ID   IML2_COPC7              Reviewed;         722 AA.
AC   A8NVW1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Inclusion body clearance protein IML2;
GN   Name=IML2; ORFNames=CC1G_04079;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000004; EAU84983.2; -; Genomic_DNA.
DR   RefSeq; XP_001836766.2; XM_001836714.2.
DR   AlphaFoldDB; A8NVW1; -.
DR   STRING; 5346.XP_001836766.2; -.
DR   EnsemblFungi; EAU84983; EAU84983; CC1G_04079.
DR   GeneID; 6013318; -.
DR   KEGG; cci:CC1G_04079; -.
DR   VEuPathDB; FungiDB:CC1G_04079; -.
DR   eggNOG; KOG3783; Eukaryota.
DR   HOGENOM; CLU_023297_0_0_1; -.
DR   InParanoid; A8NVW1; -.
DR   OMA; FWNGHSR; -.
DR   OrthoDB; 269827at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.25.40.10; -; 1.
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..722
FT                   /note="Inclusion body clearance protein IML2"
FT                   /id="PRO_0000333347"
FT   REGION          186..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   722 AA;  78444 MW;  E2531C489A52DA73 CRC64;
     MTNGTPGVPG GEPPHPSAEM LASATKGFDY LFANDIVGSR EHFNSKDDPF HLMGAGVIAF
     LEAALGMETN QVTEASRCLA LSETGTRKQM KAPKAKTHSR FPAGLEWDII NADAVVLLGL
     THALSETYMG YLQCMYSLNN AHSKFTKLYK TVFPAGIDAE EKPPAPAEVA PSSSSTLQVP
     NGLQHKSSFS SLSSVSSTGS NATLPPAPPS PTQPAVTKSF FSRWLGSSAA AAASEPTLPL
     HHHQHHHIPD GPVEELIVSG TAFGYGLFNL VFSLLPKKVQ SLVGFLGFQH DRKLALKALA
     LSASKKDVHG VFAGLVLMTY HGVVLLLSGW QADEARIINQ YKGIIDNVEE RYPEGALWIL
     NRAKILRMSC DAEGAIRVLQ NGLKPERPHS FAQADMMLLF ELAWTLLGQR RYQESADSFM
     KITELNTWSH ATYYFLSAGC HFALGNLEKT QELLDAIPGL IHNKKVGGKD LPTEVFIKKK
     LAFYKEKQKR RCGDEAKFAE AIRINPAEEL GIFWNTHARV SKEICKSHVA DVLHLTPALT
     ITSPTITALS SNSNSNPTLP TPASATAAMS SLSLSSKSST ASKTSPPSLS KSKSPLDLDT
     PDELAVRSLL LGICHRTLEE FDAARKFLLD AHGYQGQVKV NTWVGGVAMF ELAVLELKEV
     EFLEKGGGKV DWMKAMKVAD ERLDVALSLS PNSVDLSSRL DSRISMLRDE MGIKREMLGG
     KA