OPSB_ASPOR
ID OPSB_ASPOR Reviewed; 487 AA.
AC Q8NKB6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable aspartic-type endopeptidase opsB;
DE EC=3.4.23.-;
DE AltName: Full=Oryzapsin B;
DE Flags: Precursor;
GN Name=opsB; ORFNames=AO090701000002;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=12036596; DOI=10.1016/s0378-1119(02)00547-4;
RA Kunihiro S., Kawanishi Y., Sano M., Naito K., Matsuura Y., Tateno Y.,
RA Gojobori T., Yamagata Y., Abe K., Machida M.;
RT "A polymerase chain reaction-based method for cloning novel members of a
RT gene family using a combination of degenerate and inhibitory primers.";
RL Gene 289:177-184(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Probable GPI-anchored aspartic-type endopeptidase.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB044078; BAC00848.1; -; mRNA.
DR EMBL; AP007164; BAE61766.1; -; Genomic_DNA.
DR RefSeq; XP_001822899.1; XM_001822847.2.
DR AlphaFoldDB; Q8NKB6; -.
DR SMR; Q8NKB6; -.
DR STRING; 510516.Q8NKB6; -.
DR EnsemblFungi; BAE61766; BAE61766; AO090701000002.
DR GeneID; 5994956; -.
DR KEGG; aor:AO090701000002; -.
DR VEuPathDB; FungiDB:AO090701000002; -.
DR HOGENOM; CLU_013253_9_3_1; -.
DR OMA; LYFMGGV; -.
DR Proteomes; UP000006564; Chromosome 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47965; PTHR47965; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..463
FT /note="Probable aspartic-type endopeptidase opsB"
FT /id="PRO_0000397706"
FT PROPEP 464..487
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397707"
FT DOMAIN 69..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT LIPID 463
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 487 AA; 51029 MW; AC9562ADA1702B26 CRC64;
MQKSWLVLLV ACLGLQGTTA LTLHRRDLPA VVSLDIKRNN AVDPVARDRM RRKRDKTVEQ
NLDNEETLYF CNITLGTPKQ SLRLVLDTGS SDLWCNAANS TLCSSRDQPC NASGSYDPSS
SSSYAYTSSD FNISYADGTG AAGDYVTDTI HIGGATVKDF QFGVGYSSSS AEGVLGIGYT
TNEVQVGRLG KSAYANLPQA MVKNGLIQSN AYSLWLNDLG ADTGSILFGG VNTEKYHGEL
QTLPIQTVNG VYSEFIIALT GVSLSSASSH HNYSSSDALP AAVLLDSGSS LTYLPNSIVQ
DIYDDLGVTY ESSSGVGYVP CSLAQQNINV TYTFSSPIIT VGIDELVLDA GDLRFRNGAR
ACIFGIVPAG DSTAVLGDTF LRSAYVVYDL SNNEISLANT KFNSTKDNIL EIGTGDDSVP
GATQVSNPVT SVVADGSGAR IGGPTGEIFT DIPSATSSGG AAAPAGPTDV PKHLVLGAAA
IGYVLAF
