ID   IML2_SCHPO              Reviewed;         563 AA.
AC   O94699;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Inclusion body clearance protein IML2;
GN   ORFNames=SPBC83.16c {ECO:0000312|PomBase:SPBC83.16c};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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; CU329671; CAB36878.1; -; Genomic_DNA.
DR   PIR; T40705; T40705.
DR   RefSeq; NP_595648.1; NM_001021542.2.
DR   AlphaFoldDB; O94699; -.
DR   BioGRID; 277702; 12.
DR   STRING; 4896.SPBC83.16c.1; -.
DR   MaxQB; O94699; -.
DR   PaxDb; O94699; -.
DR   EnsemblFungi; SPBC83.16c.1; SPBC83.16c.1:pep; SPBC83.16c.
DR   GeneID; 2541188; -.
DR   KEGG; spo:SPBC83.16c; -.
DR   PomBase; SPBC83.16c; -.
DR   VEuPathDB; FungiDB:SPBC83.16c; -.
DR   eggNOG; KOG3783; Eukaryota.
DR   HOGENOM; CLU_014926_1_0_1; -.
DR   InParanoid; O94699; -.
DR   OMA; IATQEEW; -.
DR   PhylomeDB; O94699; -.
DR   PRO; PR:O94699; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR   GO; GO:0071218; P:cellular response to misfolded protein; ISO:PomBase.
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; Reference proteome.
FT   CHAIN           1..563
FT                   /note="Inclusion body clearance protein IML2"
FT                   /id="PRO_0000373873"
SQ   SEQUENCE   563 AA;  63485 MW;  26F4BA36B8CEA22C CRC64;
     MSKSQEQRLQ NFVTVIQGLN DILDDKMDEA TEKFKSGNSS FHLSGQAVVA FIQAVLTFEP
     SRFKDSQNRI DIAIKALSAD KDDASKNNTF LSTFDPGVEY RVSIGLMLLL SALIGFCSES
     IVTSVKSVYK LRKAHSIFSK INKRHFDHFS AAFHSTGRSD VDLANEYVQT GTLLCTGLFT
     LLISLLPPKM ITILNVFGYK GDRDWALQCM WMPALQRPTS FFAAVAFAAL IQYYSGAVQL
     CSIYKKTPEE PDGWPDKRCF EILEKVEKAH PDGPMWPLHR AKLLSMVKKQ DEAIVVLEEL
     MAKPPPRLKQ LEVLIVFEHA LDCAFSHRYV DGANSFLKLS SLNDSSTALY SYFAAACFLQ
     DVHVNANVEA LEKASKLLEP LHDLVANKTA PLDVHIRRKV GKLIKRRASA GNQGGLAEYV
     GFSPLYELVY VWNGFRRMTD DELSKFDVER MEPWQDQDDD ICQALIKATV LRNLGRTDEV
     FPILQKICAV TRTTETWAVA FAHYEMAVAF FESNGSKKEG LKHCDAYLRK ARDFGGDNEF
     ESRLIIRVQL ARHVVRKCLQ SMS