Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q99220

- OS9_YEAST

UniProt

Q99220 - OS9_YEAST

Protein

Protein OS-9 homolog

Gene

YOS9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei137 – 1371CarbohydrateBy similarity
    Binding sitei194 – 1941CarbohydrateBy similarity
    Binding sitei200 – 2001CarbohydrateBy similarity
    Binding sitei223 – 2231CarbohydrateBy similarity
    Binding sitei229 – 2291CarbohydrateBy similarity

    GO - Molecular functioni

    1. oligosaccharide binding Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. endoplasmic reticulum unfolded protein response Source: SGD
    2. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
    3. retrograde protein transport, ER to cytosol Source: SGD

    Keywords - Ligandi

    Lectin

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29666-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein OS-9 homolog
    Gene namesi
    Name:YOS9
    Ordered Locus Names:YDR057W
    ORF Names:D4222
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR057w.
    SGDiS000002464. YOS9.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 PublicationsPROSITE-ProRule annotation; Peripheral membrane protein 2 Publications; Lumenal side 2 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. luminal surveillance complex Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Interaction of substrate with HRD1 is reduced; in YOS9 and USA1 double mutants this interaction is completely abolished. Interaction of substrate (either glycosylated or non-glycosylated) with HRD3 is not affected.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi127 – 1271Y → A: Decrease of ER lumenal misfolded protein degradation. 1 Publication
    Mutagenesisi137 – 1371Q → E: Decrease of ER lumenal misfolded protein degradation. 1 Publication
    Mutagenesisi139 – 1391H → A: Decrease of ER lumenal misfolded protein degradation. 1 Publication
    Mutagenesisi200 – 2001R → A: Decrease of ER lumenal misfolded protein degradation. No effect on interaction with CDC48, HRD3, KAR2, UBX2, HRD1 or EMP47. 3 Publications
    Mutagenesisi223 – 2231E → N: Decrease of ER lumenal misfolded protein degradation. 2 Publications
    Mutagenesisi229 – 2291Y → A or F: Decrease of ER lumenal misfolded protein degradation. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 542521Protein OS-9 homologPRO_0000042758Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi117 ↔ 130By similarity
    Disulfide bondi193 ↔ 227By similarity
    Disulfide bondi208 ↔ 239By similarity
    Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ99220.
    PaxDbiQ99220.

    Expressioni

    Gene expression databases

    GenevestigatoriQ99220.

    Interactioni

    Subunit structurei

    Component of the HRD1 complex which contains HRD1, HRD3, USA1, DER1, YOS9, CDC48, NPL4, UFD1 AND UBX2/SEL1. The complex is composed of the core membrane complex, consisting of the E3 ligase HRD1 and its cofactors HRD3, DER1 and USA1, the substrate recruiting factor YOS9, and the heterotrimeric UFD1-NPL4-CDC48/p97 (UNC) ATPase complex recruited by UBX2/SEL1. Interacts with DER1, USA1, UBX2, CDC48, HRD1, KAR2 and HRD3. Interacts with EMP47. Interacts with misfolded ER lumenal proteins like PCR1. Interacts with the GPI-anchored proteins GAS1 and MKC7.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HRD1Q081096EBI-34938,EBI-37613
    HRD3Q057878EBI-34938,EBI-31647
    KAR2P164742EBI-34938,EBI-7876
    PRC1P007292EBI-34938,EBI-4153
    UBX2Q042283EBI-34938,EBI-27730

    Protein-protein interaction databases

    BioGridi32110. 43 interactions.
    IntActiQ99220. 11 interactions.
    MINTiMINT-6490923.

    Structurei

    Secondary structure

    1
    542
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi276 – 2838
    Beta strandi286 – 2938
    Beta strandi299 – 3024
    Helixi305 – 3073
    Beta strandi310 – 3123
    Helixi315 – 33016
    Beta strandi347 – 3559
    Beta strandi361 – 3699
    Beta strandi371 – 3733
    Beta strandi375 – 3806
    Beta strandi391 – 3966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YMAX-ray2.54A/B266-424[»]
    ProteinModelPortaliQ99220.
    SMRiQ99220. Positions 266-399.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini115 – 19076PRKCSHAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi539 – 5424Prevents secretion from ERPROSITE-ProRule annotation

    Domaini

    The MHR domain (mannose 6-phosphate receptor homology) is required for the ERAD-L activity.2 Publications

    Sequence similaritiesi

    Belongs to the OS-9 family.Curated
    Contains 1 PRKCSH domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG240935.
    KOiK10088.
    OMAiHEMEVIF.
    OrthoDBiEOG7R2BVR.

