OS9_GIBZE
ID OS9_GIBZE Reviewed; 512 AA.
AC Q4IEA7; A0A098DKG9; A0A0E0S7I9; V6R9V7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein OS-9 homolog;
DE Flags: Precursor;
GN Name=YOS1; ORFNames=FGRRES_04451, FGSG_04451;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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
CC {ECO:0000255|PROSITE-ProRule:PRU10138}; Peripheral membrane protein
CC {ECO:0000250}; Lumenal side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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DR EMBL; DS231664; ESU08650.1; -; Genomic_DNA.
DR EMBL; HG970333; CEF79464.1; -; Genomic_DNA.
DR RefSeq; XP_011321149.1; XM_011322847.1.
DR AlphaFoldDB; Q4IEA7; -.
DR STRING; 5518.FGSG_04451P0; -.
DR EnsemblFungi; ESU08650; ESU08650; FGSG_04451.
DR GeneID; 23551702; -.
DR KEGG; fgr:FGSG_04451; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G15325; -.
DR eggNOG; KOG3394; Eukaryota.
DR HOGENOM; CLU_025069_0_0_1; -.
DR InParanoid; Q4IEA7; -.
DR Proteomes; UP000070720; Chromosome 2.
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; IPR012913; OS9-like_dom.
DR PANTHER; PTHR15414; PTHR15414; 1.
DR Pfam; PF07915; PRKCSH; 1.
DR PROSITE; PS00014; ER_TARGET; 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..512
FT /note="Protein OS-9 homolog"
FT /id="PRO_0000043271"
FT DOMAIN 149..288
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 71..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 509..512
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 74..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 159
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 171
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 242
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 248
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 270
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 276
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 241..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 256..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 512 AA; 56835 MW; 906486CB245D2D24 CRC64;
MRRFNLILLA SLQLVGARSP GGFNIHEDLL TYPQFEVVFD NQYISEKDAH SLLDSQHPTY
SADFAQSTLG QAREADARDN EAENKDQDGP SYKYELMKMP PNEYLCSIPI LQSPEAENKT
ANELAKAEEA RELTRATASG WELLSELQDS CLYFMSGWWS YSFCNNREIV QFHALPSIPN
GQPPKRDPHT MEFTLGRVPA VPASAAHQAK MNGQEAPPPA ELQVKGDQRY LVQRLEGGTI
CDLTGRERTI EVQYHCVPGM KADRIGWIKE VTICAYLMVV NTPRLCNDVA FLPPEETRAN
PITCKLILDK LNEPPSLDQT VPLAQDEAQV PLKQEDTGAK SGDAAPRDVG KEPINIGGVL
VGARNVLSGA DEAGKPPAKL PPPRSYFSNS NTDTERFLKV VASGKSKEDG GEMEVLGNEE
LEKLDLKPSV VKDMTERMRK LAGKYGWKLE LVELPGGEKE LRGYIDADEE ELAKNKAKLK
KEKEAAAKAK GDDEEEVVEG SEEQFFDKKD EL
