ID   IML2_DEBHA              Reviewed;         886 AA.
AC   Q6BXP8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Inclusion body clearance protein IML2;
GN   Name=IML2; OrderedLocusNames=DEHA2B01254g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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.
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; CR382134; CAG85006.2; -; Genomic_DNA.
DR   RefSeq; XP_457021.2; XM_457021.1.
DR   AlphaFoldDB; Q6BXP8; -.
DR   STRING; 4959.XP_457021.2; -.
DR   EnsemblFungi; CAG85006; CAG85006; DEHA2B01254g.
DR   GeneID; 2913724; -.
DR   KEGG; dha:DEHA2B01254g; -.
DR   VEuPathDB; FungiDB:DEHA2B01254g; -.
DR   eggNOG; KOG3783; Eukaryota.
DR   HOGENOM; CLU_014926_0_0_1; -.
DR   InParanoid; Q6BXP8; -.
DR   OMA; TYVPGHG; -.
DR   OrthoDB; 269827at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR31859; PTHR31859; 1.
DR   Pfam; PF10300; DUF3808; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..886
FT                   /note="Inclusion body clearance protein IML2"
FT                   /id="PRO_0000333348"
FT   REGION          207..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  99402 MW;  F3EDD84480936F7C CRC64;
     MFKGLRKKAS ALSLYSQPTR AGGMANDPSS YDKILKQVHD FETAFKAMDY LLDDRTQDGI
     DLLQEQQKRH VKTESQQPAA IFPLALGVME FIEATLGFEP EVMERAHQTL SEAEAASMNN
     VKYNVRYSLG TSHIYPPGTE FQVTNAESTL LNALLMLLQE SNGVVESAKA LFKLRKAYQT
     LDSIYKKIKE SEPVFNKNLA KLKKEASLQH EGNSANVSTV DLPGYSNQSS RGGSSASLPQ
     DVKLLKNLET VYQMRKSRIE GTSLNDPSQA LNVNMYAATS SGESSVSVAS AVNSDSGGRP
     ESPRATTLSQ NAKFRNPIPS SADDEFDDED DEFSDASDTF HSFGNLSIPH SMHKSSSLAN
     SQVLDNAESF VSGANSSSIS LRNSDQEDNH MHVSTVDEYI HSGVQLCFGI LQVVLSLIPP
     TIGKVLSIVG FRGDRETGLK MLWRTAITSR NIHGELALLC LLVFYDGPIQ FIDDGYQLPG
     QEDANVSEVI SIDKKSNISD KELEIILKNP ALYTPQLLTK VRGYFPHNAL WLLQEGRMLA
     AQGQLVKAAT LMQSFTDNPE TKINMQQVEA LLIFDRAMLY AFKHDYDEAA RDFIYLLDIN
     SWSKSIYLFF AGSCYLEKWR MIKLGMIEVE DREKSLKYYG DQAELYLKKA PTYVPGHGIN
     ASNKKGGIGG GNKQMPFDKF LLRKLQHIEN CQKKHPKLSF LNCFGTSPIH ELIYFWNGYN
     RMNETELKLT LTLLGYSGAV NSDYSANNNE QNFAKFEENE DEAMIRYLFQ SITLRSLNRL
     SEGVSLLDSH VISKFVTQDS PNMPFKFIKM TYSPYLYPTA LYERSMFVWL LRTSKKSANL
     REAIEESKSW LKKSEMVGDG DYELSNRTGM KIKAAGDRLD QFKTQI