OS9_ARATH
ID OS9_ARATH Reviewed; 282 AA.
AC Q8GWH3; O65221; Q8LD14;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein OS-9 homolog {ECO:0000305};
DE Short=AtOS9 {ECO:0000303|PubMed:22516478};
DE AltName: Full=Protein EMS-MUTAGENIZED BRI1 SUPPRESSOR 6 {ECO:0000303|PubMed:22516478};
DE Flags: Precursor;
GN Name=OS9 {ECO:0000303|PubMed:22516478};
GN Synonyms=EBS6 {ECO:0000303|PubMed:22516478};
GN OrderedLocusNames=At5g35080 {ECO:0000312|Araport:AT5G35080};
GN ORFNames=F7N22.4 {ECO:0000312|EMBL:AAC13579.1},
GN T13C12.2 {ECO:0000312|EMBL:BAB10015.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INTERACTION WITH HRD3A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TYR-132; GLN-142; GLY-191 AND GLU-221.
RX PubMed=22516478; DOI=10.1093/mp/sss042;
RA Su W., Liu Y., Xia Y., Hong Z., Li J.;
RT "The Arabidopsis homolog of the mammalian OS-9 protein plays a key role in
RT the endoplasmic reticulum-associated degradation of misfolded receptor-like
RT kinases.";
RL Mol. Plant 5:929-940(2012).
RN [7]
RP FUNCTION, INTERACTION WITH HRD3A, SUBCELLULAR LOCATION, GLYCOSYLATION AT
RP ASN-94; ASN-169 AND ASN-190, AND DISRUPTION PHENOTYPE.
RX PubMed=22328055; DOI=10.1007/s11103-012-9891-4;
RA Huttner S., Veit C., Schoberer J., Grass J., Strasser R.;
RT "Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic
RT reticulum-associated degradation of glycoproteins.";
RL Plant Mol. Biol. 79:21-33(2012).
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. Targets the
CC misfolded LRR receptor kinase BRI1 and the misfolded receptor-like
CC kinase EFR. {ECO:0000269|PubMed:22328055, ECO:0000269|PubMed:22516478}.
CC -!- SUBUNIT: Interacts with HRD3A. {ECO:0000269|PubMed:22328055,
CC ECO:0000269|PubMed:22516478}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:22328055, ECO:0000269|PubMed:22516478}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have enhanced sensitivity to salt stress.
CC {ECO:0000269|PubMed:22328055}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13579.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB10015.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000421; BAB10015.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF058825; AAC13579.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93928.1; -; Genomic_DNA.
DR EMBL; AK118844; BAC43433.1; -; mRNA.
DR EMBL; AY086270; AAM64343.1; -; mRNA.
DR PIR; T01158; T01158.
DR RefSeq; NP_568525.1; NM_122899.3.
DR AlphaFoldDB; Q8GWH3; -.
DR SMR; Q8GWH3; -.
DR BioGRID; 18714; 3.
DR STRING; 3702.AT5G35080.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR TCDB; 8.A.67.1.2; the os-9 quality control (erad) protein (os-9) family.
DR PaxDb; Q8GWH3; -.
DR PRIDE; Q8GWH3; -.
DR ProteomicsDB; 226035; -.
DR EnsemblPlants; AT5G35080.1; AT5G35080.1; AT5G35080.
DR GeneID; 833459; -.
DR Gramene; AT5G35080.1; AT5G35080.1; AT5G35080.
DR KEGG; ath:AT5G35080; -.
DR Araport; AT5G35080; -.
DR TAIR; locus:2150361; AT5G35080.
DR eggNOG; KOG3394; Eukaryota.
DR HOGENOM; CLU_077023_0_0_1; -.
DR InParanoid; Q8GWH3; -.
DR OMA; NGTMCDL; -.
DR OrthoDB; 1475416at2759; -.
DR PhylomeDB; Q8GWH3; -.
DR PRO; PR:Q8GWH3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GWH3; baseline and differential.
DR Genevisible; Q8GWH3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:0036503; P:ERAD pathway; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:TAIR.
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 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..282
FT /note="Protein OS-9 homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431276"
FT DOMAIN 120..239
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 262..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 130
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 142
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 195
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 201
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 221
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 227
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT DISULFID 122..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 194..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 209..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT MUTAGEN 132
FT /note="Y->A: No effect on function."
FT /evidence="ECO:0000269|PubMed:22516478"
FT MUTAGEN 142
FT /note="Q->E: Loss of function in ERAD."
FT /evidence="ECO:0000269|PubMed:22516478"
FT MUTAGEN 191
FT /note="G->E: In ebs6-1; Loss of function in ERAD."
FT /evidence="ECO:0000269|PubMed:22516478"
FT MUTAGEN 221
FT /note="E->A: Loss of function in ERAD."
FT /evidence="ECO:0000269|PubMed:22516478"
SQ SEQUENCE 282 AA; 32170 MW; 64D56BDB03AACA0D CRC64;
MRITQILLCL VIVALSSSSH VWSDQIFPAH LVGTFSRNNR EPKYKIEFLP EDSPFHPGDN
LESMVMLDKH GNRFLCYLPK EEKATSGWTS SQQNISTVMM ETQQLVKLKT PDELLQPLSE
KCLFRQEGWW SYEFCHQKYV RQLHVEDENK IVQEFFLGTF DPEATAAFNQ TVSDASTDAS
QRYHSHVYTN GTTCDLTGSP REVEVRFVCA ETRAMVTSIT ELSTCKYALT VQCPTLCKHP
LFQLEKPVSH TIHCNAIPVE EDATRNKEEQ AVDESPKMIA DS
