LAP2_TRIRU
ID LAP2_TRIRU Reviewed; 495 AA.
AC Q5QHG6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 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 that releases a wide variety of
CC amino acids from natural peptides and contributes to pathogenicity.
CC {ECO:0000269|PubMed:15632434}.
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 -!- 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. Expression levels are the same whether keratin is present
CC or not in the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; AY496929; AAS76669.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5QHG6; -.
DR SMR; Q5QHG6; -.
DR PRIDE; Q5QHG6; -.
DR VEuPathDB; FungiDB:TERG_08405; -.
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 1: Evidence at protein level;
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_0000384096"
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; 53309 MW; 291D29C958A9813F CRC64;
MKSQLLSLAV AVTTISQGVV GQEPFGWPFK PMVTQDDLQN KIKLKDIMAG VEKLQSFSDA
HPEKNRVFGG NGHKDTVEWI YNEIKATGYY DVKKQEQVHL WSHAEAALNA NGKDLKASAM
SYSPPASKIM AELVVAKNNG CNATDYPANT QGKIVLVERG VCSFGEKSAQ AGDAKAAGAI
VYNNVPGSLA GTLGGLDKRH VPTAGLSQED GKNLATLVAS GKIDVTMNVI SLFENRTTWN
VIAETKGGDH NNVIMLGAHS DSVDAGPGIN DNGSGSIGIM TVAKALTNFK LNNAVRFAWW
TAEEFGLLGS TFYVNSLDDR ELHKVKLYLN FDMIGSPNFA NQIYDGDGSA YNMTGPAGSA
EIEYLFEKFF DDQGIPHQPT AFTGRSDYSA FIKRNVPAGG LFTGAEVVKT PEQVKLFGGE
AGVAYDKNYH RKGDTVANIN KGAIFLNTRA IAYAIAEYAR SLKGFPTRPK TGKRDVNPQY
SKMPGGGCGH HTVFM
