR   PANTHER; PTHR15002; PTHR15002; 1.
DR   Pfam; PF04031; Las1; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW   rRNA processing; Transcription; Transcription regulation.
FT   CHAIN           1..470
FT                   /note="Pre-rRNA-processing protein las1"
FT                   /id="PRO_0000211560"
SQ   SEQUENCE   470 AA;  54307 MW;  918F46EF2D8E6F54 CRC64;
     MDMKVVPWRL KEDFLYLMSC FYNEGQEGIP DLAALFRGVE IIQAWSTRGR IPHSVESTSQ
     LVSSLISNDR SQKLALAVSI SRFVSGLLDP IQQSQYAIPM AVLAKSIDLP TYFVELRHAI
     THEELPSLPV LRQAAQRALS WLYDHYWNPA ATAESEDTYD YTETNELHKF EIKRKVKDLL
     KQWRSWRKVN VSANMFLPVE EHDYIQQFEA LVQELVTTAN LRLPYIPASF VDDEKDLDFA
     IETTNLDIVV SCFLEKRVLI PSRTMPISFF PKLKNVWLPL LQSIASKHSF FLPALFTTLW
     SEILEISQTV DSLVFLDLKE KEELTDKESA GCYLAKWYAY LMREAYTGQP WTSTLSVTQT
     DLASVLEICL QRSDPFTKII IDELSILDKE LENKFSPLFQ YRSDMFDSRI LDEQEFEDIT
     LEQMKTELNK FSVRLNNIEA QADSSTMEFQ GHVWYKPSVE PSPIGQIIES