OS9_ASPFU
ID OS9_ASPFU Reviewed; 520 AA.
AC Q4WCG2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein OS-9 homolog;
DE Flags: Precursor;
GN Name=yos9; ORFNames=AFUA_8G04530;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 misfolded
CC endoplasmic reticulum lumenal glycoproteins for degradation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with missfolded ER lumenal proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|PROSITE-ProRule:PRU10138}; Peripheral membrane protein
CC {ECO:0000250}; Lumenal side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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DR EMBL; AAHF01000013; EAL85222.1; -; Genomic_DNA.
DR RefSeq; XP_747260.1; XM_742167.1.
DR AlphaFoldDB; Q4WCG2; -.
DR SMR; Q4WCG2; -.
DR STRING; 746128.CADAFUBP00008079; -.
DR PRIDE; Q4WCG2; -.
DR EnsemblFungi; EAL85222; EAL85222; AFUA_8G04530.
DR GeneID; 3504663; -.
DR KEGG; afm:AFUA_8G04530; -.
DR VEuPathDB; FungiDB:Afu8g04530; -.
DR eggNOG; KOG3394; Eukaryota.
DR HOGENOM; CLU_025069_0_0_1; -.
DR InParanoid; Q4WCG2; -.
DR OMA; GWWSYRF; -.
DR OrthoDB; 1475416at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
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:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
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_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR045149; OS-9-like.
DR InterPro; IPR012913; OS9-like_dom.
DR PANTHER; PTHR15414; PTHR15414; 1.
DR Pfam; PF07915; PRKCSH; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51914; MRH; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Lectin; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..520
FT /note="Protein OS-9 homolog"
FT /id="PRO_0000043266"
FT DOMAIN 161..302
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 121..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 517..520
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 461..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 171
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 183
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 257
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 263
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 284
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 290
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT DISULFID 163..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 256..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 271..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 520 AA; 58265 MW; CAD972BBB859CF98 CRC64;
MIRRIRTLTP LLVLACAGSG AWASKKAFNI QDDLLAYPQF QVFFPDEYIL DARARELLQN
QQESSSASAD KTFSEGNDAQ VYLGSRKDQS EDVNKETIEG SGFTYEEMLL EGQRYLCSIP
QVDNGNRDQT NGAESTSKED EQREIARATD RGLELLREME GKCMYYISGW WSYSFCYKKQ
IKQFHALPSG PGVPNYPPIE DSTTHSFVLG RFPNSGDDED LEGDAEHKKT TTDVAELQTK
GGSRYLVQRL GGGTKCDLTG KDRKIEVQFH CHPQSTDRIG WIKELTTCSY LMVIYTPRLC
NDVAFLPPQQ DEAHAIECRE ILSEEEVSDW EANREYHLAQ QLVESAITPE FPVVGDIEVG
AHKWVGSEGK QIEKGRVASI GEEKIEVVAK RQNGEITRLS KEELKKYGLD PEKIETLKSR
LEELAKGKDW TLEIVESNGE RGLVGTVDSN DDEKEDHAAQ GSISQPAQGT TADKGESNAE
TGEEKKKADE KIDHYEPEKS GPTTDDADDG SEEIFFKDEL
