LAP1_ASPFM
ID LAP1_ASPFM Reviewed; 388 AA.
AC Q5VJG6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Leucine aminopeptidase 1;
DE EC=3.4.11.-;
DE AltName: Full=Leucyl aminopeptidase 1;
DE Short=LAP1;
DE Flags: Precursor;
GN Name=lap1;
OS Neosartorya fumigata (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=746128;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15632434; DOI=10.1099/mic.0.27484-0;
RA Monod M., Lechenne B., Jousson O., Grand D., Zaugg C., Stoecklin R.,
RA Grouzmann E.;
RT "Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte
RT Trichophyton rubrum.";
RL Microbiology 151:145-155(2005).
CC -!- FUNCTION: Extracellular aminopeptidase 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 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000305}.
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DR EMBL; AY436356; AAR96058.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5VJG6; -.
DR SMR; Q5VJG6; -.
DR MEROPS; M28.022; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..88
FT /evidence="ECO:0000250"
FT /id="PRO_0000412423"
FT CHAIN 89..388
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_0000412424"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 322..326
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 43128 MW; CDFB7AD884C6852D CRC64;
MKVLTAIALS AIAFTGAVAA VITQEAFLNN PRIHHDQEKY LIELAPYRTR WVTEEEKWAL
KLDGVNFIDI TEEHNTGFYP TLHSASYVKY PPKMQYAEEV AALNKNLSKE NMKANLERFT
SFHTRYYKSQ TGIRSATWLF DQVQRVVSES GAAEYGATVE RFSHPWGQFS IIARIPGRTN
KTVVLGAHQD SINLFLPSIL AAPGADDDGS GTVTILEALR GLLQSDAIAK GNASNTVEFH
WYSAEEGGML GSQAIFSNYK RNRREIKAML QQDMTGYVQG ALNAGVEEAI GIMVDYVDQG
LTQFLKDVVT AYCSVGYLET KCGYACSDHT SASKYGYPAA MATEAEMENT NKKIHTTDDK
IKYLSFDHML EHAKLSLGFA FELAFAPF
