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Database: UniProt
Entry: Q03195
LinkDB: Q03195
Original site: Q03195 
ID   RLI1_YEAST              Reviewed;         608 AA.
AC   Q03195; D6VS78;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-FEB-2019, entry version 169.
DE   RecName: Full=Translation initiation factor RLI1;
DE   AltName: Full=ATP-binding cassette sub-family E member RLI1;
DE   AltName: Full=RNase L inhibitor;
GN   Name=RLI1; OrderedLocusNames=YDR091C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
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   [5]
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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, IDENTIFICATION IN THE MFC COMPLEX, MUTAGENESIS OF GLY-224;
RP   GLY-225; GLY-470; GLY-471 AND GLU-493, AND SUBCELLULAR LOCATION.
RX   PubMed=15277527; DOI=10.1074/jbc.M404502200;
RA   Dong J., Lai R., Nielsen K., Fekete C.A., Qiu H., Hinnebusch A.G.;
RT   "The essential ATP-binding cassette protein RLI1 functions in
RT   translation by promoting preinitiation complex assembly.";
RL   J. Biol. Chem. 279:42157-42168(2004).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH PRE-RIBOSOMAL
RP   PARTICLES, AND IDENTIFICATION IN THE MFC COMPLEX.
RX   PubMed=15660135; DOI=10.1038/sj.emboj.7600540;
RA   Yarunin A., Panse V.G., Petfalski E., Dez C., Tollervey D., Hurt E.C.;
RT   "Functional link between ribosome formation and biogenesis of iron-
RT   sulfur proteins.";
RL   EMBO J. 24:580-588(2005).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP   ASSOCIATION WITH PRE-RIBOSOMAL PARTICLES, AND IDENTIFICATION IN THE
RP   MFC COMPLEX.
RX   PubMed=15660134; DOI=10.1038/sj.emboj.7600541;
RA   Kispal G., Sipos K., Lange H., Fekete Z., Bedekovics T., Janaky T.,
RA   Bassler J., Aguilar Netz D.J., Balk J., Rotte C., Lill R.;
RT   "Biogenesis of cytosolic ribosomes requires the essential iron-sulphur
RT   protein Rli1p and mitochondria.";
RL   EMBO J. 24:589-598(2005).
RN   [9]
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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION
RP   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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   INTERACTION WITH YAE1, AND MUTAGENESIS OF CYS-25.
RX   PubMed=23318452; DOI=10.1038/onc.2012.604;
RA   Zhai C., Li Y., Mascarenhas C., Lin Q., Li K., Vyrides I., Grant C.M.,
RA   Panaretou B.;
RT   "The function of ORAOV1/LTO1, a gene that is overexpressed frequently
RT   in cancer: essential roles in the function and biogenesis of the
RT   ribosome.";
RL   Oncogene 33:484-494(2014).
RN   [12]
RP   INTERACTION WITH YAE1, AND MUTAGENESIS OF CYS-25 AND CYS-61.
RX   PubMed=26182403; DOI=10.7554/eLife.08231;
RA   Paul V.D., Muehlenhoff U., Stuempfig M., Seebacher J., Kugler K.G.,
RA   Renicke C., Taxis C., Gavin A.C., Pierik A.J., Lill R.;
RT   "The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the
RT   ABC protein Rli1 for iron-sulfur cluster insertion.";
RL   Elife 4:E08231-E08231(2015).
CC   -!- FUNCTION: Component of the multifactor complex (MFC) involved in
CC       translation initiation. Required for the binding of MFC to the 40S
CC       ribosome. Required for the processing and nuclear export of the
CC       60S and 40S ribosomal subunits. {ECO:0000269|PubMed:15277527,
CC       ECO:0000269|PubMed:15660134, ECO:0000269|PubMed:15660135}.
CC   -!- SUBUNIT: Component of the multifactor complex (MFC) composed of at
CC       least RLI1, the eIF2 subunit SUI2, TIF5/eIF5, and the eIF3
CC       subunits PRT1, HCR1, NIP1, RPG1, TIF34 and TIF35. The complex
CC       associates with pre-initiation complexes. Interacts with the
CC       complex YAE1:LTO1; the complex bridges the interaction between the
CC       CIA complex and RLI1 (PubMed:23318452).
CC       {ECO:0000269|PubMed:15277527, ECO:0000269|PubMed:15660134,
CC       ECO:0000269|PubMed:15660135, ECO:0000269|PubMed:23318452}.
CC   -!- INTERACTION:
CC       Q05775:HCR1; NbExp=4; IntAct=EBI-35146, EBI-8944;
CC       Q6Q7I0:SUP35 (xeno); NbExp=2; IntAct=EBI-35146, EBI-7724365;
CC       P12385:SUP45; NbExp=5; IntAct=EBI-35146, EBI-6533;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15277527, ECO:0000269|PubMed:15660134,
CC       ECO:0000269|PubMed:15660135}. Nucleus
CC       {ECO:0000269|PubMed:15277527, ECO:0000269|PubMed:15660134,
CC       ECO:0000269|PubMed:15660135}. Note=Shuttles between the nucleus
CC       and the cytoplasm. {ECO:0000269|PubMed:15660134,
CC       ECO:0000269|PubMed:15660135}.
CC   -!- MISCELLANEOUS: Present with 6280 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE
CC       family. {ECO:0000305}.
DR   EMBL; Z50111; CAA90450.1; -; Genomic_DNA.
DR   EMBL; AY723776; AAU09693.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11938.1; -; Genomic_DNA.
