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 27-MAR-2024, entry version 194. 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; P00533: EGFR; NbExp=3; IntAct=EBI-725454, EBI-297353; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 247. DR CORUM; Q13438; -. DR DIP; DIP-37493N; -. DR IntAct; Q13438; 107. 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 GlyCosmos; Q13438; 2 sites, 11 glycans. DR GlyGen; Q13438; 6 sites, 10 N-linked glycans (1 site), 2 O-linked glycans (5 sites). DR iPTMnet; Q13438; -. DR PhosphoSitePlus; Q13438; -. DR SwissPalm; Q13438; -. DR BioMuta; OS9; -. DR DMDM; 3024310; -. DR EPD; Q13438; -. DR jPOST; Q13438; -. DR MassIVE; Q13438; -. DR MaxQB; Q13438; -. DR PaxDb; 9606-ENSP00000318165; -. DR PeptideAtlas; 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 Pumba; Q13438; -. DR Antibodypedia; 2459; 311 antibodies from 29 providers. DR DNASU; 10956; -. DR Ensembl; ENST00000257966.13; ENSP00000257966.8; ENSG00000135506.17. [Q13438-7] DR Ensembl; ENST00000315970.12; ENSP00000318165.7; ENSG00000135506.17. [Q13438-1] DR Ensembl; ENST00000389142.10; ENSP00000373794.5; ENSG00000135506.17. [Q13438-3] DR Ensembl; ENST00000389146.11; ENSP00000373798.6; ENSG00000135506.17. [Q13438-4] DR Ensembl; ENST00000435406.6; ENSP00000389632.2; ENSG00000135506.17. [Q13438-6] DR Ensembl; ENST00000439210.6; ENSP00000407360.2; ENSG00000135506.17. [Q13438-8] DR Ensembl; ENST00000551035.5; ENSP00000447866.1; ENSG00000135506.17. [Q13438-5] DR Ensembl; ENST00000552285.6; ENSP00000450010.1; ENSG00000135506.17. [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 AGR; HGNC:16994; -. 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; 91536at2759; -. 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; 35 hits in 1167 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 213 other cell types or tissues. DR ExpressionAtlas; Q13438; baseline and differential. 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; Mannose-6-phosphate receptor binding domain; 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; OS-9-RELATED; 1. DR PANTHER; PTHR15414:SF5; PROTEIN OS-9; 1. DR Pfam; PF07915; PRKCSH; 1. DR SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 1. DR PROSITE; PS51914; MRH; 1. DR Genevisible; Q13438; HS. 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 //