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Q99220 (OS9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein OS-9 homolog
Gene names
Name:YOS9
Ordered Locus Names:YDR057W
ORF Names:D4222
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subunit structure

Interacts with missfolded ER lumenal proteins like PCR1. Interacts with the GPI-anchored proteins GAS1 and MKC7. Ref.4 Ref.6 Ref.7 Ref.8

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side Ref.4 Ref.7.

Domain

The MHR domain (mannose 6-phosphate receptor homology) is required for the ERAD-L activity. Ref.6 Ref.8

Sequence similarities

Belongs to the OS-9 family.

Contains 1 PRKCSH domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 542521Protein OS-9 homolog
PRO_0000042758

Regions

Domain115 – 19076PRKCSH
Motif539 – 5424Prevents secretion from ER Potential

Sites

Binding site1371Carbohydrate By similarity
Binding site1941Carbohydrate By similarity
Binding site2001Carbohydrate By similarity
Binding site2231Carbohydrate By similarity
Binding site2291Carbohydrate By similarity

Amino acid modifications

Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Disulfide bond117 ↔ 130 By similarity
Disulfide bond193 ↔ 227 By similarity
Disulfide bond208 ↔ 239 By similarity

Experimental info

Mutagenesis1271Y → A: Decrease of ER lumenal misfolded protein degradation. Ref.8
Mutagenesis1371Q → E: Decrease of ER lumenal misfolded protein degradation. Ref.8
Mutagenesis1391H → A: Decrease of ER lumenal misfolded protein degradation. Ref.8
Mutagenesis2001R → A: Decrease of ER lumenal misfolded protein degradation. Ref.6 Ref.8
Mutagenesis2231E → N: Decrease of ER lumenal misfolded protein degradation. Ref.6 Ref.8
Mutagenesis2291Y → A or F: Decrease of ER lumenal misfolded protein degradation. Ref.6 Ref.8
Sequence conflict251P → L in CAA89086. Ref.2

Secondary structure

....................... 542
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99220 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BF353A0278703BE8

FASTA54261,258
        10         20         30         40         50         60 
MQAKIIYALS AISALIPLGS SLLAPIEDPI VSNKYLISYI DEDDWSDRIL QNQSVMNSGY 

        70         80         90        100        110        120 
IVNMGDDLEC FIQNASTQLN DVLEDSNEHS NSEKTALLTK TLNQGVKTIF DKLNERCIFY 

       130        140        150        160        170        180 
QAGFWIYEYC PGIEFVQFHG RVNTKTGEIV NRDESLVYRL GKPKANVEER EFELLYDDVG 

       190        200        210        220        230        240 
YYISEIIGSG DICDVTGAER MVEIQYVCGG SNSGPSTIQW VRETKICVYE AQVTIPELCN 

       250        260        270        280        290        300 
LELLAKNEDQ KNASPILCRM PAKSKIGSNS IDLITKYEPI FLGSGIYFLR PFNTDERDKL 

       310        320        330        340        350        360 
MVTDNAMSNW DEITETYYQK FGNAINKMLS LRLVSLPNGH ILQPGDSCVW LAEVVDMKDR 

       370        380        390        400        410        420 
FQTTLSLNIL NSQRAEIFFN KTFTFNEDNG NFLSYKIGDH GESTELGQIT HSNKADINTA 

       430        440        450        460        470        480 
EIRSDEYLIN TDNELFLRIS KEIAEVKELL NEIVSPHEME VIFENMRNQP NNDFELALMN 

       490        500        510        520        530        540 
KLKSSLNDDN KVEQINNARM DDDESTSHTT RDIGEAGSQT TGNTESEVTN VAAGVFIEHD 


EL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84162 Genomic DNA. Translation: CAA58973.1.
Z74353 Genomic DNA. Translation: CAA98875.1.
Z49209 Genomic DNA. Translation: CAA89086.1.
BK006938 Genomic DNA. Translation: DAA11903.1.
PIRS58837.
RefSeqNP_010342.3. NM_001180365.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YMAX-ray2.54A/B266-424[»]
ProteinModelPortalQ99220.
SMRQ99220. Positions 266-399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32110. 43 interactions.
IntActQ99220. 11 interactions.
MINTMINT-6490923.

Proteomic databases

MaxQBQ99220.
PaxDbQ99220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR057W; YDR057W; YDR057W.
GeneID851627.
KEGGsce:YDR057W.

Organism-specific databases

CYGDYDR057w.
SGDS000002464. YOS9.

Phylogenomic databases

eggNOGNOG240935.
KOK10088.
OMAHEMEVIF.
OrthoDBEOG7R2BVR.

Enzyme and pathway databases

BioCycYEAST:G3O-29666-MONOMER.

Gene expression databases

GenevestigatorQ99220.

Family and domain databases

InterProIPR012913. PRKCSH.
[Graphical view]
PfamPF07915. PRKCSH. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969169.
PROQ99220.

Entry information

Entry nameOS9_YEAST
AccessionPrimary (citable) accession number: Q99220
Secondary accession number(s): D6VS43, Q04313
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references