IML2_SCLS1
ID IML2_SCLS1 Reviewed; 645 AA.
AC A7E727;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Inclusion body clearance protein iml2;
GN Name=iml2; ORFNames=SS1G_01103;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476622; EDN96179.1; -; Genomic_DNA.
DR RefSeq; XP_001596911.1; XM_001596861.1.
DR AlphaFoldDB; A7E727; -.
DR STRING; 665079.A7E727; -.
DR PRIDE; A7E727; -.
DR EnsemblFungi; EDN96179; EDN96179; SS1G_01103.
DR GeneID; 5493696; -.
DR KEGG; ssl:SS1G_01103; -.
DR eggNOG; KOG3783; Eukaryota.
DR HOGENOM; CLU_014926_1_0_1; -.
DR InParanoid; A7E727; -.
DR OMA; IATQEEW; -.
DR Proteomes; UP000001312; 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..645
FT /note="Inclusion body clearance protein iml2"
FT /id="PRO_0000333357"
SQ SEQUENCE 645 AA; 72846 MW; 9D788AD86A96AF69 CRC64;
MSRWFKSAVK ATPAMVAESE EQHLRDVEAA MLKLLNDDIE EADKLLKKHD SSYHHLGRGI
SGFLSAMMGV EKDLLKEAAV ILQDAENKSW DDMKKAQKDS TAFQSNIYPQ GTEYLLCYSV
AQLTSAITAV LSGSITEAVK GFYKLRKAYL TLDGILEVEN KYLEKIAHSS TTSLSSRTPS
HKSSMAALTV DEIAHRTADL SVGDLDEKML DPNNPYPNIS RPPSPPSVTN PYDIDPELAA
RVFTNRTDIF IHSGVRLCCG LLLLVFSMIE NPIFNKILYI VGFKGDRERG TRLLWQATRY
QNFNSAIAAL ALLGYYNGLV GFCDILPTDD AADDNPTGYP KNKCQALLVD MQSRYPHSKL
WKLEEARMLS YKQDLKGALV ILEENSKSKM KQITMINTFE MALTTLFIHE YEKSATAWIN
CSEQSAWSPT LYFYIAGISY VELYRNTRLS DPAAAEVHKK KAIEFILKAP PLAGKQKVMA
KQLPFDIYIV SKVGKWEQRA KAWGVDLVDA IGPSPFVEMI YFWNGVKKSG TVELEKCLDL
LKKERMTCPE KCNEDEEDVA IHLLLRGSCC SWREKDLPPG GDSTSGEKMS EKKLLEYRRE
KLMDCEEKLL KLHSWPQTYV FETRMSFKIS TSLLTVKRHK GLMGF