OS9_RAT
ID OS9_RAT Reviewed; 666 AA.
AC Q5RKH6;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein OS-9;
DE Flags: Precursor;
GN Name=Os9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TOPOLOGY.
RX PubMed=19084021; DOI=10.1016/j.jmb.2008.11.045;
RA Alcock F., Swanton E.;
RT "Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress
RT and facilitates ubiquitination of misfolded glycoproteins.";
RL J. Mol. Biol. 385:1032-1042(2009).
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. Possible
CC targets include TRPV4 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with CPNE6 (via second C2 domain);
CC this interaction occurs in a calcium-dependent manner in vitro (By
CC similarity). Component of the HRD1 complex, which comprises at least
CC SYNV1/HRD1, DERL1/2, FAM8A1, HERPUD1/HERP, OS9, SEL1L and UBE2J1.
CC FAM8A1 is stabilized by interaction with SYNV1, which prevents its
CC proteasomal degradation. OS9 and UBE2J1 recruitment to the complex may
CC be mediated by SEL1L (By similarity). Through this complex, may
CC interact with ERLEC1 and HSPA5 (By similarity). Interacts with HSP90B1
CC (By similarity). Interacts with CREB3 (By similarity).
CC {ECO:0000250|UniProtKB:Q13438, ECO:0000250|UniProtKB:Q8K2C7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- PTM: Intramolecular disulfide bonds. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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DR EMBL; BC085907; AAH85907.1; -; mRNA.
DR RefSeq; NP_001007266.1; NM_001007265.1.
DR AlphaFoldDB; Q5RKH6; -.
DR SMR; Q5RKH6; -.
DR BioGRID; 263807; 2.
DR CORUM; Q5RKH6; -.
DR STRING; 10116.ENSRNOP00000044914; -.
DR GlyGen; Q5RKH6; 1 site.
DR PhosphoSitePlus; Q5RKH6; -.
DR jPOST; Q5RKH6; -.
DR PaxDb; Q5RKH6; -.
DR PRIDE; Q5RKH6; -.
DR Ensembl; ENSRNOT00000049895; ENSRNOP00000044914; ENSRNOG00000025570.
DR GeneID; 362891; -.
DR KEGG; rno:362891; -.
DR UCSC; RGD:1359574; rat.
DR CTD; 10956; -.
DR RGD; 1359574; Os9.
DR eggNOG; KOG3394; Eukaryota.
DR GeneTree; ENSGT00530000063603; -.
DR HOGENOM; CLU_026715_0_0_1; -.
DR InParanoid; Q5RKH6; -.
DR OMA; WLKRLYV; -.
DR OrthoDB; 1475416at2759; -.
DR PhylomeDB; Q5RKH6; -.
DR TreeFam; TF314309; -.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR PRO; PR:Q5RKH6; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000025570; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q5RKH6; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:RGD.
DR GO; GO:0006621; P:protein retention in ER lumen; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IDA:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..666
FT /note="Protein OS-9"
FT /id="PRO_0000386450"
FT DOMAIN 108..230
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 261..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..433
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 118
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 182
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 188
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 212
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 218
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 181..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 196..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 666 AA; 75365 MW; 8E1F48228C671ED6 CRC64;
MAAEALLSSL LGLLFLGLLL PAHLTGGVGS LNLEELSEMR YGIQILPLPV MGGQSQASDV
VVVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY
EFCYGRHIQQ YHMEDSEIKG DVLYLGYYQS AFNWDDETAK ASKQHRLKRY HSQTYGNGSK
CDLNGKPREA EVRFLCDEGA GISGDYIDRV DEPFSCSYVL SIRTSRLCPH PLLRPPASAA
PQAILCHPAL QPDEYMAYLQ RQAESKQHEE KVTEEVQDTD HQVWSGSKAA GAPPKKEDVS
PTKEDKESEF WKMLQEPEEQ ATGTEEAQAG EQDLNHEAAA DPAPAPPTDF QNNVQVKLIR
SPADLIRLIE ELKGAEKGKP SVRQEQPGDD TTEAPQREAE AKGKGGEPRG LVEEEDGDEE
EEDEDEDEQQ LLGEFEKELE GMLLPSDRER LRSEVKAGME RELENIIQET EKELDPEGLR
KESEREQAIL ALTSTLDKLI KRLQESQSPE LVQKYKKRRV VPQKPPPSPH PTEEEPEHRV
RVRVTKLRHG GPNQDLTVLE MNRENPQLKQ IEGLVTEVLE REGLTAEGKI EIKIVRPGAE
GKEEDTRWLT DEDTRNLKEI FFNILVQGAE EANKERQRQS ELESNYRRVW GSPGGEDTGD
LDEFDF
