NPI_ASPOR
ID NPI_ASPOR Reviewed; 634 AA.
AC Q2U1G7; Q9UVW4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Extracellular metalloproteinase NpI;
DE EC=3.4.24.-;
DE AltName: Full=Elastinolytic metalloproteinase NpI;
DE AltName: Full=Fungalysin NpI;
DE AltName: Full=Neutral protease I;
DE Flags: Precursor;
GN Name=NpI; ORFNames=AO090011000036;
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].
RA Doumas A., Crameri R., Monod M.;
RT "Cloning and characterization of the gene encoding neutral protease I of
RT the koji mold Aspergillus oryzae.";
RL Submitted (OCT-1998) 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).
RN [3]
RP INDUCTION.
RX PubMed=18930158; DOI=10.1016/j.fgb.2008.09.007;
RA Punt P.J., Schuren F.H., Lehmbeck J., Christensen T., Hjort C.,
RA van den Hondel C.A.;
RT "Characterization of the Aspergillus niger prtT, a unique regulator of
RT extracellular protease encoding genes.";
RL Fungal Genet. Biol. 45:1591-1599(2008).
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 {ECO:0000269|PubMed:18930158}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR EMBL; AF099904; AAF04628.1; -; Genomic_DNA.
DR EMBL; AP007171; BAE64598.1; -; Genomic_DNA.
DR RefSeq; XP_001825731.1; XM_001825679.2.
DR AlphaFoldDB; Q2U1G7; -.
DR SMR; Q2U1G7; -.
DR MEROPS; M36.001; -.
DR EnsemblFungi; BAE64598; BAE64598; AO090011000036.
DR GeneID; 5997834; -.
DR KEGG; aor:AO090011000036; -.
DR VEuPathDB; FungiDB:AO090011000036; -.
DR HOGENOM; CLU_012703_3_0_1; -.
DR OMA; WALIEAH; -.
DR Proteomes; UP000006564; Chromosome 7.
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 Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..245
FT /evidence="ECO:0000250"
FT /id="PRO_0000407195"
FT CHAIN 246..634
FT /note="Extracellular metalloproteinase NpI"
FT /id="PRO_0000407196"
FT REGION 289..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 356
FT /note="L -> S (in Ref. 1; AAF04628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 69170 MW; 6A2855D3CD25312C CRC64;
MRGLLLAGAL GLPLAVLAHP THHAHGLQRR TVDLNSFRLH QAAKYINATE SSSDVSSSFS
PFTEQSYVET ATQLVKNILP DATFRVVKDH YIGSNGVAHV NFRQTAHGLD IDNADFNVNV
GKNGKIFSYG HSFYTGKIPD ANPLTKRDYT DPVAALRGTN EALQLSITLD QVSTEATEDK
ESFNFKGVSG TVSDPKAQLV YLVKEDGSLA LTWKVETDID SNWLLTYIDA NTGKDVHGVV
DYVAEADYQV YAWGINDPTE GPRTVISDPW DSSASAFTWI SDGENNYTTT RGNNGIAQSN
PTGGSQYLKN YRPDSPDLKF QYPYSLNATP PESYIDASIT QLFYTANTYH DLLYTLGFNE
EAGNFQYDNN GKGGAGNDYV ILNAQDGSGT NNANFATPPD GQPGRMRMYI WTESQPYRDG
SFEAGIVIHE YTHGLSNRLT GGPANSRCLN ALESGGMGEG WGDFMATAIR LKAGDTHSTD
YTMGEWAANK KGGIRAYPFS TSLETNPLTY TSLNELDEVH AIGAVWANVL YELLWNLIDK
HGKNDGPKPE FKDGVPTDGK YLAMKLVIDG MALQPCNPNC VQARDAILDA DKALTDGANK
CEIWKAFAKR GLGEGAEYHA SRRVGSDKVP SDAC