DR   PIR; S58091; S58091.
DR   RefSeq; NP_010376.3; NM_001180399.3.
DR   PDB; 3J16; EM; -; B=1-608.
DR   PDB; 4CRM; EM; 8.75 A; P=1-608.
DR   PDB; 5LL6; EM; 3.90 A; h=1-608.
DR   PDBsum; 3J16; -.
DR   PDBsum; 4CRM; -.
DR   PDBsum; 5LL6; -.
DR   ProteinModelPortal; Q03195; -.
DR   SMR; Q03195; -.
DR   BioGrid; 32148; 181.
DR   DIP; DIP-4492N; -.
DR   IntAct; Q03195; 44.
DR   MINT; Q03195; -.
DR   STRING; 4932.YDR091C; -.
DR   iPTMnet; Q03195; -.
DR   MaxQB; Q03195; -.
DR   PaxDb; Q03195; -.
DR   PRIDE; Q03195; -.
DR   TopDownProteomics; Q03195; -.
DR   EnsemblFungi; YDR091C_mRNA; YDR091C_mRNA; YDR091C.
DR   GeneID; 851665; -.
DR   KEGG; sce:YDR091C; -.
DR   EuPathDB; FungiDB:YDR091C; -.
DR   SGD; S000002498; RLI1.
DR   GeneTree; ENSGT00390000015089; -.
DR   HOGENOM; HOG000222803; -.
DR   InParanoid; Q03195; -.
DR   KO; K06174; -.
DR   OMA; GQYFFLE; -.
DR   BioCyc; YEAST:G3O-29696-MONOMER; -.
DR   PRO; PR:Q03195; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATPase activity; ISS:SGD.
DR   GO; GO:0005506; F:iron ion binding; IDA:SGD.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:UniProtKB.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:SGD.
DR   GO; GO:0032790; P:ribosome disassembly; IDA:SGD.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006413; P:translational initiation; IMP:SGD.
DR   GO; GO:0006415; P:translational termination; IGI:SGD.
DR   CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013283; RLI1.
DR   InterPro; IPR034348; RLI_dom_1.
DR   InterPro; IPR007209; RNaseL-inhib_metal-bd_dom.
DR   PANTHER; PTHR19248; PTHR19248; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF04068; RLI; 1.
DR   PRINTS; PR01868; ABCEFAMILY.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm;
KW   Initiation factor; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome; Repeat; Ribosome biogenesis;
KW   rRNA processing; Transport.
FT   CHAIN         1    608       Translation initiation factor RLI1.
FT                                /FTId=PRO_0000268703.
FT   DOMAIN        7     39       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       46     75       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       70    320       ABC transporter 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   DOMAIN      345    568       ABC transporter 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   NP_BIND     110    117       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   NP_BIND     385    392       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   MOD_RES     349    349       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MUTAGEN      25     25       C->S: Not viable in aerobic conditions.
FT                                Lethal; when associated with S-61.
FT                                {ECO:0000269|PubMed:23318452,
FT                                ECO:0000269|PubMed:26182403}.
FT   MUTAGEN      61     61       C->S: Lethal; when associated with S-25.
FT                                {ECO:0000269|PubMed:26182403}.
FT   MUTAGEN     224    224       G->D: Lethal; when associated with D-225.
FT                                {ECO:0000269|PubMed:15277527}.
FT   MUTAGEN     225    225       G->D: Lethal; when associated with D-224.
FT                                {ECO:0000269|PubMed:15277527}.
FT   MUTAGEN     470    470       G->D: Lethal; when associated with D-471.
FT                                {ECO:0000269|PubMed:15277527}.
FT   MUTAGEN     471    471       G->D: Lethal; when associated with D-470.
FT                                {ECO:0000269|PubMed:15277527}.
FT   MUTAGEN     493    493       E->Q: Lethal. Inhibits translation in
FT                                vitro. {ECO:0000269|PubMed:15277527}.
SQ   SEQUENCE   608 AA;  68340 MW;  1E76EC3D0457963D CRC64;
     MSDKNSRIAI VSADKCKPKK CRQECKRSCP VVKTGKLCIE VTPTSKIAFI SEILCIGCGI
     CVKKCPFDAI QIINLPTNLE AHVTHRYSAN SFKLHRLPTP RPGQVLGLVG TNGIGKSTAL
     KILAGKQKPN LGRFDDPPEW QEIIKYFRGS ELQNYFTKML EDDIKAIIKP QYVDNIPRAI
     KGPVQKVGEL LKLRMEKSPE DVKRYIKILQ LENVLKRDIE KLSGGELQRF AIGMSCVQEA
     DVYMFDEPSS YLDVKQRLNA AQIIRSLLAP TKYVICVEHD LSVLDYLSDF VCIIYGVPSV
     YGVVTLPASV REGINIFLDG HIPAENLRFR TEALQFRIAD ATEDLQNDSA SRAFSYPSLK
     KTQGDFVLNV EEGEFSDSEI LVMMGENGTG KTTLIKLLAG ALKPDEGQDI PKLNVSMKPQ
     KIAPKFPGTV RQLFFKKIRG QFLNPQFQTD VVKPLRIDDI IDQEVQHLSG GELQRVAIVL
     ALGIPADIYL IDEPSAYLDS EQRIICSKVI RRFILHNKKT AFIVEHDFIM ATYLADKVIV
     FEGIPSKNAH ARAPESLLTG CNRFLKNLNV TFRRDPNSFR PRINKLDSQM DKEQKSSGNY
     FFLDNTGI
//
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