OS9_YARLI
ID OS9_YARLI Reviewed; 558 AA.
AC Q6C3U1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein OS-9 homolog;
DE Flags: Precursor;
GN Name=YOS9; OrderedLocusNames=YALI0E32131g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Lectin involved in the quality control of the secretory
CC pathway. As a member of the endoplasmic reticulum-associated
CC degradation lumenal (ERAD-L) surveillance system, targets misfolded
CC endoplasmic reticulum lumenal glycoproteins for degradation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with missfolded ER lumenal proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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DR EMBL; CR382131; CAG80275.1; -; Genomic_DNA.
DR RefSeq; XP_504671.1; XM_504671.1.
DR AlphaFoldDB; Q6C3U1; -.
DR STRING; 4952.CAG80275; -.
DR EnsemblFungi; CAG80275; CAG80275; YALI0_E32131g.
DR GeneID; 2912332; -.
DR KEGG; yli:YALI0E32131g; -.
DR VEuPathDB; FungiDB:YALI0_E32131g; -.
DR HOGENOM; CLU_488536_0_0_1; -.
DR InParanoid; Q6C3U1; -.
DR OMA; RETKICH; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR045149; OS-9-like.
DR InterPro; IPR012913; OS9-like_dom.
DR PANTHER; PTHR15414; PTHR15414; 1.
DR Pfam; PF07915; PRKCSH; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51914; MRH; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..558
FT /note="Protein OS-9 homolog"
FT /id="PRO_0000043275"
FT DOMAIN 111..237
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 435..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 197
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 219
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 225
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 190..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 205..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 558 AA; 63074 MW; AA7A6D214A731C2E CRC64;
MLLKSLALIA SSSLAATFNI GDDLFADPQF TVQFHNRPLR QADVQNGLLP HRDPVYGHPL
GYEMMQFNGT NHICGIPEVT TTKSSKSREE GELSPTEARD RALELMLPLL GDCLFYEQGF
FSYRFCYGSG VVQYRRHGDN YFPRIYPPPQ ADDSPTFVLG SFEKDDTTNT VTSAGGIPFL
AHRLRSGTHC PLTGANREIE VQFVCDKNVQ HDHILWIKEK RTCNYVMQVG TPRLCKDMRF
QPPPDESLPI MCYSVESEAP EFETIDGMFD GVAHVKEEQE AVSARAHQFV GSNVNKDKID
EIEVAWRFTK ARALNYIGVW LGDCVNRQTL FKELGIATPS HDAPFIIQTR SMFVPAPINR
HFEVRLMITR QQLLLSINDD DVTLEEKYAW WQEQGDMSNL EIQGLTMLDD AGIEDVLARA
TDEVMKQLNK EAKQSKKLAK KKEAASTKRE EAKKQVEASV EEKAVDSAED DGTDTVTSTQ
TFFRTQTLST AEAESKQMPD KAEEDEDEDL IVTMYFEDGE FKIEGFEVAD FEGVKSAMKD
LADKEDDDDD YEDYGLSD
