ID   LAP1_TRITO              Reviewed;         373 AA.
AC   B6V870;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Probable leucine aminopeptidase 1;
DE            EC=3.4.11.-;
DE   AltName: Full=Leucyl aminopeptidase 1;
DE            Short=LAP1;
DE   Flags: Precursor;
GN   Name=LAP1;
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].
RX   PubMed=19609717; DOI=10.1007/s11046-009-9223-7;
RA   Abdel-Rahman S.M., Sugita T., Gonzalez G.M., Ellis D., Arabatzis M.,
RA   Vella-Zahra L., Viguie-Vallanet C., Hiruma M., Leeder J.S., Preuett B.;
RT   "Divergence among an international population of Trichophyton tonsurans
RT   isolates.";
RL   Mycopathologia 169:1-13(2010).
CC   -!- FUNCTION: Extracellular aminopeptidase which contributes to
CC       pathogenicity. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACJ06661.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FJ267693; ACJ06661.1; ALT_TERM; Genomic_DNA.
DR   AlphaFoldDB; B6V870; -.
DR   SMR; B6V870; -.
DR   VEuPathDB; FungiDB:TESG_07124; -.
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; Virulence; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..373
FT                   /note="Probable leucine aminopeptidase 1"
FT                   /id="PRO_0000397765"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        310..314
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  40677 MW;  8A066FA6C7F690B8 CRC64;
     MKLLSVLALS ATATSVLGAS IPVDTRAQKF LIELAPGETR WVTEEEKWEL KQKGQDFFDI
     TDEEVGFTAA VAQPAIAYPT SIRHADAVNA MIATLSKENM QRDLTKLSSF HNRYYKSDYG
     KQSATWLQQQ VQAVINSSGA SRYGAKVVSV RHNFVQHSIV ATIPGRSPEI VVVGAHQDSI
     NQRSPMTGRA PGADDNGSGS VTILEALRGV LQDQTIVQGK AANTIEFHWY AGEEAGLLGS
     QAIFANYKQT GKKVKGMLNQ DMTGYIKGMV DRGLKVSFGI ITDNVSTSLT SFIRMVITKY
     CSIPTIDTRC GYACSDHASA NRNGYPSAMV AESPINLLDP HLHTDSDLIS YLDFDHMIEH
     AKLVVGFVTE LAK