REI1_YEAST
ID REI1_YEAST Reviewed; 393 AA.
AC P38344; D6VQR3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cytoplasmic 60S subunit biogenesis factor REI1;
DE AltName: Full=Required for isotropic bud growth protein 1;
DE AltName: Full=pre-60S factor REI1;
GN Name=REI1; OrderedLocusNames=YBR267W; ORFNames=YBR1736;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Aigle M., Baclet M.C., Barthe C., Biteau N., Crouzet M., Doignon F.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 152-153.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP DOMAIN.
RX PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA Boehm S., Frishman D., Mewes H.-W.;
RT "Variations of the C2H2 zinc finger motif in the yeast genome and
RT classification of yeast zinc finger proteins.";
RL Nucleic Acids Res. 25:2464-2469(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15107529; DOI=10.1247/csf.29.1;
RA Iwase M., Toh-e A.;
RT "Ybr267w is a new cytoplasmic protein belonging to the mitotic signaling
RT network of Saccharomyces cerevisiae.";
RL Cell Struct. Funct. 29:1-15(2004).
RN [9]
RP FUNCTION, INTERACTION WITH RPL24, AND ASSOCIATION WITH PRE-60S PARTICLES.
RX PubMed=16651379; DOI=10.1083/jcb.200510080;
RA Lebreton A., Saveanu C., Decourty L., Rain J.-C., Jacquier A.,
RA Fromont-Racine M.;
RT "A functional network involved in the recycling of nucleocytoplasmic pre-
RT 60S factors.";
RL J. Cell Biol. 173:349-360(2006).
RN [10]
RP FUNCTION, INTERACTION WITH ARX1, AND ASSOCIATION WITH PRE-60S PARTICLES.
RX PubMed=16648468; DOI=10.1128/mcb.26.10.3718-3727.2006;
RA Hung N.J., Johnson A.W.;
RT "Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1
RT depends on Rei1 in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 26:3718-3727(2006).
RN [11]
RP FUNCTION.
RX PubMed=17652132; DOI=10.1261/rna.585007;
RA Demoinet E., Jacquier A., Lutfalla G., Fromont-Racine M.;
RT "The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling
RT of preribosomal factors in Saccharomyces cerevisiae.";
RL RNA 13:1570-1581(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP FUNCTION, AND ASSOCIATION WITH PRE-60S PARTICLES.
RX PubMed=19433447; DOI=10.1128/mcb.01582-08;
RA Parnell K.M., Bass B.L.;
RT "Functional redundancy of yeast proteins Reh1 and Rei1 in cytoplasmic 60S
RT subunit maturation.";
RL Mol. Cell. Biol. 29:4014-4023(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH JJJ1.
RX PubMed=19901025; DOI=10.1074/jbc.m109.038349;
RA Meyer A.E., Hoover L.A., Craig E.A.;
RT "The cytosolic J-protein, Jjj1, and Rei1 function in the removal of the
RT pre-60 S subunit factor Arx1.";
RL J. Biol. Chem. 285:961-968(2010).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY, FUNCTION, AND INTERACTION WITH ARX1.
RX PubMed=23142985; DOI=10.1038/nsmb.2425;
RA Greber B.J., Boehringer D., Montellese C., Ban N.;
RT "Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to
RT the 60S ribosomal subunit.";
RL Nat. Struct. Mol. Biol. 19:1228-1233(2012).
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 like ARX1, TIF6 and ALB1 before
CC newly synthesized large ribosomal subunits enter translation.
CC Cooperates with the co-chaperone JJJ1 in the release of the nuclear-
CC export factor ARX1. May act redundantly with REH1 to directly promote a
CC stabilizing structural rearrangement in cytoplasmic 60S subunit
CC maturation independent on ARX1 recycling. {ECO:0000269|PubMed:15107529,
CC ECO:0000269|PubMed:16648468, ECO:0000269|PubMed:16651379,
CC ECO:0000269|PubMed:17652132, ECO:0000269|PubMed:19433447,
CC ECO:0000269|PubMed:19901025, ECO:0000269|PubMed:23142985}.
