OS9_HUMAN
ID OS9_HUMAN Reviewed; 667 AA.
AC Q13438; A6NDD1; A6NFR7; A6NLB2; A8K5Q9; B4DE28; B4DPX1; B4E1I6; E7ENT8;
AC E7EW91; F8VUH2; G3XA88; O00579; Q6IBL2; Q8IZ58; Q9BW99;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein OS-9;
DE AltName: Full=Amplified in osteosarcoma 9;
DE Flags: Precursor;
GN Name=OS9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8634085;
RX DOI=10.1002/(sici)1098-2744(199604)15:4<270::aid-mc4>3.0.co;2-k;
RA Su Y.A., Hutter C.M., Trent J.M., Meltzer P.S.;
RT "Complete sequence analysis of a gene (OS-9) ubiquitously expressed in
RT human tissues and amplified in sarcomas.";
RL Mol. Carcinog. 15:270-275(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9498564; DOI=10.1093/oxfordjournals.jbchem.a021880;
RA Kimura Y., Nakazawa M., Tsuchiya N., Asakawa S., Shimizu N., Yamada M.;
RT "Genomic organization of the OS-9 gene amplified in human sarcomas.";
RL J. Biochem. 122:1190-1195(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), CHARACTERIZATION, AND
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
RC TISSUE=Promyelocytic leukemia;
RX PubMed=9562620; DOI=10.1093/oxfordjournals.jbchem.a022019;
RA Kimura Y., Nakazawa M., Yamada M.;
RT "Cloning and characterization of three isoforms of OS-9 cDNA and expression
RT of the OS-9 gene in various human tumor cell lines.";
RL J. Biochem. 123:876-882(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4; 5; 6 AND 8), AND
RP VARIANT ASN-305.
RC TISSUE=Brain, Tongue, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-667.
RX PubMed=9192850; DOI=10.1006/geno.1997.4727;
RA Elkahloun A.G., Krizman D.B., Wang Z., Hofmann T.A., Roe B.A.,
RA Meltzer P.S.;
RT "Transcript mapping in a 46-kb sequenced region at the core of 12q13.3
RT amplification in human cancers.";
RL Genomics 42:295-301(1997).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=10403379; DOI=10.1016/s0014-5793(99)00700-0;
RA Nakayama T., Yaoi T., Kuwajima G., Yoshie O., Sakata T.;
RT "Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain
RT protein family, with OS-9, the product of a gene frequently amplified in
RT osteosarcoma.";
RL FEBS Lett. 453:77-80(1999).
RN [11]
RP FUNCTION IN TRPV4 MATURATION.
RX PubMed=17932042; DOI=10.1074/jbc.m703903200;
RA Wang Y., Fu X., Gaiser S., Koettgen M., Kramer-Zucker A., Walz G.,
RA Wegierski T.;
RT "OS-9 regulates the transit and polyubiquitination of TRPV4 in the
RT endoplasmic reticulum.";
RL J. Biol. Chem. 282:36561-36570(2007).
RN [12]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP DISULFIDE BONDS, GLYCOSYLATION, INDUCTION, AND MUTAGENESIS OF ARG-188.
RX PubMed=18417469; DOI=10.1074/jbc.m802272200;
RA Bernasconi R., Pertel T., Luban J., Molinari M.;
RT "A dual task for the Xbp1-responsive OS-9 variants in the mammalian
RT endoplasmic reticulum: inhibiting secretion of misfolded protein conformers
RT and enhancing their disposal.";
RL J. Biol. Chem. 283:16446-16454(2008).
RN [13]
RP INTERACTION WITH ERLEC1; HSPA5; SEL1L AND SYVN1.
RX PubMed=18502753; DOI=10.1074/jbc.m709336200;
RA Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.;
RT "Human XTP3-B forms an endoplasmic reticulum quality control scaffold with
RT the HRD1-SEL1L ubiquitin ligase complex and BiP.";
RL J. Biol. Chem. 283:20914-20924(2008).
