ID   IML2_VANPO              Reviewed;         728 AA.
AC   A7TST2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Inclusion body clearance protein IML2;
GN   Name=IML2; ORFNames=Kpol_282p6;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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.
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; DS480523; EDO14679.1; -; Genomic_DNA.
DR   RefSeq; XP_001642537.1; XM_001642487.1.
DR   AlphaFoldDB; A7TST2; -.
DR   STRING; 436907.A7TST2; -.
DR   PRIDE; A7TST2; -.
DR   EnsemblFungi; EDO14679; EDO14679; Kpol_282p6.
DR   GeneID; 5542698; -.
DR   KEGG; vpo:Kpol_282p6; -.
DR   eggNOG; KOG3783; Eukaryota.
DR   HOGENOM; CLU_014926_0_0_1; -.
DR   InParanoid; A7TST2; -.
DR   OMA; FWNGHSR; -.
DR   OrthoDB; 269827at2759; -.
DR   PhylomeDB; A7TST2; -.
DR   Proteomes; UP000000267; 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   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..728
FT                   /note="Inclusion body clearance protein IML2"
FT                   /id="PRO_0000333358"
SQ   SEQUENCE   728 AA;  82930 MW;  5F998512A9E305F2 CRC64;
     MLRVFGSLTR SRSSSVLSQD DKIKQILKQA HDFEIALQAM DYVLDDRAEE GLALLKKNEA
     EDGSDQTINV LARGVIEFLE ATLGFEAEEM KKASETLAKA ENLSLKSRQY AQKNDLKSSS
     LYAPGTVYAV TYTESCLLHA LLMIFSESYV ETAKALLKLR KAYYMLQEIF EEMKKVKQTN
     GNMSIYKSET NHSEASVDSS NASFSSVDIP YELTREESNN SLYQESAEKV QKMRVRRLTG
     SHIGNTPAID RLRSELGLDG PKVTTEENSN EYSALSENMD FSQATIDEFI HSGVNLCYGI
     LQVVLSLLPS GIGAVLSVVG FHGSREDGLR LVWRATKQRN IHGCIGLLGL MFYYDGPFQF
     TDADFDIPVP ENELKKTKSS STYEEGDLDG PTLLHPGKIL EDALLQSRAL FPHSALWLLN
     EATMLSGQGR LRDSVKLMDS IEADKIEMRQ VKSLLIFNRA LTLVHLHEYE RAADDFLSLL
     DISSWSHSLY HYFAGSCYLE IYRMHQLGVR KSDRPEHFKQ RATDLIFGAP NLLTRKSFNA
     RPLPLDRFML RKVDQFKATQ KRLKLSDPLD AIATSPVHEL QYFYNGYNRM GKQDLELANI
     MLTEYHNPAI DAKEPNQEMI KDFLVSLTYR RLDRAEEGCE LLDRNVLPKI FTMVNGKVKY
     FKKTEDPWLY PSALYERSLF SWKLKHMDGL EESKEWLTRA QGYADDYELS TRVEMKIKAA
     IDRVDESL