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Q99220

- OS9_YEAST

UniProt

Q99220 - OS9_YEAST

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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

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

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
Complete GO annotation...

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. luminal surveillance complex Source: SGD
  3. membrane Source: UniProtKB-KW
Complete GO annotation...

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.
InParanoidiQ99220.
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

        10         20         30         40         50
MQAKIIYALS AISALIPLGS SLLAPIEDPI VSNKYLISYI DEDDWSDRIL
60 70 80 90 100
QNQSVMNSGY IVNMGDDLEC FIQNASTQLN DVLEDSNEHS NSEKTALLTK
110 120 130 140 150
TLNQGVKTIF DKLNERCIFY QAGFWIYEYC PGIEFVQFHG RVNTKTGEIV
160 170 180 190 200
NRDESLVYRL GKPKANVEER EFELLYDDVG YYISEIIGSG DICDVTGAER
210 220 230 240 250
MVEIQYVCGG SNSGPSTIQW VRETKICVYE AQVTIPELCN LELLAKNEDQ
260 270 280 290 300
KNASPILCRM PAKSKIGSNS IDLITKYEPI FLGSGIYFLR PFNTDERDKL
310 320 330 340 350
MVTDNAMSNW DEITETYYQK FGNAINKMLS LRLVSLPNGH ILQPGDSCVW
360 370 380 390 400
LAEVVDMKDR FQTTLSLNIL NSQRAEIFFN KTFTFNEDNG NFLSYKIGDH
410 420 430 440 450
GESTELGQIT HSNKADINTA EIRSDEYLIN TDNELFLRIS KEIAEVKELL
460 470 480 490 500
NEIVSPHEME VIFENMRNQP NNDFELALMN KLKSSLNDDN KVEQINNARM
510 520 530 540
DDDESTSHTT RDIGEAGSQT TGNTESEVTN VAAGVFIEHD EL
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.
InParanoidi Q99220.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 103 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