Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5BDB9 (OS9_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

Subunit structure

Interacts with missfolded ER lumenal proteins By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity.

Sequence similarities

Belongs to the OS-9 family.

Contains 1 PRKCSH domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainSignal
   LigandLectin
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 509486Protein OS-9 homolog
PRO_0000043270

Regions

Domain151 – 23080PRKCSH
Motif506 – 5094Prevents secretion from ER Potential

Sites

Binding site1731Carbohydrate By similarity
Binding site2461Carbohydrate By similarity
Binding site2521Carbohydrate By similarity
Binding site2731Carbohydrate By similarity
Binding site2791Carbohydrate By similarity

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Disulfide bond153 ↔ 166 By similarity
Disulfide bond245 ↔ 277 By similarity
Disulfide bond260 ↔ 289 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BDB9 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: AE1741546DB1DAA2

FASTA50957,548
        10         20         30         40         50         60 
MRRQSRIVAS LLVLACASSG AFAHRKFNVH DDLLAYPQFR IKFPDGFILE SQARAFLEQA 

        70         80         90        100        110        120 
PYSSPDLNDI SEQTPLKDES EESIRDGSSG EKAKFSYEEL SLEGQRYLCQ IPVVEDGDSN 

       130        140        150        160        170        180 
RTKVEVNEEE ERKELARATD RGLELLREME GKCLYYISGW WSYSFCYMNQ IKQFHALPSG 

       190        200        210        220        230        240 
GGVPNYPPME DHTTHSFILG RFPQEEGQDE GKGAKSGKSS TELAELQTKG GSRYLVQRLE 

       250        260        270        280        290        300 
SGDQCDLTGK NRKIEVQFHC NPQSTDRIAW IKELYTCSYL MLIYTPRLCN DVAFLPPQQE 

       310        320        330        340        350        360 
EVHTIECREI LTPEEVTGWQ AMHEYQLSQQ LVESAEAPKH QVIGGIEVGA QRLVGTEGKR 

       370        380        390        400        410        420 
IEKGRVASIG EEKVDVVAKR VNGEVQLLSA EELKKFDLDE AKIEELRKKL EEWAKGKDWT 

       430        440        450        460        470        480 
LEIVTGNGAY LRGVVDTDED EEDGYENEEG ETDKREQREN TQETTGQPGQ PGHQEETESG 

       490        500 
QAGHPMDDRS EDGEDPDVDG SEEIFKDEL

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000022 Genomic DNA. Translation: EAA64591.1.
BN001307 Genomic DNA. Translation: CBF84906.1.
RefSeqXP_659065.1. XM_653973.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00008077.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008077; CADANIAP00008077; CADANIAG00008077.
GeneID2875379.
KEGGani:AN1461.2.

Phylogenomic databases

eggNOGNOG309879.
HOGENOMHOG000157538.
KOK10088.
OMASGWWSYS.
OrthoDBEOG4PCF2J.

Family and domain databases

InterProIPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR012913. PRKCSH.
[Graphical view]
PfamPF07915. PRKCSH. 1 hit.
[Graphical view]
SUPFAMSSF50911. Man6php_recept. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOS9_EMENI
AccessionPrimary (citable) accession number: Q5BDB9
Secondary accession number(s): C8VMD1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: April 26, 2005
Last modified: April 3, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents