OS9_KLULA
ID OS9_KLULA Reviewed; 457 AA.
AC Q6CNH1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Protein OS-9 homolog;
DE Flags: Precursor;
GN Name=YOS9; OrderedLocusNames=KLLA0E12639g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99605.1; -; Genomic_DNA.
DR RefSeq; XP_454518.1; XM_454518.1.
DR AlphaFoldDB; Q6CNH1; -.
DR STRING; 28985.XP_454518.1; -.
DR EnsemblFungi; CAG99605; CAG99605; KLLA0_E12607g.
DR GeneID; 2894447; -.
DR KEGG; kla:KLLA0_E12607g; -.
DR eggNOG; KOG3394; Eukaryota.
DR HOGENOM; CLU_598594_0_0_1; -.
DR InParanoid; Q6CNH1; -.
DR Proteomes; UP000000598; Chromosome E.
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:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
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; IPR041039; Yos9_DD.
DR PANTHER; PTHR15414; PTHR15414; 1.
DR Pfam; PF17880; Yos9_DD; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..457
FT /note="Protein OS-9 homolog"
FT /id="PRO_0000043272"
FT DOMAIN 104..222
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT BINDING 116
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 175
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 181
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 204
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 210
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 174..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 189..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 457 AA; 51621 MW; FADF066283199395 CRC64;
MIFLPVTSVV FAISWIYSGV SAFNPYSSTP YSLKYVDEQE FLSVIDNETL LQEGRLFRPY
EGSDVLCYQR NTSSLIQHHE EDTFNSEGAL IEAVNMVNAI LAPNPIEMNT VPISYWTYII
SSGETRTVVQ KGYFGETYLL GNSSNYNSTI DYHFAKSKTG RVYLSETLVD GCTCDLTHKP
REVEIQYICP KRPLSRPFHL EVREIQSCKY QLRLFLPQLC ELSSFNPLLG QLSEHNIICH
RSGSKLSPAL DIFNRYSATV LDHGIYLLKP KNSAKDRRQL MYHAAEPLDS QTTLFELTVE
ERFIGDFISS LKKLIGSDFI QSPTGKSIKP GDLFLWRAPV VDETGNLLFL IDLELNSASE
AIGKVNNDAS LLNELPIHNM VYFDSMTVNQ TDETSSNSLP EKSTGLVPDI FATDEIESPY
KGGTAQELKD KLMEAFRDIG YPDIEVEILE EVVEEQN
