IML2_YEAS7
ID IML2_YEAS7 Reviewed; 731 AA.
AC A6ZPP2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Inclusion body clearance protein IML2;
DE AltName: Full=Increased minichromosome loss protein 2;
GN Name=IML2; ORFNames=SCY_2852;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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:0000250|UniProtKB:P47031}.
CC -!- SUBUNIT: Interacts with lipid droplet proteins PET10 and PDR16.
CC {ECO:0000250|UniProtKB:P47031}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47031}. Nucleus
CC {ECO:0000250|UniProtKB:P47031}. Note=Localized exclusively in
CC cytoplasmic inclusion bodies under protein folding stress conditions.
CC {ECO:0000250|UniProtKB:P47031}.
CC -!- SIMILARITY: Belongs to the IML2 family. {ECO:0000305}.
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DR EMBL; AAFW02000038; EDN63495.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZPP2; -.
DR PRIDE; A6ZPP2; -.
DR EnsemblFungi; EDN63495; EDN63495; SCY_2852.
DR HOGENOM; CLU_014926_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR019412; Iml2/TPR_39.
DR PANTHER; PTHR31859; PTHR31859; 1.
DR Pfam; PF10300; DUF3808; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Phosphoprotein.
FT CHAIN 1..731
FT /note="Inclusion body clearance protein IML2"
FT /id="PRO_0000333356"
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:0000250|UniProtKB:P47031"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47031"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36114"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P47031"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47031"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47031"
SQ SEQUENCE 731 AA; 82548 MW; 63BC2D27B85FB1AF 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 WKAIKERNVH 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