LAP1_TRIRU
ID LAP1_TRIRU Reviewed; 373 AA.
AC Q5QHG5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, 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 Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [2]
RP INDUCTION.
RX PubMed=19098130; DOI=10.1128/ec.00208-08;
RA Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J.,
RA Bueno M., Giddey K., Staib P.;
RT "Gene expression profiling in the human pathogenic dermatophyte
RT Trichophyton rubrum during growth on proteins.";
RL Eukaryot. Cell 8:241-250(2009).
CC -!- FUNCTION: Extracellular aminopeptidase which contributes to
CC pathogenicity. {ECO:0000250, ECO:0000269|PubMed:15632434}.
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 -!- ACTIVITY REGULATION: Activity is inhibited by EDTA, o-phenanthroline,
CC bestatin and amastatin. {ECO:0000269|PubMed:15632434}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:15632434};
CC Temperature dependence:
CC Optimum temperatures are ranging from 40 to 50 degrees Celsius.
CC {ECO:0000269|PubMed:15632434};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15632434}.
CC -!- INDUCTION: Expression is strongly increased during growth on protein-
CC rich medium. Expressed at even higher levels when keratin is present in
CC the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000305}.
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DR EMBL; AY496930; AAS76670.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5QHG5; -.
DR SMR; Q5QHG5; -.
DR MEROPS; M28.022; -.
DR PRIDE; Q5QHG5; -.
DR VEuPathDB; FungiDB:TERG_05652; -.
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 1: Evidence at protein level;
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="Leucine aminopeptidase 1"
FT /id="PRO_0000384100"
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 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..314
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 40635 MW; 7754DE880535DF81 CRC64;
MKLLSVLALS ATATSVLGAS IPVDARAEKF LIELAPGETR WVTEEEKWEL KRKGQDFFDI
TDEEVGFTAA VAQPAIAYPT SIRHANAVNA MIATLSKENM QRDLTKLSSF QTAYYKVDFG
KQSATWLQEQ VQAAINTAGA NRYGAKVASF RHNFAQHSII ATIPGRSPEV VVVGAHQDSI
NQRSPMTGRA PGADDNGSGS VTILEALRGV LRDQTILQGK AANTIEFHWY AGEEAGLLGS
QAIFANYKQT GKKVKGMLNQ DMTGYIKGMV DKGLKVSFGI ITDNVNANLT KFVRMVITKY
CSIPTIDTRC GYACSDHASA NRNGYPSAMV AESPIDLLDP HLHTDSDNIS YLDFDHMIEH
AKLIVGFVTE LAK