RN [14]
RP FUNCTION, INTERACTION WITH HSP90B1; SEL1L AND SYVN1, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND MUTAGENESIS OF ARG-188.
RX PubMed=18264092; DOI=10.1038/ncb1689;
RA Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.;
RT "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L
RT ubiquitin ligase complex for ERAD.";
RL Nat. Cell Biol. 10:272-282(2008).
RN [15]
RP FUNCTION AS A LECTIN, AND MUTAGENESIS OF ARG-188.
RX PubMed=19346256; DOI=10.1074/jbc.m809725200;
RA Hosokawa N., Kamiya Y., Kamiya D., Kato K., Nagata K.;
RT "Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-
RT associated degradation, recognizes mannose-trimmed N-glycans.";
RL J. Biol. Chem. 284:17061-17068(2009).
RN [16]
RP FUNCTION IN MISFOLDED GLYCOPROTEIN UBIQUITINATION, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, INTERACTION WITH DERL2; HRD1 AND SEL1L, AND INDUCTION BY ER
RP STRESS.
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).
RN [17]
RP INTERACTION WITH CREB3.
RX PubMed=20546900; DOI=10.1016/j.molimm.2010.04.019;
RA Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.A., Looman M.W.,
RA Hendriks I.A., Jansen B.J., Adema G.J.;
RT "DC-STAMP interacts with ER-resident transcription factor LUMAN which
RT becomes activated during DC maturation.";
RL Mol. Immunol. 47:1963-1973(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP IDENTIFICATION IN THE HRD1 COMPLEX.
RX PubMed=28827405; DOI=10.1242/jcs.206847;
RA Schulz J., Avci D., Queisser M.A., Gutschmidt A., Dreher L.S., Fenech E.J.,
RA Volkmar N., Hayashi Y., Hoppe T., Christianson J.C.;
RT "Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex
RT formation for ER-associated degradation (ERAD).";
RL J. Cell Sci. 130:3322-3335(2017).
RN [21] {ECO:0007744|PDB:3AIH}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 108-229 IN COMPLEX WITH
RP MANNOPENTAOSE, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=21172656; DOI=10.1016/j.molcel.2010.11.017;
RA Satoh T., Chen Y., Hu D., Hanashima S., Yamamoto K., Yamaguchi Y.;
RT "Structural basis for oligosaccharide recognition of misfolded
RT glycoproteins by OS-9 in ER-associated degradation.";
RL Mol. Cell 40:905-916(2010).
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. {ECO:0000269|PubMed:17932042,
CC ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469,
CC ECO:0000269|PubMed:19084021, ECO:0000269|PubMed:19346256,
CC ECO:0000269|PubMed:21172656}.
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 (PubMed:18502753, PubMed:18264092,
CC PubMed:19084021, PubMed:28827405). Through this complex, may interact
CC with ERLEC1 and HSPA5 (PubMed:18502753). Interacts with HSP90B1
CC (PubMed:18264092). Interacts with CREB3 (PubMed:20546900).
CC {ECO:0000250|UniProtKB:Q8K2C7, ECO:0000269|PubMed:18264092,
CC ECO:0000269|PubMed:18502753, ECO:0000269|PubMed:19084021,
CC ECO:0000269|PubMed:20546900, ECO:0000269|PubMed:28827405}.
