ID   RIX1_SCHPO              Reviewed;         828 AA.
AC   P87243;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Pre-rRNA-processing protein rix1;
GN   Name=rix1; ORFNames=SPCC4G3.18;
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 LAS1,
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: Component of the RIX1 complex required for processing of ITS2
CC       sequences from 35S pre-rRNA and the nucleoplasmic transit of the pre-
CC       60S ribosomal subunits (PubMed:21385875). Regulates pre-60S association
CC       of the critical remodeling factor mdn1 (By similarity). Also required
CC       for heterochromatic gene silencing (PubMed:21385875).
CC       {ECO:0000250|UniProtKB:P38883, ECO:0000269|PubMed:21385875}.
CC   -!- SUBUNIT: Component of the RIX1 complex, composed of ipi1, rix1/ipi2 and
CC       crb3/ipi3 in a 1:2:2 stoichiometry. The complex interacts (via rix1)
CC       with mdn1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome
CC       particles (By similarity). Interacts with crb3/ipi3, gcr3 and Las1
CC       (PubMed:21385875). {ECO:0000250|UniProtKB:P38883,
CC       ECO:0000269|PubMed:21385875}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38883}.
CC   -!- SIMILARITY: Belongs to the RIX1/PELP1 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAB09765.1; -; Genomic_DNA.
DR   PIR; T41358; T41358.
DR   RefSeq; NP_587820.1; NM_001022813.2.
DR   AlphaFoldDB; P87243; -.
DR   SMR; P87243; -.
DR   BioGRID; 276104; 9.
DR   STRING; 4896.SPCC4G3.18.1; -.
DR   iPTMnet; P87243; -.
DR   MaxQB; P87243; -.
DR   PaxDb; P87243; -.
DR   PRIDE; P87243; -.
DR   EnsemblFungi; SPCC4G3.18.1; SPCC4G3.18.1:pep; SPCC4G3.18.
DR   GeneID; 2539542; -.
DR   KEGG; spo:SPCC4G3.18; -.
DR   PomBase; SPCC4G3.18; rix1.
DR   VEuPathDB; FungiDB:SPCC4G3.18; -.
DR   eggNOG; ENOG502QSEW; Eukaryota.
DR   HOGENOM; CLU_017323_0_0_1; -.
DR   InParanoid; P87243; -.
DR   OMA; LIRPRMP; -.
DR   PhylomeDB; P87243; -.
DR   Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:P87243; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0097344; C:Rix1 complex; IDA:PomBase.
DR   GO; GO:0006364; P:rRNA processing; IMP:PomBase.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012583; RIX1_N.
DR   Pfam; PF08167; RIX1; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; rRNA processing; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..828
FT                   /note="Pre-rRNA-processing protein rix1"
FT                   /id="PRO_0000343216"
FT   REGION          604..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  91996 MW;  0A40304CFCDE8C41 CRC64;
     MSDLLERGSL PLVKSWLAIT FANEEDLPFQ VPQIADILVH QKCIERLGTS ENALSVRKNW
     CTSLTKMLQS KDFRIRWSAI ILIHCTISQS WDCLVEHGAT WAKLLIALLN RPETPKTLEI
     AMITVSKMFS STVGRPAVTR ELVTPNLPTF VNNCLRIAES GKCLCTVCSC LYQGIISHSP
     TFRPFVSSIR NICIKILDGE EVVPSSLQKK AAVLYASLYR CVGKGNFEDY WKQSIISILK
     EYHLTLDFLF QFVIEPQTYP TREENLMFPK LKGHYEETYQ KALHRCRTLN LILISFLSTK
     TDKIVLLPIN ALKDLIQRVY TVQLSLPVKS VESSVQALLF MVLPHLHTLV NELTLKLFVV
     IPPAIILSFD SYLDSLNDCL LSESTHTGVL CSSLKLLSKF LDVTHMNVPL SKYENIVTLV
     LEYLANSSKG LASKSIEFSK NRGHSQKKRK TLSESQAGDT LMSSEESHQL YDSDVMDCCF
     SFLASILTHS IALPRLLRTK IDLCTLQISL SNPTSTVLIS MHNLLLASIL SPGDSQAVIV
     PHAIRIISGP LGLVHPDPLV ASHARSSMQT IESLIHPRFP PLQKHLSPSE FENTFESRFE
     PVSLENQSHI SPPQVDSQSE YKESSILAPS NPPFETESIT DSTEIEGIKE SFASTDTGLQ
     NNSTATSENK RSESELTMSN VLSNEGDRNE EGSEINSSQP STINHGTDHI NIVSENKETT
     VSLLHGDVEV EETTNVALNN SQDTETKFTA IDVDFVDRPT SVVSSQIENI NGDENGNTTS
     SVVETFEKTT DVVDEKTTSI NVEGNGEDDE EEDNISLPSI NLESDSDS