ID   OS9_ASHGO               Reviewed;         421 AA.
AC   Q756T2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Protein OS-9 homolog;
DE   Flags: Precursor;
GN   Name=YOS9; OrderedLocusNames=AER171W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52853.1; -; Genomic_DNA.
DR   RefSeq; NP_985029.1; NM_210383.1.
DR   AlphaFoldDB; Q756T2; -.
DR   SMR; Q756T2; -.
DR   STRING; 33169.AAS52853; -.
DR   EnsemblFungi; AAS52853; AAS52853; AGOS_AER171W.
DR   GeneID; 4621237; -.
DR   KEGG; ago:AGOS_AER171W; -.
DR   eggNOG; KOG3394; Eukaryota.
DR   HOGENOM; CLU_679768_0_0_1; -.
DR   InParanoid; Q756T2; -.
DR   OMA; ANTIYCT; -.
DR   Proteomes; UP000000591; Chromosome V.
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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..421
FT                   /note="Protein OS-9 homolog"
FT                   /id="PRO_0000042757"
FT   DOMAIN          99..220
FT                   /note="MRH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   REGION          375..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..397
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         115
FT                   /ligand="a mannooligosaccharide derivative"
FT                   /ligand_id="ChEBI:CHEBI:71274"
FT                   /evidence="ECO:0000250|UniProtKB:Q13438"
FT   BINDING         180
FT                   /ligand="a mannooligosaccharide derivative"
FT                   /ligand_id="ChEBI:CHEBI:71274"
FT                   /evidence="ECO:0000250|UniProtKB:Q13438"
FT   BINDING         202
FT                   /ligand="a mannooligosaccharide derivative"
FT                   /ligand_id="ChEBI:CHEBI:71274"
FT                   /evidence="ECO:0000250|UniProtKB:Q13438"
FT   BINDING         208
FT                   /ligand="a mannooligosaccharide derivative"
FT                   /ligand_id="ChEBI:CHEBI:71274"
FT                   /evidence="ECO:0000250|UniProtKB:Q13438"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        173..206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        188..218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ   SEQUENCE   421 AA;  47924 MW;  6E57E2FE19181651 CRC64;
     MWRWSTGVRT MLGYAMCFLA LGSALTVRLH STRTNLPQYL TREIGDDEFE ELLRSSASAG
     HKWHVEQFVD GSRCYVPETE QNMAPVPDDL LERGIKLVEE ATVGKKLEYL PISYWGYKFI
     NSELNKTVIQ HKDQHQVLLG SMVKADPQTV QHSLERDEDS YYISERFGDG DLCSLLEEDR
     TVEVQYRCKY DTPLEIILDL KEYETCRYTM LVSIPSLCEL PEFGPYTRQT PANTIYCTAP
     ATPEFNIATL VEAYKPTFLG HGFYHLAPHA NLTHKETTAM LMYHQQPIPG NEEDDGTMDS
     AFIKHSTMAY MQLLEMGLLN GPDGLPFSEE GNFTVYAKVI GFDGGLITVT RFQISHGEVI
     IDHVVPEVLE DMEQGNSEDY EQQAPEQLDE EEAELTSQSD DPAIMRVHLQ EFITPEYDAI
     E