CC -!- INTERACTION:
CC Q13438; Q9GZT9: EGLN1; NbExp=4; IntAct=EBI-725454, EBI-1174818;
CC Q13438; Q9H6Z9: EGLN3; NbExp=2; IntAct=EBI-725454, EBI-1175354;
CC Q13438; O75460-1: ERN1; NbExp=2; IntAct=EBI-725454, EBI-15600828;
CC Q13438; Q16665: HIF1A; NbExp=9; IntAct=EBI-725454, EBI-447269;
CC Q13438; Q9UBV2: SEL1L; NbExp=11; IntAct=EBI-725454, EBI-358766;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469,
CC ECO:0000269|PubMed:19084021}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=OS-9-1;
CC IsoId=Q13438-1; Sequence=Displayed;
CC Name=2; Synonyms=OS-9-2;
CC IsoId=Q13438-2; Sequence=VSP_004353;
CC Name=3; Synonyms=OS-9-3;
CC IsoId=Q13438-3; Sequence=VSP_004352, VSP_004353;
CC Name=4;
CC IsoId=Q13438-4; Sequence=VSP_004352;
CC Name=5;
CC IsoId=Q13438-5; Sequence=VSP_044701, VSP_044702, VSP_004353;
CC Name=6;
CC IsoId=Q13438-6; Sequence=VSP_046001, VSP_004353;
CC Name=7;
CC IsoId=Q13438-7; Sequence=VSP_044702, VSP_004353;
CC Name=8;
CC IsoId=Q13438-8; Sequence=VSP_046770, VSP_004352, VSP_004353;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Found as well in all tumor
CC cell lines analyzed, amplified in sarcomas. Highly expressed in
CC osteosarcoma SJSA-1 and rhabdomyosarcoma Rh30 cell lines. Isoform 2 is
CC the major isoform detected in all cell types examined.
CC -!- INDUCTION: Up-regulated in response to endoplasmic reticulum stress (at
CC protein level). {ECO:0000269|PubMed:18417469,
CC ECO:0000269|PubMed:19084021}.
CC -!- PTM: Intramolecular disulfide bonds.
CC -!- PTM: Isoform 1 and isoform 2 are N-glycosylated.
CC {ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469,
CC ECO:0000269|PubMed:19084021}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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DR EMBL; U41635; AAB06495.1; -; mRNA.
DR EMBL; AB002805; BAA24362.1; -; Genomic_DNA.
DR EMBL; AB002806; BAA24363.1; -; mRNA.
DR EMBL; AK291374; BAF84063.1; -; mRNA.
DR EMBL; AK293435; BAG56939.1; -; mRNA.
DR EMBL; AK296770; BAG59349.1; -; mRNA.
DR EMBL; AK298532; BAG60733.1; -; mRNA.
DR EMBL; AK303858; BAG64798.1; -; mRNA.
DR EMBL; CR456791; CAG33072.1; -; mRNA.
DR EMBL; AC025165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97045.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97046.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97047.1; -; Genomic_DNA.
DR EMBL; BC000532; AAH00532.1; -; mRNA.
DR EMBL; BC007254; AAH07254.1; -; mRNA.
DR EMBL; BC023513; AAH23513.2; -; mRNA.
DR EMBL; U81031; AAC39523.2; -; Genomic_DNA.
DR CCDS; CCDS31843.1; -. [Q13438-1]
DR CCDS; CCDS31844.1; -. [Q13438-2]
DR CCDS; CCDS31845.1; -. [Q13438-4]
DR CCDS; CCDS31846.1; -. [Q13438-3]
DR CCDS; CCDS58246.1; -. [Q13438-6]
DR CCDS; CCDS58247.1; -. [Q13438-7]
DR CCDS; CCDS58248.1; -. [Q13438-5]
DR CCDS; CCDS58249.1; -. [Q13438-8]
DR PIR; JC5889; JC5889.
DR RefSeq; NP_001017956.1; NM_001017956.2. [Q13438-2]
DR RefSeq; NP_001017957.1; NM_001017957.2. [Q13438-3]
DR RefSeq; NP_001017958.1; NM_001017958.2. [Q13438-4]
DR RefSeq; NP_001248349.1; NM_001261420.1. [Q13438-7]
DR RefSeq; NP_001248350.1; NM_001261421.1. [Q13438-5]
DR RefSeq; NP_001248351.1; NM_001261422.1. [Q13438-6]
DR RefSeq; NP_001248352.1; NM_001261423.1. [Q13438-8]
DR RefSeq; NP_006803.1; NM_006812.3. [Q13438-1]
DR PDB; 3AIH; X-ray; 2.10 A; A/B=108-229.
DR PDBsum; 3AIH; -.
DR AlphaFoldDB; Q13438; -.
DR SMR; Q13438; -.
DR BioGRID; 116156; 233.
