OS9_SCHPO
ID OS9_SCHPO Reviewed; 310 AA.
AC Q9UTC8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein OS-9 homolog;
DE Flags: Precursor;
GN Name=yos9; ORFNames=SPAC227.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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; CU329670; CAB61460.3; -; Genomic_DNA.
DR PIR; T50167; T50167.
DR RefSeq; NP_592965.3; NM_001018365.3.
DR AlphaFoldDB; Q9UTC8; -.
DR BioGRID; 277961; 10.
DR STRING; 4896.SPAC227.11c.1; -.
DR MaxQB; Q9UTC8; -.
DR PaxDb; Q9UTC8; -.
DR EnsemblFungi; SPAC227.11c.1; SPAC227.11c.1:pep; SPAC227.11c.
DR GeneID; 2541459; -.
DR KEGG; spo:SPAC227.11c; -.
DR PomBase; SPAC227.11c; yos9.
DR VEuPathDB; FungiDB:SPAC227.11c; -.
DR eggNOG; KOG3394; Eukaryota.
DR HOGENOM; CLU_078323_0_0_1; -.
DR InParanoid; Q9UTC8; -.
DR OMA; AYLQTTY; -.
DR Reactome; R-SPO-5358346; Hedgehog ligand biogenesis.
DR PRO; PR:Q9UTC8; -.
DR Proteomes; UP000002485; Chromosome I.
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:0016020; C:membrane; NAS:PomBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:PomBase.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
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..40
FT /evidence="ECO:0000255"
FT CHAIN 41..310
FT /note="Protein OS-9 homolog"
FT /id="PRO_0000043274"
FT DOMAIN 129..255
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 282..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 151
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 209
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 215
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 237
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 243
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 208..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 223..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 310 AA; 35393 MW; B2346AA9BD360FAD CRC64;
MFSSSMFPHL ILPAIGSSKV RTMVLPFAFV GFFIFPICLA SLLDWNDAYE YPKYSFEWSN
VSILEGDIDS IKEKTEKTKL SSLFYAGKHE YFCVYPNASL IKQNSTTEPS YDLQELRIQG
TEKINELANV FLIENRGYWT YDYVYGQHVR QYHLEPQQGS DKVLANPMYI LGTAPNTQTK
KNLEENWAIG FVEGKAYLQT TFRNGTMCDI TKRPRHVILS YECSTNSDTP EITQYQEVSS
CAYSMTIHVP GLCSLPAFKI QEDIPSEKIV CYNVIKEKSN EVDHKDSQHV VDEVAQTSPP
EVKEVETQSS
