REI1_SCHPO
ID REI1_SCHPO Reviewed; 463 AA.
AC O59811;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cytoplasmic 60S subunit biogenesis factor SPCC550.15c;
DE AltName: Full=pre-60S factor REI1 homolog;
GN ORFNames=SPCC550.15c;
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-150 AND SER-155, 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).
CC -!- FUNCTION: Pre-60S-associated factor involved in the cytoplasmic
CC maturation of the 60S subunit. Involved in the dissociation and
CC recycling of other late pre-60S factors before newly synthesized large
CC ribosomal subunits enter translation (By similarity).
CC {ECO:0000250|UniProtKB:P38344}.
CC -!- SUBUNIT: Associates with nascent pre-60S particles that have not yet
CC entered the translating pool, and is released from mature 60S subunits.
CC {ECO:0000250|UniProtKB:P38344}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the REI1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA19119.1; -; Genomic_DNA.
DR PIR; T41390; T41390.
DR RefSeq; NP_588107.1; NM_001023098.2.
DR AlphaFoldDB; O59811; -.
DR BioGRID; 276124; 17.
DR STRING; 4896.SPCC550.15c.1; -.
DR iPTMnet; O59811; -.
DR MaxQB; O59811; -.
DR PaxDb; O59811; -.
DR PRIDE; O59811; -.
DR EnsemblFungi; SPCC550.15c.1; SPCC550.15c.1:pep; SPCC550.15c.
DR GeneID; 2539563; -.
DR KEGG; spo:SPCC550.15c; -.
DR PomBase; SPCC550.15c; -.
DR VEuPathDB; FungiDB:SPCC550.15c; -.
DR eggNOG; KOG2785; Eukaryota.
DR HOGENOM; CLU_018787_1_0_1; -.
DR InParanoid; O59811; -.
DR OMA; YAEYYDY; -.
DR PhylomeDB; O59811; -.
DR PRO; PR:O59811; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISO:PomBase.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:PomBase.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR040025; Znf622/Rei1/Reh1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13182; PTHR13182; 1.
DR Pfam; PF12756; zf-C2H2_2; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; Zinc; Zinc-finger.
FT CHAIN 1..463
FT /note="Cytoplasmic 60S subunit biogenesis factor
FT SPCC550.15c"
FT /id="PRO_0000310843"
FT ZN_FING 5..30
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 70..94
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 208..231
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 259..283
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 109..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..339
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 463 AA; 52251 MW; B9EF7ED9910AE9A9 CRC64;
MSTSFACTTC TVAFNNAESQ KIHWKSDWHH YNLKRKVASL PPLSAEVFAG KILSIQKQNE
EVQKKAEFYQ NCEVCNKKFY SEGAYSSHMA SKKHRDNLSK FQRNSRIKKL QSEDASSIAS
STLSMGEPVV DSEIEEEEDL ASQLTSRAIS LSNLSLHGRE SEPSKTELAT SIPQSNEASK
SHLFTQEPTP EEIEAELARR SSQRLSPRDC LFCAASFSSF DTCKKHMKAS HSLYIPEREY
LVDEPSLFDY LAEKISIGFT CLTCNREFKS LEAVRAHMQQ KGHTSIAYDT EDEQLELSDF
YDFTTSYPDY AVKQDETVVE EDGSSGEGDW EDVSDDSDNS SLDSLEMGRV PIADEYELHL
PSGNRVGHRS LSRYFRQNLH SSSTAVGDGA SIHQNVARRA MSGNARAYRQ AVETSIAGVR
DGRKNYSASH IKSFQDQRRR EEFANKMGIK NNTKKHFRDA LLQ
