IML2_YEAST
ID IML2_YEAST Reviewed; 731 AA.
AC P47031; D6VWA1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Inclusion body clearance protein IML2 {ECO:0000305|PubMed:26004510};
DE AltName: Full=Increased minichromosome loss protein 2 {ECO:0000303|PubMed:10628851};
GN Name=IML2 {ECO:0000303|PubMed:10628851};
GN OrderedLocusNames=YJL082W {ECO:0000312|SGD:S000003618}; ORFNames=J1007;
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=7483841; DOI=10.1002/yea.320110709;
RA Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT cerevisiae chromosome X, including putative proteins with leucine zippers,
RT a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT alpha 2 binding site.";
RL Yeast 11:681-689(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
RP GENE NAME.
RX PubMed=10628851; DOI=10.1007/pl00013817;
RA Entian K.-D., Schuster T., Hegemann J.H., Becher D., Feldmann H.,
RA Gueldener U., Goetz R., Hansen M., Hollenberg C.P., Jansen G., Kramer W.,
RA Klein S., Koetter P., Kricke J., Launhardt H., Mannhaupt G., Maierl A.,
RA Meyer P., Mewes W., Munder T., Niedenthal R.K., Ramezani Rad M.,
RA Roehmer A., Roemer A., Rose M., Schaefer B., Siegler M.-L., Vetter J.,
RA Wilhelm N., Wolf K., Zimmermann F.K., Zollner A., Hinnen A.;
RT "Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by
RT a systematic approach.";
RL Mol. Gen. Genet. 262:683-702(1999).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-268 AND SER-383, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-268; THR-380;
RP SER-383 AND SER-392, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PET10 AND PDR16.
RX PubMed=26004510; DOI=10.1016/j.devcel.2015.04.015;
RA Moldavski O., Amen T., Levin-Zaidman S., Eisenstein M., Rogachev I.,
RA Brandis A., Kaganovich D., Schuldiner M.;
RT "Lipid droplets are essential for efficient clearance of cytosolic
RT inclusion bodies.";
RL Dev. Cell 33:603-610(2015).
CC -!- FUNCTION: Inclusion body (IB) resident protein that interacts strongly
CC with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing
CC after protein folding stress, probably by enabling access to the IBs of
CC an LD-stored soluble sterol derivative that acts as chaperone in
CC inclusion clearing. {ECO:0000269|PubMed:26004510}.
CC -!- SUBUNIT: Interacts with lipid droplet proteins PET10 and PDR16.
CC {ECO:0000269|PubMed:26004510}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Note=Localized exclusively in
CC cytoplasmic inclusion bodies under protein folding stress conditions.
CC {ECO:0000269|PubMed:26004510}.
CC -!- MISCELLANEOUS: Present with 4980 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IML2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z49357; CAA89375.1; -; Genomic_DNA.
DR EMBL; X83502; CAA58488.1; -; Genomic_DNA.
DR EMBL; X88851; CAA61317.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08717.1; -; Genomic_DNA.
DR PIR; S56028; S56028.
DR RefSeq; NP_012453.1; NM_001181515.1.
DR AlphaFoldDB; P47031; -.
DR BioGRID; 33674; 86.
DR DIP; DIP-4836N; -.
DR IntAct; P47031; 1.
DR MINT; P47031; -.
DR STRING; 4932.YJL082W; -.
DR iPTMnet; P47031; -.
DR MaxQB; P47031; -.
DR PaxDb; P47031; -.
DR PRIDE; P47031; -.
DR EnsemblFungi; YJL082W_mRNA; YJL082W; YJL082W.
DR GeneID; 853363; -.
DR KEGG; sce:YJL082W; -.
DR SGD; S000003618; IML2.
DR VEuPathDB; FungiDB:YJL082W; -.
DR eggNOG; KOG3783; Eukaryota.
DR GeneTree; ENSGT00940000176789; -.
DR HOGENOM; CLU_014926_0_0_1; -.
DR InParanoid; P47031; -.
DR OMA; TYVPGHG; -.
DR BioCyc; YEAST:G3O-31539-MON; -.
DR PRO; PR:P47031; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47031; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0071218; P:cellular response to misfolded protein; IMP:SGD.
DR InterPro; IPR019412; Iml2/TPR_39.
DR PANTHER; PTHR31859; PTHR31859; 1.
DR Pfam; PF10300; DUF3808; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..731
FT /note="Inclusion body clearance protein IML2"
FT /id="PRO_0000203051"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36114"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 731 AA; 82536 MW; 61441915779F8D53 CRC64;
MFRVFGSFGS KGNQSSGEEQ STKTKQVLKQ ANDFEIALKA MDFVLDDRTD EGLNLLKKAE
METGSDQTIL TLARGVIEFL QATLSFETEE MKRAAITLGK AEQMSWKSKQ NAEKTNFRSS
SIYPPGTVYA VTYTESCLLH ALLMLFSESM MEAAKALLKL RRAYTMLQDI MVTVKKAERS
KNSSSPSPSE KSQESCGSFV SAETTFISVD IPYKLSSEDK SNPLLLEFAE KIYTMRMGRL
SGAHIGNTPS FHRLRDDLGL QTTPSQASDR HSVSDDFDLE QATIDEFIHS GANLCYGILQ
VVLSLLPPAI GAVLSIVGFK GSREEGLRLV WKATKERNVH GCIGLLGLMF YYDGPFQFTD
ADFDIPPNDN GSRALNKSRT NDSSLLPGYM DSATLLHPGK ILEDALLKAR ALFPNSALWL
LNEAKMLAGK GRLRDSLALM DSIDVNSIRM RQVKSLMVFE RAILLVNLHE YNRAADDLIS
LLDISDWSHA LYTYFAGCCY LENWRMTQLG LLNDGKEQFY KERARELIFD APSLLGKKTF
KSKNLPLDRF MLRKVQQFNN MQKKLNLQEP LDSIATSPVH ELAYFYNGYN RMTENDLILT
KKMLTEYHNP AIDSEDPDQE LIRNLLLSLT LRRLGDAERG LALLDDIVLP KIFYIQNGKV
KYFKKTEDPW AYPAALYERA LFCWKLGGME SLNECREWLL RAQNYAADYE LSTRIGMKIK
AALDRVENAL A
