ID LAP2_TRIEQ Reviewed; 495 AA.
AC A7UI09;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, 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 equinum (Horse ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63418;
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 -!- 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; EU072467; ABU49644.1; -; Genomic_DNA.
DR AlphaFoldDB; A7UI09; -.
DR SMR; A7UI09; -.
DR GlyCosmos; A7UI09; 4 sites, No reported glycans.
DR VEuPathDB; FungiDB:TEQG_05395; -.
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 CDD; cd02130; PA_ScAPY_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 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_0000384095"
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; 53197 MW; EE0C8BCE5A34101C CRC64;
MKSQLLSLAV AVSTISQGVV GQEPFGWPFK PMVTQDDLQN KIKLKDIMAG VEKLQSFSDA
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
//
