ID   LAP1_TRIHA              Reviewed;         398 AA.
AC   A4V8W0;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Leucine aminopeptidase 1;
DE            EC=3.4.11.-;
DE   AltName: Full=Leucyl aminopeptidase 1;
DE            Short=LAP1;
DE   AltName: Full=Peptidase p2920;
DE   Flags: Precursor;
GN   Name=lap1; Synonyms=p2920;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150;
RX   PubMed=17415567; DOI=10.1007/s00294-007-0130-5;
RA   Suarez M.B., Vizcaino J.A., Llobell A., Monte E.;
RT   "Characterization of genes encoding novel peptidases in the biocontrol
RT   fungus Trichoderma harzianum CECT 2413 using the TrichoEST functional
RT   genomics approach.";
RL   Curr. Genet. 51:331-342(2007).
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   -!- INDUCTION: Expressed in presence of glucose, chitin or fungal cell
CC       walls. However, lower levels of expression were found on chitin. Also
CC       expressed in carbon starvation conditions.
CC       {ECO:0000269|PubMed:17415567}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM294973; CAL25573.1; -; mRNA.
DR   AlphaFoldDB; A4V8W0; -.
DR   SMR; A4V8W0; -.
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   2: Evidence at transcript level;
KW   Aminopeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..87
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000412450"
FT   CHAIN           88..398
FT                   /note="Leucine aminopeptidase 1"
FT                   /id="PRO_0000412451"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        321..325
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  43932 MW;  006E18478CC7CE44 CRC64;
     MKFLQTSLIA AALPAALVSG RFVIENEGDN VQLDEPAKYL IELSPGETQW VTEEDKWDLR
     RNGQNFMDIT DTQELGTLRA WTQSQASVAF PDKCVKQKEV GELAGHLTKD GMRRNLEKLT
     SFHTRYYKSD YGRQSSEWVL ERINGIIKDA GAEDTVTAEH FGHSWPQSSV IARIPGKTNT
     TVIIGAHQDS INLWLPSILG APGADDDGSG TVTIMEVFHT LLKAKDVVGG SAPNTVEFHW
     YSAEEGGLLG SQAIFQSYEK EGRDVKAMLQ QDMTGFVQGT EDAGKPESVG VITDFVHPGL
     TAFIKKVIEE YCSIPWVETK CGYACSDHAS ASKAGYPSAF VIESAFENSD QHIHGTDDLI
     KYLSFDHMLE HAKMTLGLVY ELAYHDFSSK AVEEPSEL