ID   IML2_NEUCR              Reviewed;         811 AA.
AC   Q7SA06;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Inclusion body clearance protein iml2;
GN   Name=iml2; ORFNames=NCU07911;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002239; EAA33191.1; -; Genomic_DNA.
DR   RefSeq; XP_962427.1; XM_957334.2.
DR   AlphaFoldDB; Q7SA06; -.
DR   STRING; 5141.EFNCRP00000008191; -.
DR   PRIDE; Q7SA06; -.
DR   EnsemblFungi; EAA33191; EAA33191; NCU07911.
DR   GeneID; 3878599; -.
DR   KEGG; ncr:NCU07911; -.
DR   VEuPathDB; FungiDB:NCU07911; -.
DR   HOGENOM; CLU_014926_1_0_1; -.
DR   InParanoid; Q7SA06; -.
DR   OMA; FWNGHSR; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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; Reference proteome.
FT   CHAIN           1..811
FT                   /note="Inclusion body clearance protein iml2"
FT                   /id="PRO_0000333353"
FT   REGION          14..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  88880 MW;  D6028451C5B05C54 CRC64;
     MSAALRFWLR GQSAASNQSS KAPSAAPSPA ASSTSLRDQF NKHGRSSTGS VSAAQQEASN
     IEDAMAAVAL IMNDDIDGAE AMLRAREDAS TFHQLGVGVS TFLRSILGFE KDIMNEATTR
     LGETETRAWN DMKKAQKEAE KHGVYGGSVY PQGHPSGGSH IYPPGSEFAL VNAEAQLMGA
     VVAVMHESLT EGIKGFYKLR KAYATLDGIM ASELLYLQTL EKKGIITNAS STKTSLDKMP
     GAFSDSEFAT LENTKGANTP SQNGAAADSA SVAKDPSGPQ TPASASASNE AKTAADVDIL
     DEKLGHLQLD ADAASEQNVL PDASLEDTTP STPQFSHLDQ LNKFGADRSL FKSPVDIFVH
     SGASMCFGIL LLIISMVPPA FSRLLSVIGF KGDRDRGVQM LWQSTKYDNV NGAMAGLVLL
     QYYNLFFGIA DILPSELDIQ QLSKPSTGGA KFEAVGYPHN ECTALLAQMR HRYPDSRLWR
     LEEARVLANA RRIEEALAML ADNNDSKMRQ IAALNSFELS MNSIYALDFK AAPVHFLRCV
     ELNSWSHALY YYLAACAELE LYRDLFHSGE ATSPAALKHK KLAEEYFRKA PTVAGKKRFM
     AKAMPFEVFV LRKLQKWEER VKAYGLDLAD VICVSPAMEM IYLWNGSKRM PPHLLEKART
     YLPWERCTAP ADKDVVAKIK KLEQDEVAIG LLAESSFLRQ LGKSVEARKL VEPLLGVDKS
     VFKGPTRDDY CGAAAHYEVA AVAWMEACSP EAWPSAPEEV ESFRKQKTDE CQLHLDKVSK
     WDGFVLDARF GMRVQAGIDS VKWLKSKKGW M