ID   OS9_BOVIN               Reviewed;         667 AA.
AC   Q3MHX6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Protein OS-9;
DE   Flags: Precursor;
GN   Name=OS9;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; BC104554; AAI04555.1; -; mRNA.
DR   RefSeq; NP_001029397.1; NM_001034225.1.
DR   AlphaFoldDB; Q3MHX6; -.
DR   SMR; Q3MHX6; -.
DR   STRING; 9913.ENSBTAP00000009410; -.
DR   PaxDb; Q3MHX6; -.
DR   PeptideAtlas; Q3MHX6; -.
DR   PRIDE; Q3MHX6; -.
DR   GeneID; 504832; -.
DR   KEGG; bta:504832; -.
DR   CTD; 10956; -.
DR   eggNOG; KOG3394; Eukaryota.
DR   InParanoid; Q3MHX6; -.
DR   OrthoDB; 1475416at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
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:0006621; P:protein retention in ER lumen; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
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   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..667
FT                   /note="Protein OS-9"
FT                   /id="PRO_0000254020"
FT   DOMAIN          108..230
FT                   /note="MRH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   REGION          262..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..432
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..450
FT                   /note="Basic and 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   667 AA;  75779 MW;  1504FE4BB3B4CFDE CRC64;
     MAAETLLSSL LGLLLLGLLL PATLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQASDV
     VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMKDAPC LLKTKDWWTY
     EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK ASKQHRLKRY HSQTYGNGSK
     CDLNGRPREA EVRFLCDEGA GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA
     PQAILCHPAL QPEEYMAYVQ RQADSKQYGD RAIEGRQDPD PPVWSETKPG VVPPKKAGAS
     PAKENSKESD FWKMLHEPEE QPPEKEETQA EEQEPNLEAT DPPPTSPDDF QNNVQVKVIR
     SPADLIRLIE ELKGGTRKGK PNTGQEQPGD SATEVPSREP EMKEKGDPEQ QNEVEEEEDD
     EDEDEDEDER QLLGEFEKEL EGILLPSDRE RLRAEVKAGM ERELENIIQE TEKELDPDGL
     KKESERDRAI LALTSTLNKL IKRLEEKQSP ELMKKHRKRR VVPKKPPPSP QSTEEDPEHR
     VRVRVTKLRH GGPNQDLTVL EMKRENPQLK QIEGLVKDLL EREGLTAEGK IEIKIVRPGT
     EGTEEDARWL TDEDTKNLKE IFFNILVQGA EEAQKERQRQ KELESNYRRV WGSPGGEGTG
     DLDEFDF