DR CORUM; Q13438; -.
DR DIP; DIP-37493N; -.
DR IntAct; Q13438; 104.
DR MINT; Q13438; -.
DR STRING; 9606.ENSP00000318165; -.
DR TCDB; 8.A.67.1.1; the os-9 quality control (erad) protein (os-9) family.
DR UniLectin; Q13438; -.
DR GlyConnect; 1666; 8 N-Linked glycans (1 site).
DR GlyGen; Q13438; 2 sites, 10 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q13438; -.
DR PhosphoSitePlus; Q13438; -.
DR BioMuta; OS9; -.
DR DMDM; 3024310; -.
DR EPD; Q13438; -.
DR jPOST; Q13438; -.
DR MassIVE; Q13438; -.
DR MaxQB; Q13438; -.
DR PaxDb; Q13438; -.
DR PeptideAtlas; Q13438; -.
DR PRIDE; Q13438; -.
DR ProteomicsDB; 17218; -.
DR ProteomicsDB; 18799; -.
DR ProteomicsDB; 28738; -.
DR ProteomicsDB; 33680; -.
DR ProteomicsDB; 59432; -. [Q13438-1]
DR ProteomicsDB; 59433; -. [Q13438-2]
DR ProteomicsDB; 59434; -. [Q13438-3]
DR ProteomicsDB; 59435; -. [Q13438-4]
DR Antibodypedia; 2459; 289 antibodies from 29 providers.
DR DNASU; 10956; -.
DR Ensembl; ENST00000257966.12; ENSP00000257966.8; ENSG00000135506.16. [Q13438-7]
DR Ensembl; ENST00000315970.12; ENSP00000318165.7; ENSG00000135506.16. [Q13438-1]
DR Ensembl; ENST00000389142.9; ENSP00000373794.5; ENSG00000135506.16. [Q13438-3]
DR Ensembl; ENST00000389146.10; ENSP00000373798.6; ENSG00000135506.16. [Q13438-4]
DR Ensembl; ENST00000435406.6; ENSP00000389632.2; ENSG00000135506.16. [Q13438-6]
DR Ensembl; ENST00000439210.6; ENSP00000407360.2; ENSG00000135506.16. [Q13438-8]
DR Ensembl; ENST00000551035.5; ENSP00000447866.1; ENSG00000135506.16. [Q13438-5]
DR Ensembl; ENST00000552285.5; ENSP00000450010.1; ENSG00000135506.16. [Q13438-2]
DR GeneID; 10956; -.
DR KEGG; hsa:10956; -.
DR MANE-Select; ENST00000315970.12; ENSP00000318165.7; NM_006812.4; NP_006803.1.
DR UCSC; uc001spj.4; human. [Q13438-1]
DR CTD; 10956; -.
DR DisGeNET; 10956; -.
DR GeneCards; OS9; -.
DR HGNC; HGNC:16994; OS9.
DR HPA; ENSG00000135506; Low tissue specificity.
DR MIM; 609677; gene.
DR neXtProt; NX_Q13438; -.
DR OpenTargets; ENSG00000135506; -.
DR PharmGKB; PA164724245; -.
DR VEuPathDB; HostDB:ENSG00000135506; -.
DR eggNOG; KOG3394; Eukaryota.
DR GeneTree; ENSGT00530000063603; -.
DR HOGENOM; CLU_026715_0_0_1; -.
DR InParanoid; Q13438; -.
DR OMA; WLKRLYV; -.
DR OrthoDB; 1475416at2759; -.
DR PhylomeDB; Q13438; -.
DR TreeFam; TF314309; -.
DR PathwayCommons; Q13438; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR SignaLink; Q13438; -.
DR SIGNOR; Q13438; -.
DR BioGRID-ORCS; 10956; 29 hits in 1088 CRISPR screens.
DR ChiTaRS; OS9; human.
DR EvolutionaryTrace; Q13438; -.
DR GeneWiki; OS9_(gene); -.
DR GenomeRNAi; 10956; -.
DR Pharos; Q13438; Tbio.
