OS9_ORYSJ
ID OS9_ORYSJ Reviewed; 298 AA.
AC Q67WM9; A0A0P0WZD9;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein OS-9 homolog {ECO:0000305};
DE Short=OsOS9 {ECO:0000305};
DE Flags: Precursor;
GN Name=OS9 {ECO:0000305};
GN OrderedLocusNames=Os06g0644800 {ECO:0000312|EMBL:BAH93656.1},
GN LOC_Os06g43710 {ECO:0000305};
GN ORFNames=OsJ_22141 {ECO:0000312|EMBL:EAZ37805.1},
GN P0017B12.18-1 {ECO:0000312|EMBL:BAD37440.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000312|Proteomes:UP000059680};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Lectin which functions in endoplasmic reticulum (ER) quality
CC control and ER-associated degradation (ERAD). May bind terminally
CC misfolded non-glycosylated proteins as well as improperly folded
CC glycoproteins, retain them in the ER, and possibly transfer them to the
CC ubiquitination machinery and promote their degradation.
CC {ECO:0000250|UniProtKB:Q8GWH3}.
CC -!- SUBUNIT: Interacts with HRD3. {ECO:0000250|UniProtKB:Q8GWH3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8GWH3}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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DR EMBL; AP003568; BAD37440.1; -; Genomic_DNA.
DR EMBL; AP008212; BAH93656.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98847.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ37805.1; -; Genomic_DNA.
DR EMBL; AK109442; BAG98751.1; -; mRNA.
DR RefSeq; XP_015641067.1; XM_015785581.1.
DR AlphaFoldDB; Q67WM9; -.
DR STRING; 4530.OS06T0644800-01; -.
DR PaxDb; Q67WM9; -.
DR PRIDE; Q67WM9; -.
DR EnsemblPlants; Os06t0644800-01; Os06t0644800-01; Os06g0644800.
DR GeneID; 9268424; -.
DR Gramene; Os06t0644800-01; Os06t0644800-01; Os06g0644800.
DR KEGG; osa:9268424; -.
DR eggNOG; KOG3394; Eukaryota.
DR HOGENOM; CLU_077023_0_0_1; -.
DR InParanoid; Q67WM9; -.
DR OMA; NGTMCDL; -.
DR OrthoDB; 1475416at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q67WM9; baseline and differential.
DR Genevisible; Q67WM9; OS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
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:0009651; P:response to salt stress; IEA:EnsemblPlants.
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 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..298
FT /note="Protein OS-9 homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431277"
FT DOMAIN 121..246
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT BINDING 130
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 131
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 143
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 BINDING 228
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 234
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 123..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 201..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 216..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 298 AA; 33439 MW; 73B0E5B070415475 CRC64;
MGLAGGARVV LFVVAAAAAA ALTAAADQIF TSSGAPFGRN SREPRYHVEF HPVDAPFNPE
NGQESVPMTS HVGKHYTCFL PVEETKTMKS IIPQNATNVI IESERRVKPK DPDELLEILK
DQCFYRHEGW WSYEFCYYGK IRQVHVEGEK VIQEYVLGEY DADATDAYYE NQTSDSADED
DNLIDTSKRY HVHLYTNGTV CDLTDMPRET EVRFVCSEPT VVISSIKEIS SCKYVLTVQS
PMLCKNPLFQ QEKRTLSIHC NELLAEAEAT VDDDSLPKEA QIIIPDPDGL HNYAAYAT
