ID   LAP2_TRITO              Reviewed;         495 AA.
AC   A7UI10;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Leucine aminopeptidase 2;
DE            EC=3.4.11.-;
DE   AltName: Full=Leucyl aminopeptidase 2;
DE            Short=LAP2;
DE   Flags: Precursor;
GN   Name=LAP2;
OS   Trichophyton tonsurans (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Preuett B.L., Brown J.T., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular aminopeptidase that releases a wide variety of
CC       amino acids from natural peptides and contributes to pathogenicity.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P80561};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; EU072468; ABU49645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7UI10; -.
DR   SMR; A7UI10; -.
DR   PRIDE; A7UI10; -.
DR   VEuPathDB; FungiDB:TESG_06750; -.
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   CDD; cd03876; M28_SGAP_like; 1.
DR   InterPro; IPR029514; Ape3.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR041756; M28_SGAP-like.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; PTHR12147; 1.
DR   PANTHER; PTHR12147:SF17; PTHR12147:SF17; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Virulence; Zinc.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..495
FT                   /note="Leucine aminopeptidase 2"
FT                   /id="PRO_0000384097"
FT   DOMAIN          124..218
FT                   /note="PA"
FT   ACT_SITE        303
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   BINDING         430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   SITE            429
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
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        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   495 AA;  53211 MW;  FA6FAFE8BE9A834D CRC64;
     MKSQLLSLAV AVSTISQGVV GQEPFGWPFK PMVTQDDLQN KIKLKDIMAG IEKLQSFSDA
     HPEKNRVFGG NGHKDTVEWI YNELKATGYY NVKKQEQVHL WSHAEAALSA NGKDLKASAM
     SYSPPANKIM AELVVAKNNG CNATDYPENT QGKIVLIQRG VCSFGEKSSQ AGDAKAIGAV
     VYNNVPGSLA GTLGGLDKRH VPTAGLSQED GKNLASLVAS GKVDVTMNVV SLFENRTTWN
     VIAETKGGDH NNVVMLGAHS DSVDAGPGIN DNGSGSIGIM TVAKALTNFK LNNAVRFAWW
     TAEEFGLLGS TFYVDSLDDR ELHKVKLYLN FDMIGSPNFA NQIYDGDGSA YNMTGPAGSA
     EIEYLFEKFF DDQGLPHQPT AFTGRSDYSA FIKRNVPAGG LFTGAEVVKT PEQVKLFGGE
     AGVAYDKNYH GKGDTVANIN KGAIFLNTRA IAYSVAEYAR SLKGFPTRPK TGKRAVNPQY
     AKMPGGGCGH HTVFM