DR PRO; PR:Q13438; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q13438; protein.
DR Bgee; ENSG00000135506; Expressed in calcaneal tendon and 211 other tissues.
DR ExpressionAtlas; Q13438; baseline and differential.
DR Genevisible; Q13438; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; NAS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
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; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006621; P:protein retention in ER lumen; IDA:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP: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 3D-structure; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Lectin; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..667
FT /note="Protein OS-9"
FT /id="PRO_0000021951"
FT DOMAIN 108..230
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 284..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..483
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 633..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
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:0000269|PubMed:21172656,
FT ECO:0007744|PDB:3AIH"
FT BINDING 118
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000269|PubMed:21172656,
FT ECO:0007744|PDB:3AIH"
FT BINDING 130
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000269|PubMed:21172656,
FT ECO:0007744|PDB:3AIH"
FT BINDING 182
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000269|PubMed:21172656,
FT ECO:0007744|PDB:3AIH"
FT BINDING 188
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000269|PubMed:21172656,
FT ECO:0007744|PDB:3AIH"
FT BINDING 212
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000269|PubMed:21172656,
FT ECO:0007744|PDB:3AIH"
FT BINDING 218
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000269|PubMed:21172656,
FT ECO:0007744|PDB:3AIH"
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"
FT VAR_SEQ 55..113
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046770"
FT VAR_SEQ 142..193
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046001"
FT VAR_SEQ 161..193
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044701"
FT VAR_SEQ 263
FT /note="A -> AV (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044702"
FT VAR_SEQ 456..470
FT /note="Missing (in isoform 3, isoform 4 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_004352"
FT VAR_SEQ 534..588
FT /note="Missing (in isoform 2, isoform 3, isoform 5, isoform
FT 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_004353"
FT VARIANT 305
FT /note="D -> N (in dbSNP:rs141986192)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_069062"
FT VARIANT 398
FT /note="R -> W (in dbSNP:rs1804598)"
FT /id="VAR_011897"
FT VARIANT 454
FT /note="S -> L (in dbSNP:rs34764811)"
FT /id="VAR_034364"
FT MUTAGEN 188
FT /note="R->A: Loss of glycan-binding activity and partial
FT inhibition of ERAD of the misfolded glycoprotein NHK
FT (PubMed:19346256). Reduced interaction with SEL1L
FT (PubMed:18264092) not confirmed in (PubMed:19346256)."
FT /evidence="ECO:0000269|PubMed:18264092,
FT ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19346256"
FT CONFLICT 7
FT /note="L -> V (in Ref. 5; CAG33072)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="F -> V (in Ref. 4; BAG64798)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="E -> G (in Ref. 4; BAG56939)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="L -> F (in Ref. 4; BAG64798)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="V -> I (in Ref. 4; BAG60733)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="S -> P (in Ref. 4; BAG56939)"
FT /evidence="ECO:0000305"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:3AIH"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3AIH"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3AIH"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3AIH"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:3AIH"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:3AIH"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3AIH"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:3AIH"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:3AIH"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:3AIH"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3AIH"
SQ SEQUENCE 667 AA; 75562 MW; 65BA3F66CEC58756 CRC64;
MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV
VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY
EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK ASKQHRLKRY HSQTYGNGSK
CDLNGRPREA EVRFLCDEGA GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA
PQAILCHPSL QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS
PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF QNNVQVKVIR
SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP EKERGDPERQ REMEEEEDED
EDEDEDEDER QLLGEFEKEL EGILLPSDRD RLRSEVKAGM ERELENIIQE TEKELDPDGL
KKESERDRAM LALTSTLNKL IKRLEEKQSP ELVKKHKKKR VVPKKPPPSP QPTEEDPEHR
VRVRVTKLRL GGPNQDLTVL EMKRENPQLK QIEGLVKELL EREGLTAAGK IEIKIVRPWA
EGTEEGARWL TDEDTRNLKE IFFNILVPGA EEAQKERQRQ KELESNYRRV WGSPGGEGTG
DLDEFDF
