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Q5BDB9

- OS9_EMENI

UniProt

Q5BDB9 - OS9_EMENI

Protein

Protein OS-9 homolog

Gene

yos9

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
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    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei173 – 1731CarbohydrateBy similarity
    Binding sitei246 – 2461CarbohydrateBy similarity
    Binding sitei252 – 2521CarbohydrateBy similarity
    Binding sitei273 – 2731CarbohydrateBy similarity
    Binding sitei279 – 2791CarbohydrateBy similarity

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein OS-9 homolog
    Gene namesi
    Name:yos9
    ORF Names:AN1461
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VII

    Subcellular locationi

    Endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein By similarity; Lumenal side By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 509486Protein OS-9 homologPRO_0000043270Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi153 ↔ 166By similarity
    Disulfide bondi245 ↔ 277By similarity
    Disulfide bondi260 ↔ 289By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Interacts with missfolded ER lumenal proteins.By similarity

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00008077.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini151 – 23080PRKCSHAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi506 – 5094Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG309879.
    HOGENOMiHOG000157538.
    KOiK10088.
    OMAiLCDDVAF.
    OrthoDBiEOG7R2BVR.

    Family and domain databases

    Gene3Di2.70.130.10. 1 hit.
    InterProiIPR009011. Man6P_isomerase_rcpt-bd_dom.
    IPR012913. PRKCSH.
    [Graphical view]
    PfamiPF07915. PRKCSH. 1 hit.
    [Graphical view]
    SUPFAMiSSF50911. SSF50911. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q5BDB9-1 [UniParc]FASTAAdd to Basket

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    MRRQSRIVAS LLVLACASSG AFAHRKFNVH DDLLAYPQFR IKFPDGFILE    50
    SQARAFLEQA PYSSPDLNDI SEQTPLKDES EESIRDGSSG EKAKFSYEEL 100
    SLEGQRYLCQ IPVVEDGDSN RTKVEVNEEE ERKELARATD RGLELLREME 150
    GKCLYYISGW WSYSFCYMNQ IKQFHALPSG GGVPNYPPME DHTTHSFILG 200
    RFPQEEGQDE GKGAKSGKSS TELAELQTKG GSRYLVQRLE SGDQCDLTGK 250
    NRKIEVQFHC NPQSTDRIAW IKELYTCSYL MLIYTPRLCN DVAFLPPQQE 300
    EVHTIECREI LTPEEVTGWQ AMHEYQLSQQ LVESAEAPKH QVIGGIEVGA 350
    QRLVGTEGKR IEKGRVASIG EEKVDVVAKR VNGEVQLLSA EELKKFDLDE 400
    AKIEELRKKL EEWAKGKDWT LEIVTGNGAY LRGVVDTDED EEDGYENEEG 450
    ETDKREQREN TQETTGQPGQ PGHQEETESG QAGHPMDDRS EDGEDPDVDG 500
    SEEIFKDEL 509
    Length:509
    Mass (Da):57,548
    Last modified:April 26, 2005 - v1
    Checksum:iAE1741546DB1DAA2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000022 Genomic DNA. Translation: EAA64591.1.
    BN001307 Genomic DNA. Translation: CBF84906.1.
    RefSeqiXP_659065.1. XM_653973.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00008077; CADANIAP00008077; CADANIAG00008077.
    GeneIDi2875379.
    KEGGiani:AN1461.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000022 Genomic DNA. Translation: EAA64591.1 .
    BN001307 Genomic DNA. Translation: CBF84906.1 .
    RefSeqi XP_659065.1. XM_653973.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00008077.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00008077 ; CADANIAP00008077 ; CADANIAG00008077 .
    GeneIDi 2875379.
    KEGGi ani:AN1461.2.

    Phylogenomic databases

    eggNOGi NOG309879.
    HOGENOMi HOG000157538.
    KOi K10088.
    OMAi LCDDVAF.
    OrthoDBi EOG7R2BVR.

    Family and domain databases

    Gene3Di 2.70.130.10. 1 hit.
    InterProi IPR009011. Man6P_isomerase_rcpt-bd_dom.
    IPR012913. PRKCSH.
    [Graphical view ]
    Pfami PF07915. PRKCSH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50911. SSF50911. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.

    Entry informationi

    Entry nameiOS9_EMENI
    AccessioniPrimary (citable) accession number: Q5BDB9
    Secondary accession number(s): C8VMD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 56 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3