Q99220 (OS9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein OS-9 homolog

Gene names

Name:	YOS9
Ordered Locus Names:	YDR057W
ORF Names:	D4222

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal
Ligand	Lectin
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.6Ref.7Ref.8. Source: SGD
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell luminal surveillance complex Inferred from direct assay PubMed 16873065. Source: SGD
Molecular_function	oligosaccharide binding Inferred from direct assay PubMed 19111666. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HRD1	Q08109	6	EBI-34938,EBI-37613
HRD3	Q05787	8	EBI-34938,EBI-31647
KAR2	P16474	2	EBI-34938,EBI-7876
PRC1	P00729	2	EBI-34938,EBI-4153
UBX2	Q04228	3	EBI-34938,EBI-27730

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 542

521

Protein OS-9 homolog

PRO_0000042758

Regions

Domain

115 – 190

76

PRKCSH

Motif

539 – 542

4

Prevents secretion from ER Potential

Sites

Binding site

137

1

Carbohydrate By similarity

Binding site

194

1

Carbohydrate By similarity

Binding site

200

1

Carbohydrate By similarity

Binding site

223

1

Carbohydrate By similarity

Binding site

229

1

Carbohydrate By similarity

Amino acid modifications

Glycosylation

52

1

N-linked (GlcNAc...) Potential

Glycosylation

74

1

N-linked (GlcNAc...) Potential

Glycosylation

380

1

N-linked (GlcNAc...) Potential

Disulfide bond

117 ↔ 130

By similarity

Disulfide bond

193 ↔ 227

By similarity

Disulfide bond

208 ↔ 239

By similarity

Experimental info

Mutagenesis

127

1

Y → A: Decrease of ER lumenal misfolded protein degradation. Ref.8

Mutagenesis

137

1

Q → E: Decrease of ER lumenal misfolded protein degradation. Ref.8

Mutagenesis

139

1

H → A: Decrease of ER lumenal misfolded protein degradation. Ref.8

Mutagenesis

200

1

R → A: Decrease of ER lumenal misfolded protein degradation. Ref.6 Ref.8

Mutagenesis

223

1

E → N: Decrease of ER lumenal misfolded protein degradation. Ref.6 Ref.8

Mutagenesis

229

1

Y → A or F: Decrease of ER lumenal misfolded protein degradation. Ref.6 Ref.8

Sequence conflict

25

1

P → L in CAA89086. Ref.2

Secondary structure

1

.

.

.

.

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542

Helix Strand Turn

Details...

Beta strand

276 – 283

8

Beta strand

286 – 293

8

Beta strand

299 – 302

4

Helix

305 – 307

3

Beta strand

310 – 312

3

Helix

315 – 330

16

Beta strand

347 – 355

9

Beta strand

361 – 369

9

Beta strand

371 – 373

3

Beta strand

375 – 380

6

Beta strand

391 – 396

6

Sequences

	Sequence		Length	Mass (Da)
	Q99220 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BF353A0278703BE8	FASTA	542	61,258
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.

PIR

S58837.

RefSeq

NP_010342.3. NM_001180365.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YMA	X-ray	2.54	A/B	266-424	[»]

ProteinModelPortal

Q99220.

SMR

Q99220. Positions 266-399.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99220. 10 interactions.

Proteomic databases

PaxDb

Q99220.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR057W; YDR057W; YDR057W.

GeneID

851627.

KEGG

sce:YDR057W.
sce:YDR061W.

Organism-specific databases

CYGD

YDR057w.

SGD

S000002464. YOS9.

Phylogenomic databases

eggNOG

NOG240935.

KO

K10088.

OMA

HEMEVIF.

OrthoDB

EOG4PCF2J.

Gene expression databases

Genevestigator

Q99220.

GermOnline

YDR057W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR012913. PRKCSH.
[Graphical view]

Pfam

PF07915. PRKCSH. 1 hit.
[Graphical view]

PROSITE

PS00014. ER_TARGET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

969169.

Entry information

Entry name

OS9_YEAST

Accession

Primary (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:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program