Q03195 (RLI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	608 AA.
Sequence status	Complete.
Protein existence	Evidence 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 pre-initiation complexes.
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. Ref.5
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 process	Protein biosynthesis Ribosome biogenesis Transport rRNA processing
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	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.8. Source: SGD translational termination Inferred from genetic interaction. Source: SGD
Cellular component	cytosolic ribosome Inferred from direct assay Ref.6Ref.8. Source: SGD nucleus Inferred from direct assay Ref.6. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 608	608	Translation initiation factor RLI1		PRO_0000268703
Regions
	Domain	7 – 39	33	4Fe-4S ferredoxin-type 1
	Domain	46 – 75	30	4Fe-4S ferredoxin-type 2
	Domain	70 – 320	251	ABC transporter 1
	Domain	345 – 568	224	ABC transporter 2
	Nucleotide binding	110 – 117	8	ATP Potential
	Nucleotide binding	385 – 392	8	ATP Potential
Amino acid modifications
	Modified residue	342	1	Phosphothreonine Ref.9
	Modified residue	349	1	Phosphoserine Ref.9
	Modified residue	351	1	Phosphoserine Ref.9
Experimental info
	Mutagenesis	224	1	G → D: Lethal; when associated with D-225. Ref.6
	Mutagenesis	225	1	G → D: Lethal; when associated with D-224. Ref.6
	Mutagenesis	470	1	G → D: Lethal; when associated with D-471. Ref.6
	Mutagenesis	471	1	G → D: Lethal; when associated with D-470. Ref.6
	Mutagenesis	493	1	E → Q: Lethal. Inhibits translation in vitro. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q03195 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1E76EC3D0457963D	FASTA	608	68,340
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 9169867] [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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [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: 14562095] [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: 14562106] [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: 15277527] [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: 15660135] [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: 15660134] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, 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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-342; SER-349 AND SER-351, MASS SPECTROMETRY.
+	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.
PIR	S58091.
RefSeq	NP_010376.1. NM_001180399.1.
3D structure databases
HSSP	HSSP built from PDB template 1XMI based on UniProtKB P13569.
ProteinModelPortal	Q03195.
SMR	Q03195. Positions 4-602.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4492N.
IntAct	Q03195. 32 interactions.
MINT	MINT-472764.
STRING	Q03195.
Proteomic databases
PeptideAtlas	Q03195.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR091C; YDR091C; YDR091C.
GeneID	851665.
KEGG	sce:YDR091C.
NMPDR	fig|4932.3.peg.1122.
Organism-specific databases
CYGD	YDR091c.
SGD	S000002498. RLI1.
Phylogenomic databases
eggNOG	fuNOG04166.
GeneTree	EFGT00050000001689.
HOGENOM	HBG297745.
OMA	TENMRFR.
OrthoDB	EOG4NW2TF.
Gene expression databases
ArrayExpress	Q03195.
Genevestigator	Q03195.
GermOnline	YDR091C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR013283. ABC_E. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR003593. ATPase_AAA+_core. IPR007209. RNaseL-inhib_metal-bd_dom. [Graphical view]
KO	K06174.
Pfam	PF00005. ABC_tran. 2 hits. PF00037. Fer4. 1 hit. PF04068. RLI. 1 hit. [Graphical view]
PRINTS	PR01868. ABCEFAMILY.
SMART	SM00382. AAA. 2 hits. [Graphical view]
PROSITE	PS00198. 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]
ProtoNet	Search...
Other
NextBio	969280.

Entry information

Entry name

RLI1_YEAST

Accession

Primary (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:	December 14, 2011
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program