IPI3_SCHPO
ID IPI3_SCHPO Reviewed; 446 AA.
AC Q10272;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pre-rRNA-processing protein crb3/ipi3;
GN Name=crb3; Synonyms=ipi3; ORFNames=SPAC13G7.08c;
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].
RX PubMed=9407031; DOI=10.1101/gad.11.24.3387;
RA Saka Y., Esashi F., Matsusaka T., Mochida S., Yanagida M.;
RT "Damage and replication checkpoint control in fission yeast is ensured by
RT interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1.";
RL Genes Dev. 11:3387-3400(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RIX1, 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: Required for both pre-rRNA processing and heterochromatic
CC gene silencing. {ECO:0000269|PubMed:21385875}.
CC -!- FUNCTION: Component of the RIX1 complex required for processing of ITS2
CC sequences from 35S pre-rRNA. {ECO:0000250|UniProtKB:P53877}.
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 rix1, gcr3 and Las1
CC (PubMed:21385875). {ECO:0000250|UniProtKB:P53877,
CC ECO:0000269|PubMed:21385875}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21385875}. Chromosome
CC {ECO:0000269|PubMed:21385875}.
CC -!- SIMILARITY: Belongs to the WD repeat IPI3/WDR18 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB008572; BAA23358.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93596.1; -; Genomic_DNA.
DR PIR; T37658; S67437.
DR RefSeq; NP_593710.1; NM_001019141.2.
DR AlphaFoldDB; Q10272; -.
DR SMR; Q10272; -.
DR BioGRID; 279290; 10.
DR IntAct; Q10272; 3.
DR MINT; Q10272; -.
DR STRING; 4896.SPAC13G7.08c.1; -.
DR MaxQB; Q10272; -.
DR PaxDb; Q10272; -.
DR EnsemblFungi; SPAC13G7.08c.1; SPAC13G7.08c.1:pep; SPAC13G7.08c.
DR GeneID; 2542844; -.
DR KEGG; spo:SPAC13G7.08c; -.
DR PomBase; SPAC13G7.08c; crb3.
DR VEuPathDB; FungiDB:SPAC13G7.08c; -.
DR eggNOG; KOG0646; Eukaryota.
DR HOGENOM; CLU_619884_0_0_1; -.
DR InParanoid; Q10272; -.
DR OMA; VNARIYT; -.
DR PhylomeDB; Q10272; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q10272; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0097344; C:Rix1 complex; IDA:PomBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; ISO:PomBase.
DR GO; GO:0006364; P:rRNA processing; IMP:PomBase.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR045227; WDR18/Ipi3/RID3.
DR PANTHER; PTHR18763; PTHR18763; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Chromosome; Nucleus; Reference proteome; Repeat; Ribosome biogenesis;
KW rRNA processing; Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..446
FT /note="Pre-rRNA-processing protein crb3/ipi3"
FT /id="PRO_0000050942"
FT REPEAT 74..113
FT /note="WD 1"
FT REPEAT 116..155
FT /note="WD 2"
FT REPEAT 172..214
FT /note="WD 3"
FT REPEAT 216..257
FT /note="WD 4"
FT REPEAT 294..333
FT /note="WD 5"
SQ SEQUENCE 446 AA; 49506 MW; 4C426880926401A1 CRC64;
MELLLSGCEA IEGEPSNVLC HNLHTGTLVS TFRQSSPAKN ATCTTLNHLL SAQHTRPQLN
IHNFGKEILD QSIILPEILI CVQSSPCGSW LAAGTEKGNL YIWSLKSGAL IYFFRAHYQP
LTILKFSNDG MVLFTASNDG DVFAWLISTL VDQNSTFETS NSSVKAISHF SGHKRSIVSM
EIGPGPIVSG RLYTASEDNT IRIWDVSTGN LLTTIALPST PSCMTVDPSE RVVYVGNEKG
IIWIPLYTGS STFSNNVKEK KRVTSVDNTT IPNAIGGMGR VVDYNDSRES SIISCQSPIT
TLTVSFDASL LISGDKDGNV LVWDSVSRQV LRRLVQYYSP VSFLQCKVDK ISFYSNSSLS
FPVLKRMITN EYLNSDVRIC IQDDGVEQLM QPENILKISS DIVTQGSESS WRAKAETSEM
QLKEAKRLFY ELKQIHQALW EKYLQK
