ACL4_YEAST
ID ACL4_YEAST Reviewed; 387 AA.
AC Q03771; D6VSE1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Assembly chaperone of RPL4 {ECO:0000303|PubMed:25936803};
GN Name=ACL4 {ECO:0000303|PubMed:25936803};
GN OrderedLocusNames=YDR161W {ECO:0000312|SGD:S000002568};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
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 [3]
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 [4]
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 [5]
RP IDENTIFICATION BY 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RPL4A AND RPL4B.
RX PubMed=25936803; DOI=10.1016/j.molcel.2015.03.029;
RA Stelter P., Huber F.M., Kunze R., Flemming D., Hoelz A., Hurt E.;
RT "Coordinated ribosomal L4 protein assembly into the pre-ribosome is
RT regulated by its eukaryote-specific extension.";
RL Mol. Cell 58:854-862(2015).
CC -!- FUNCTION: Acts as a chaperone for the L4 ribosomal subunit encoded by
CC RPL4A and PRPL4B, required for hierarchical ribosome assembly. Shields
CC ribosomal protein L4 until timely release and insertion into the pre-
CC ribosome is possible, once ribosomal protein L18 is present.
CC {ECO:0000269|PubMed:25936803}.
CC -!- SUBUNIT: Interacts with RPL4A and RPL4B. {ECO:0000269|PubMed:25936803}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:25936803}. Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:25936803}. Note=Distributed throughout the cell but
CC is enriched in the nucleus. {ECO:0000269|PubMed:25936803}.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ACL4 family. {ECO:0000305}.
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DR EMBL; Z50046; CAA90381.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12001.1; -; Genomic_DNA.
DR PIR; S57985; S57985.
DR RefSeq; NP_010445.1; NM_001180468.1.
DR AlphaFoldDB; Q03771; -.
DR SMR; Q03771; -.
DR BioGRID; 32212; 262.
DR IntAct; Q03771; 35.
DR STRING; 4932.YDR161W; -.
DR iPTMnet; Q03771; -.
DR MaxQB; Q03771; -.
DR PaxDb; Q03771; -.
DR PRIDE; Q03771; -.
DR EnsemblFungi; YDR161W_mRNA; YDR161W; YDR161W.
DR GeneID; 851739; -.
DR KEGG; sce:YDR161W; -.
DR SGD; S000002568; ACL4.
DR VEuPathDB; FungiDB:YDR161W; -.
DR eggNOG; ENOG502QSAH; Eukaryota.
DR HOGENOM; CLU_061203_0_0_1; -.
DR InParanoid; Q03771; -.
DR OMA; CIEMGLY; -.
DR BioCyc; YEAST:G3O-29751-MON; -.
DR PRO; PR:Q03771; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03771; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0140318; F:protein transporter activity; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; HGI:SGD.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Ribosome biogenesis; TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..387
FT /note="Assembly chaperone of RPL4"
FT /id="PRO_0000253808"
FT REPEAT 42..75
FT /note="TPR 1"
FT REPEAT 163..196
FT /note="TPR 2"
FT REPEAT 224..257
FT /note="TPR 3"
FT REGION 363..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 387 AA; 42943 MW; 539F5C1AB133614E CRC64;
MSELEATIRQ AKEALAENNA KKALKILKPF KSSLKKENAN NVILNEVFAD AYLDNGQVEK
AYPILARACE LDPEGQVGGP DKFFTMGQIM GGQDGVSIIT RGIMNISNTG GEMLTNVQVE
KIVGGLLSVI EIWMTDLCME PNAEEQCEEL IQKAMELTEG KSPETWSTLG SIKISQQKFG
EAYEAFSQAW NFFELKKQEI GSGINENGDT TQKAGLQSEY VDLLQPLLSL TKMCLEVGAY
EVALKVIAAV RDIDEDNIEG YYLEGFTYYL MSKLEIFKLN NPEVSLRPEN IYEFNQLIQE
VPLDLSHEPI SQLIYDSRLA LSFALQAGVN ADSKDEIVQE LLGGANALLQ EIGGPLDPSE
LTQIKKGDLV NENEDLEELD IEEEYSD
