IML2_NEOFI
ID IML2_NEOFI Reviewed; 719 AA.
AC A1D345;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Inclusion body clearance protein iml2;
GN Name=iml2; ORFNames=NFIA_015310;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW22838.1; -; Genomic_DNA.
DR RefSeq; XP_001264735.1; XM_001264734.1.
DR AlphaFoldDB; A1D345; -.
DR STRING; 36630.CADNFIAP00000948; -.
DR EnsemblFungi; EAW22838; EAW22838; NFIA_015310.
DR GeneID; 4590991; -.
DR KEGG; nfi:NFIA_015310; -.
DR VEuPathDB; FungiDB:NFIA_015310; -.
DR eggNOG; KOG3783; Eukaryota.
DR HOGENOM; CLU_014926_1_0_1; -.
DR OMA; FWNGHSR; -.
DR OrthoDB; 269827at2759; -.
DR Proteomes; UP000006702; 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 PANTHER; PTHR31859; PTHR31859; 1.
DR Pfam; PF10300; DUF3808; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..719
FT /note="Inclusion body clearance protein iml2"
FT /id="PRO_0000333352"
FT REGION 177..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 80595 MW; 242061915636FB01 CRC64;
MFRVGSWLYG KKPAANASTQ SLDSLVELRD PATLILNDDV DGAEAGLAEG TSTFHNLGRG
VVAFIRATLG FEQDIMRQAS ERLNEAETSA SVDQHRAQHN SHAPNTYHSP MYSPGTEFAL
CQAIAQLMSA IVGVLNESLT ESIKAFYRLR KAYITLDAIL KMEQKYMEES RSATLVESTT
SGSVPSSQRH SSSNLQSSSS SISSAKVKEA TADTLAAPSK DTDVNERLAD LSLSGEAPVA
EDPGQTPTPI NTDILDHDPD SDIFQNQIDV FVHSGSNFCF GVLLLLISMV PPSFSKLLSI
IGFHGDKERG LKMLWQASKF HNLIGGIAAF AILGYYNGFV RYCDIMPDSI PGKDGDVQGY
PQKRLELLLA KMRERFPKSQ LWLLEESRMS GANKNLDRAL ELLCGEERSP LKQVEALRVF
ERSLNAMYLH KYELCADSFL ECVDLNSWSR SLYYYIAGSC HLSLYRDVKE TDSAKAAKHA
ELAEKYFRMA PTVAGKKRFM ARQLPFDVFV ARKFAKWEAR AKEWKVSLVD AVGIDPIEEM
IFFWNGHSRM TDEQLQESLQ KLAWSESNAN TTWSREGPEE KAILKLLRAA VHRSLRKHTQ
AKEMLEDILG QDRTLFKGHL KDDWICPVAH FEMAANLWME RPTYIANHSG AKQDSDKESA
GPADAKDALQ YERERVRKCK EYLEKAAKWE SYELDARIGL KVTAAMEAVQ KWESTHPTV