ID NPIII_ASPOR Reviewed; 639 AA.
AC Q2U1N5; Q7Z8T2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Extracellular metalloproteinase NpIII;
DE EC=3.4.24.-;
DE AltName: Full=Elastinolytic metalloproteinase NpIII;
DE AltName: Full=Fungalysin NpIII;
DE AltName: Full=Neutral protease III;
DE Flags: Precursor;
GN Name=NpIII; ORFNames=AO090138000160;
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 [GENOMIC DNA].
RC STRAIN=JCM02238;
RA Tanaka A., Takagi H.;
RT "New neutral protease of Aspergillus oryzae.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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: Secreted metalloproteinase that allows assimilation of
CC proteinaceous substrates. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expression is controlled by the prtT transcription factor.
CC -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR EMBL; AB041338; BAC78815.1; -; Genomic_DNA.
DR EMBL; AP007170; BAE64530.1; -; Genomic_DNA.
DR RefSeq; XP_001825663.1; XM_001825611.1.
DR AlphaFoldDB; Q2U1N5; -.
DR SMR; Q2U1N5; -.
DR STRING; 510516.Q2U1N5; -.
DR MEROPS; M36.001; -.
DR GlyCosmos; Q2U1N5; 5 sites, No reported glycans.
DR EnsemblFungi; BAE64530; BAE64530; AO090138000160.
DR GeneID; 5997764; -.
DR KEGG; aor:AO090138000160; -.
DR VEuPathDB; FungiDB:AO090138000160; -.
DR HOGENOM; CLU_012703_3_0_1; -.
DR OMA; TRATDYG; -.
DR OrthoDB; 2786251at2759; -.
DR Proteomes; UP000006564; Chromosome 6.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..245
FT /evidence="ECO:0000250"
FT /id="PRO_0000407193"
FT CHAIN 246..639
FT /note="Extracellular metalloproteinase NpIII"
FT /id="PRO_0000407194"
FT ACT_SITE 430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 70
FT /note="T -> A (in Ref. 1; BAC78815)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="L -> V (in Ref. 1; BAC78815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 71153 MW; 240A3FA25AC35299 CRC64;
MHMLLFIGAL ALPVFVCTQS CEPASLSPRL AGVDLEKFRL TPNAEYVDSD QQIPISTTNV
GLIEQSYVET AIKLVRETFP NATFRLREDH YVGDNGVAHV HFRQTVHNLD VDNGDFNVNV
GRDGSVFSYG NSFYTGPVPS ITQLTKRDFT DPVAALKFAL THLQLPITAE DVSVESTKHP
HKYVLRGTSG AVTNPKARLV YFVKPDGTLC LVWRVETDVD DNWLLTYVDA KTAEEIHGVV
DYVSEATFQV YGWGINDPGQ VDSRAVLTDP WDLKESPLTW FRDGQKNWTT TRGNNGIAQE
NINNLPTYLN NFRPDSPTQN FSYEYPAGGS PKDYINASIT QLFYTANAYH DLLYTLGFNE
KAGNFQWNNS GLGGKEKDYV ILNAQDGASR NNADFATPPD GSPARMRMYL FTHTTPPRDG
VFESGIVIHE YTHGLSMRLT GGPDNSRCLS AFESASMGEG WGDFMATAIR LKPSDTRATD
YGMGMWVYNN EKGIRQYLYS TSMETNPLNY TSLNRMWEAH AGGTVWASML YEVLWNLIDR
HGKNDGPRPT FDERGVPKDG KYLAMKIVID AMALQPCNPD FVQARNAILD ADQALTGGQN
KCEIWTGFAK RGLGQGAEYG RGRRVGSYDI PGDVCQKKI
//