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 Interacts with pre-60S factors ARX1 and RPL24. Interacts with JJJ1.
CC {ECO:0000269|PubMed:16648468, ECO:0000269|PubMed:16651379,
CC ECO:0000269|PubMed:19901025, ECO:0000269|PubMed:23142985}.
CC -!- INTERACTION:
CC P38344; Q03862: ARX1; NbExp=5; IntAct=EBI-21136, EBI-31385;
CC P38344; P53863: JJJ1; NbExp=6; IntAct=EBI-21136, EBI-29183;
CC P38344; P53145: LSG1; NbExp=5; IntAct=EBI-21136, EBI-23885;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15107529}.
CC -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the REI1 family. {ECO:0000305}.
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DR EMBL; X70529; CAA49931.1; -; Genomic_DNA.
DR EMBL; Z36135; CAA85229.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07383.2; -; Genomic_DNA.
DR PIR; S77691; S77691.
DR RefSeq; NP_009825.4; NM_001178615.4.
DR PDB; 5APN; EM; 3.91 A; y=1-393.
DR PDB; 6RZZ; EM; 3.20 A; u=1-393.
DR PDBsum; 5APN; -.
DR PDBsum; 6RZZ; -.
DR AlphaFoldDB; P38344; -.
DR SMR; P38344; -.
DR BioGRID; 32962; 456.
DR DIP; DIP-6347N; -.
DR IntAct; P38344; 13.
DR MINT; P38344; -.
DR STRING; 4932.YBR267W; -.
DR iPTMnet; P38344; -.
DR SWISS-2DPAGE; P38344; -.
DR MaxQB; P38344; -.
DR PaxDb; P38344; -.
DR PRIDE; P38344; -.
DR EnsemblFungi; YBR267W_mRNA; YBR267W; YBR267W.
DR GeneID; 852569; -.
DR KEGG; sce:YBR267W; -.
DR SGD; S000000471; REI1.
DR VEuPathDB; FungiDB:YBR267W; -.
DR eggNOG; KOG2785; Eukaryota.
DR GeneTree; ENSGT00390000018047; -.
DR HOGENOM; CLU_018787_1_1_1; -.
DR InParanoid; P38344; -.
DR OMA; YAEYYDY; -.
DR BioCyc; YEAST:G3O-29188-MON; -.
DR PRO; PR:P38344; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38344; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007117; P:budding cell bud growth; IGI:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IGI:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
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; 3.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Ribosome biogenesis; Zinc; Zinc-finger.
FT CHAIN 1..393
FT /note="Cytoplasmic 60S subunit biogenesis factor REI1"
FT /id="PRO_0000202529"
FT ZN_FING 7..31
FT /note="C2H2-type 1"
FT ZN_FING 162..187
FT /note="C2H2-type 2"
FT ZN_FING 215..239
FT /note="C2H2-type 3"
FT REGION 55..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..293
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 152..153
FT /note="KL -> NV (in Ref. 1; CAA49931 and 2; CAA85229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 45862 MW; D01AA8FFDF4A0BAC CRC64;
MSSSGVYTCN SCVLTFDSSD EQRAHMKSDW HRYNLKRRVA QLPPISFETF DSKVSAAAAS
TSKSAEKEKP VTKKELKRRE KQALLEKKKK LLEIARANML ENMQKSQEGN TPDLSKLSLQ
ENEENKEKEE PKKEEPEQLT EEEMAERVMQ EKLRNRVDIP LEQCLFCEHN KHFKDVEENL
EHMFRTHGFY IPEQKYLVDK IGLVKYMSEK IGLGNICIVC NYQGRTLTAV RQHMLAKRHC
KIPYESEDER LEISEFYDFT SSYANFNSNT TPDNEDDWED VGSDEAGSDD EDLPQEYLYN
DGIELHLPTG IKVGHRSLQR YYKQDLKPEV ILTEGQGTLV AAETRSFLPA FDKKGVQTQQ
RVWQTERFDK KRLDKRSAKF VNNQPHYRDQ LLQ
