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Q03195 (RLI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Translation initiation factor RLI1
Alternative name(s):
ATP-binding cassette sub-family E member RLI1
RNase L inhibitor
Gene names
Name:RLI1
Ordered Locus Names:YDR091C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the multifactor complex (MFC) involved in translation initiation. Required for the binding of MFC to the 40S ribosome. Required for the processing and nuclear export of the 60S and 40S ribosomal subunits. Ref.6 Ref.7 Ref.8

Subunit structure

Component of the multifactor complex (MFC) composed of at least RLI1, the eIF2 subunit SUI2, TIF5/eIF5, and the eIF3 subunits PRT1, HCR1, NIP1, RPG1, TIF34 and TIF35. The complex associates with preinitiation complexes. Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasm. Nucleus. Note: Shuttles between the nucleus and the cytoplasm. Ref.4 Ref.6 Ref.7 Ref.8

Miscellaneous

Present with 6280 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCE family.

Contains 2 4Fe-4S ferredoxin-type domains.

Contains 2 ABC transporter domains.

Ontologies

Keywords
   Biological processProtein biosynthesis
Ribosome biogenesis
rRNA processing
Transport
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionInitiation factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity Ref.6. Source: GOC

cellular response to oxidative stress

Inferred from mutant phenotype PubMed 22855532. Source: SGD

positive regulation of translation

Inferred from mutant phenotype PubMed 24424461. Source: SGD

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

ribosomal large subunit biogenesis

Inferred from mutant phenotype Ref.6. Source: SGD

ribosomal subunit export from nucleus

Inferred from mutant phenotype Ref.8PubMed 22855532. Source: SGD

ribosome disassembly

Inferred from mutant phenotype PubMed 22770215. Source: SGD

translational initiation

Inferred from mutant phenotype Ref.6Ref.8. Source: SGD

translational termination

Inferred from genetic interaction PubMed 20062004. Source: SGD

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6Ref.8. Source: SGD

cytosolic ribosome

Inferred from direct assay Ref.6Ref.8. Source: SGD

nucleus

Inferred from direct assay Ref.6. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from sequence or structural similarity Ref.6. Source: SGD

iron ion binding

Inferred from direct assay Ref.8. Source: SGD

iron-sulfur cluster binding

Inferred from electronic annotation. Source: InterPro

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HCR1Q057754EBI-35146,EBI-8944
SUP35Q6Q7I02EBI-35146,EBI-7724365From a different organism.
SUP45P123855EBI-35146,EBI-6533

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 608608Translation initiation factor RLI1
PRO_0000268703

Regions

Domain7 – 39334Fe-4S ferredoxin-type 1
Domain46 – 75304Fe-4S ferredoxin-type 2
Domain70 – 320251ABC transporter 1
Domain345 – 568224ABC transporter 2
Nucleotide binding110 – 1178ATP Potential
Nucleotide binding385 – 3928ATP Potential

Amino acid modifications

Modified residue3491Phosphoserine Ref.10

Experimental info

Mutagenesis2241G → D: Lethal; when associated with D-225. Ref.6
Mutagenesis2251G → D: Lethal; when associated with D-224. Ref.6
Mutagenesis4701G → D: Lethal; when associated with D-471. Ref.6
Mutagenesis4711G → D: Lethal; when associated with D-470. Ref.6
Mutagenesis4931E → Q: Lethal. Inhibits translation in vitro. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q03195 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1E76EC3D0457963D

FASTA60868,340
        10         20         30         40         50         60 
MSDKNSRIAI VSADKCKPKK CRQECKRSCP VVKTGKLCIE VTPTSKIAFI SEILCIGCGI 

        70         80         90        100        110        120 
CVKKCPFDAI QIINLPTNLE AHVTHRYSAN SFKLHRLPTP RPGQVLGLVG TNGIGKSTAL 

       130        140        150        160        170        180 
KILAGKQKPN LGRFDDPPEW QEIIKYFRGS ELQNYFTKML EDDIKAIIKP QYVDNIPRAI 

