ILM1_YEAST
ID ILM1_YEAST Reviewed; 203 AA.
AC P47155; D6VWT7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein ILM1;
DE AltName: Full=Increased loss of mitochondrial DNA protein 1;
GN Name=ILM1; OrderedLocusNames=YJR118C; ORFNames=J2033;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- INTERACTION:
CC P47155; Q04201: CUE4; NbExp=3; IntAct=EBI-2051644, EBI-27928;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ILM1 family. {ECO:0000305}.
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DR EMBL; Z49618; CAA89648.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08903.1; -; Genomic_DNA.
DR PIR; S57141; S57141.
DR RefSeq; NP_012652.3; NM_001181776.3.
DR AlphaFoldDB; P47155; -.
DR BioGRID; 33874; 688.
DR IntAct; P47155; 10.
DR MINT; P47155; -.
DR STRING; 4932.YJR118C; -.
DR MaxQB; P47155; -.
DR PaxDb; P47155; -.
DR PRIDE; P47155; -.
DR DNASU; 853582; -.
DR EnsemblFungi; YJR118C_mRNA; YJR118C; YJR118C.
DR GeneID; 853582; -.
DR KEGG; sce:YJR118C; -.
DR SGD; S000003879; ILM1.
DR VEuPathDB; FungiDB:YJR118C; -.
DR eggNOG; ENOG502RZTE; Eukaryota.
DR HOGENOM; CLU_117796_0_1_1; -.
DR InParanoid; P47155; -.
DR OMA; YSFVEVW; -.
DR BioCyc; YEAST:G3O-31739-MON; -.
DR PRO; PR:P47155; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47155; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR InterPro; IPR018815; Incr_loss_mito_DNA_1.
DR PANTHER; PTHR28029; PTHR28029; 1.
DR Pfam; PF10311; Ilm1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..203
FT /note="Protein ILM1"
FT /id="PRO_0000203115"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..58
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 175..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 23645 MW; F7F27F4D0BF61F53 CRC64;
MAQALNSTNI AFFRVAFLFT IAFFCLKNVN SILQNTYFIV LTQAMNLPQL TLSRYSGQLG
LFALLFTLNG VHDLIPLLEN NVKYFQSVVP VRLLIFFILT SISYLWESNF YVHNNSVFIY
CFAEVWINFL LYNAIREEKN EEFKRLNQFM VNDEDIEEPQ PFTVKTETTE IIEIINDEEN
DDEDGKDNDD NNEKGNDDSD AKK
