(data stored in ACNUC16935 zone)

SWISSPROT: OS9_EMENI

ID   OS9_EMENI               Reviewed;         509 AA.
AC   Q5BDB9; C8VMD1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 70.
DE   RecName: Full=Protein OS-9 homolog;
DE   Flags: Precursor;
GN   Name=yos9; ORFNames=AN1461;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Lectin involved in the quality control of the secretory
CC       pathway. As a member of the endoplasmic reticulum-associated
CC       degradation lumenal (ERAD-L) surveillance system, targets
CC       misfolded endoplasmic reticulum lumenal glycoproteins for
CC       degradation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with missfolded ER lumenal proteins.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|PROSITE-ProRule:PRU10138}; Peripheral membrane
CC       protein {ECO:0000250}; Lumenal side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
DR   EMBL; AACD01000022; EAA64591.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF84906.1; -; Genomic_DNA.
DR   RefSeq; XP_659065.1; XM_653973.1.
DR   SMR; Q5BDB9; -.
DR   STRING; 162425.CADANIAP00008077; -.
DR   EnsemblFungi; CADANIAT00008077; CADANIAP00008077; CADANIAG00008077.
DR   EnsemblFungi; EAA64591; EAA64591; AN1461.2.
DR   GeneID; 2875379; -.
DR   KEGG; ani:AN1461.2; -.
DR   HOGENOM; HOG000157538; -.
DR   InParanoid; Q5BDB9; -.
DR   KO; K10088; -.
DR   OMA; IVQFHAL; -.
DR   OrthoDB; EOG092C4FPG; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   Gene3D; 2.70.130.10; -; 1.
DR   InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom.
DR   InterPro; IPR012913; PRKCSH.
DR   Pfam; PF07915; PRKCSH; 1.
DR   SUPFAM; SSF50911; SSF50911; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5BDB9.
DR   SWISS-2DPAGE; Q5BDB9.
KW   Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Lectin; Membrane; Reference proteome; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    509       Protein OS-9 homolog.
FT                                /FTId=PRO_0000043270.
FT   DOMAIN      151    230       PRKCSH.
FT   MOTIF       506    509       Prevents secretion from ER.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10138}.
FT   BINDING     173    173       Carbohydrate. {ECO:0000250}.
FT   BINDING     246    246       Carbohydrate. {ECO:0000250}.
FT   BINDING     252    252       Carbohydrate. {ECO:0000250}.
FT   BINDING     273    273       Carbohydrate. {ECO:0000250}.
FT   BINDING     279    279       Carbohydrate. {ECO:0000250}.
FT   CARBOHYD    120    120       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    153    166       {ECO:0000250}.
FT   DISULFID    245    277       {ECO:0000250}.
FT   DISULFID    260    289       {ECO:0000250}.
SQ   SEQUENCE   509 AA;  57548 MW;  AE1741546DB1DAA2 CRC64;
     MRRQSRIVAS LLVLACASSG AFAHRKFNVH DDLLAYPQFR IKFPDGFILE SQARAFLEQA
     PYSSPDLNDI SEQTPLKDES EESIRDGSSG EKAKFSYEEL SLEGQRYLCQ IPVVEDGDSN
     RTKVEVNEEE ERKELARATD RGLELLREME GKCLYYISGW WSYSFCYMNQ IKQFHALPSG
     GGVPNYPPME DHTTHSFILG RFPQEEGQDE GKGAKSGKSS TELAELQTKG GSRYLVQRLE
     SGDQCDLTGK NRKIEVQFHC NPQSTDRIAW IKELYTCSYL MLIYTPRLCN DVAFLPPQQE
     EVHTIECREI LTPEEVTGWQ AMHEYQLSQQ LVESAEAPKH QVIGGIEVGA QRLVGTEGKR
     IEKGRVASIG EEKVDVVAKR VNGEVQLLSA EELKKFDLDE AKIEELRKKL EEWAKGKDWT
     LEIVTGNGAY LRGVVDTDED EEDGYENEEG ETDKREQREN TQETTGQPGQ PGHQEETESG
     QAGHPMDDRS EDGEDPDVDG SEEIFKDEL
//

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