    Family and domain databases

    InterProiIPR012913. PRKCSH.
    [Graphical view]
    PfamiPF07915. PRKCSH. 1 hit.
    [Graphical view]
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99220-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQAKIIYALS AISALIPLGS SLLAPIEDPI VSNKYLISYI DEDDWSDRIL    50
    QNQSVMNSGY IVNMGDDLEC FIQNASTQLN DVLEDSNEHS NSEKTALLTK 100
    TLNQGVKTIF DKLNERCIFY QAGFWIYEYC PGIEFVQFHG RVNTKTGEIV 150
    NRDESLVYRL GKPKANVEER EFELLYDDVG YYISEIIGSG DICDVTGAER 200
    MVEIQYVCGG SNSGPSTIQW VRETKICVYE AQVTIPELCN LELLAKNEDQ 250
    KNASPILCRM PAKSKIGSNS IDLITKYEPI FLGSGIYFLR PFNTDERDKL 300
    MVTDNAMSNW DEITETYYQK FGNAINKMLS LRLVSLPNGH ILQPGDSCVW 350
    LAEVVDMKDR FQTTLSLNIL NSQRAEIFFN KTFTFNEDNG NFLSYKIGDH 400
    GESTELGQIT HSNKADINTA EIRSDEYLIN TDNELFLRIS KEIAEVKELL 450
    NEIVSPHEME VIFENMRNQP NNDFELALMN KLKSSLNDDN KVEQINNARM 500
    DDDESTSHTT RDIGEAGSQT TGNTESEVTN VAAGVFIEHD EL 542
    Length:542
    Mass (Da):61,258
    Last modified:November 1, 1996 - v1
    Checksum:iBF353A0278703BE8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251P → L in CAA89086. (PubMed:9169867)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84162 Genomic DNA. Translation: CAA58973.1.
    Z74353 Genomic DNA. Translation: CAA98875.1.
    Z49209 Genomic DNA. Translation: CAA89086.1.
    BK006938 Genomic DNA. Translation: DAA11903.1.
    PIRiS58837.
    RefSeqiNP_010342.3. NM_001180365.3.

    Genome annotation databases

    EnsemblFungiiYDR057W; YDR057W; YDR057W.
    GeneIDi851627.
    KEGGisce:YDR057W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84162 Genomic DNA. Translation: CAA58973.1 .
    Z74353 Genomic DNA. Translation: CAA98875.1 .
    Z49209 Genomic DNA. Translation: CAA89086.1 .
    BK006938 Genomic DNA. Translation: DAA11903.1 .
    PIRi S58837.
    RefSeqi NP_010342.3. NM_001180365.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YMA X-ray 2.54 A/B 266-424 [» ]
    ProteinModelPortali Q99220.
    SMRi Q99220. Positions 266-399.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32110. 43 interactions.
    IntActi Q99220. 11 interactions.
    MINTi MINT-6490923.

    Proteomic databases

    MaxQBi Q99220.
    PaxDbi Q99220.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR057W ; YDR057W ; YDR057W .
    GeneIDi 851627.
    KEGGi sce:YDR057W.

    Organism-specific databases

    CYGDi YDR057w.
    SGDi S000002464. YOS9.

    Phylogenomic databases

    eggNOGi NOG240935.
    KOi K10088.
    OMAi HEMEVIF.
    OrthoDBi EOG7R2BVR.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29666-MONOMER.

    Miscellaneous databases

    NextBioi 969169.
    PROi Q99220.

    Gene expression databases

    Genevestigatori Q99220.

    Family and domain databases

    InterProi IPR012913. PRKCSH.
    [Graphical view ]
    Pfami PF07915. PRKCSH. 1 hit.
    [Graphical view ]
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV."
      Brandt P., Ramlow S., Otto B., Bloecker H.
      Yeast 12:85-90(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins."
      Friedmann E., Salzberg Y., Weinberger A., Shaltiel S., Gerst J.E.
      J. Biol. Chem. 277:35274-35281(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH GAS1 AND MKC7.
    5. "A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins."
      Buschhorn B.A., Kostova Z., Medicherla B., Wolf D.H.
      FEBS Lett. 577:422-426(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen."
      Bhamidipati A., Denic V., Quan E.M., Weissman J.S.
      Mol. Cell 19:741-751(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, INTERACTION WITH MISFOLDED PRC1, MUTAGENESIS OF ARG-200; GLU-223 AND TYR-229.
    7. "Yos9p detects and targets misfolded glycoproteins for ER-associated degradation."
      Kim W., Spear E.D., Ng D.T.W.
      Mol. Cell 19:753-764(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MISFOLDED PRC1.
    8. "Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD."
      Szathmary R., Bielmann R., Nita-Lazar M., Burda P., Jakob C.A.
      Mol. Cell 19:765-775(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, INTERACTION WITH MISFOLDED PRC1, MUTAGENESIS OF TYR-127; GLN-137; HIS-139; ARG-200; GLU-223 AND TYR-229.
    9. "A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation."
      Denic V., Quan E.M., Weissman J.S.
      Cell 126:349-359(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE HRD1 COMPLEX, INTERACTION WITH CDC48; UBX2; HRD1; KAR2; HRD3 AND EMP47, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-200.
    10. "Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins."
      Carvalho P., Goder V., Rapoport T.A.
      Cell 126:361-373(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE HRD1 COMPLEX, INTERACTION WITH HRD1; UBX2; HRD3; USA1; CDC48 AND DER1.
    11. "Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p."
      Carvalho P., Stanley A.M., Rapoport T.A.
      Cell 143:579-591(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiOS9_YEAST
    AccessioniPrimary (citable) accession number: Q99220
    Secondary accession number(s): D6VS43, Q04313
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3