       190        200        210        220        230        240 
KGPVQKVGEL LKLRMEKSPE DVKRYIKILQ LENVLKRDIE KLSGGELQRF AIGMSCVQEA 

       250        260        270        280        290        300 
DVYMFDEPSS YLDVKQRLNA AQIIRSLLAP TKYVICVEHD LSVLDYLSDF VCIIYGVPSV 

       310        320        330        340        350        360 
YGVVTLPASV REGINIFLDG HIPAENLRFR TEALQFRIAD ATEDLQNDSA SRAFSYPSLK 

       370        380        390        400        410        420 
KTQGDFVLNV EEGEFSDSEI LVMMGENGTG KTTLIKLLAG ALKPDEGQDI PKLNVSMKPQ 

       430        440        450        460        470        480 
KIAPKFPGTV RQLFFKKIRG QFLNPQFQTD VVKPLRIDDI IDQEVQHLSG GELQRVAIVL 

       490        500        510        520        530        540 
ALGIPADIYL IDEPSAYLDS EQRIICSKVI RRFILHNKKT AFIVEHDFIM ATYLADKVIV 

       550        560        570        580        590        600 
FEGIPSKNAH ARAPESLLTG CNRFLKNLNV TFRRDPNSFR PRINKLDSQM DKEQKSSGNY 


FFLDNTGI 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly."
Dong J., Lai R., Nielsen K., Fekete C.A., Qiu H., Hinnebusch A.G.
J. Biol. Chem. 279:42157-42168(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE MFC COMPLEX, MUTAGENESIS OF GLY-224; GLY-225; GLY-470; GLY-471 AND GLU-493, SUBCELLULAR LOCATION.
[7]"Functional link between ribosome formation and biogenesis of iron-sulfur proteins."
Yarunin A., Panse V.G., Petfalski E., Dez C., Tollervey D., Hurt E.C.
EMBO J. 24:580-588(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH PRE-RIBOSOMAL PARTICLES, IDENTIFICATION IN THE MFC COMPLEX.
[8]"Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria."
Kispal G., Sipos K., Lange H., Fekete Z., Bedekovics T., Janaky T., Bassler J., Aguilar Netz D.J., Balk J., Rotte C., Lill R.
EMBO J. 24:589-598(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ASSOCIATION WITH PRE-RIBOSOMAL PARTICLES, IDENTIFICATION IN THE MFC COMPLEX.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z50111 Genomic DNA. Translation: CAA90450.1.
AY723776 Genomic DNA. Translation: AAU09693.1.
BK006938 Genomic DNA. Translation: DAA11938.1.
PIRS58091.
RefSeqNP_010376.3. NM_001180399.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J16electron microscopy-B1-608[»]
ProteinModelPortalQ03195.
SMRQ03195. Positions 4-603.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32148. 116 interactions.
DIPDIP-4492N.
IntActQ03195. 42 interactions.
MINTMINT-472764.
STRING4932.YDR091C.

Proteomic databases

PaxDbQ03195.
PeptideAtlasQ03195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR091C; YDR091C; YDR091C.
GeneID851665.
KEGGsce:YDR091C.

Organism-specific databases

CYGDYDR091c.
SGDS000002498. RLI1.

Phylogenomic databases

eggNOGCOG1245.
GeneTreeENSGT00390000015089.
HOGENOMHOG000222803.
KOK06174.
OMALRFRTES.
OrthoDBEOG7G1VFV.

Enzyme and pathway databases

BioCycYEAST:G3O-29696-MONOMER.

Gene expression databases

GenevestigatorQ03195.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR003593. AAA+_ATPase.
IPR013283. ABC_E.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
IPR007209. RNaseL-inhib_metal-bd_dom.
[Graphical view]
PfamPF00005. ABC_tran. 2 hits.
PF00037. Fer4. 1 hit.
PF04068. RLI. 1 hit.
[Graphical view]
PRINTSPR01868. ABCEFAMILY.
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio969280.
PROQ03195.

Entry information

Entry nameRLI1_YEAST
AccessionPrimary (citable) accession number: Q03195
Secondary accession number(s): D6VS78
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references