LAP2_ARTOC
ID LAP2_ARTOC Reviewed; 495 AA.
AC C5FTZ6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, 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; ORFNames=MCYG_06199;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995706; EEQ33380.1; -; Genomic_DNA.
DR RefSeq; XP_002844235.1; XM_002844189.1.
DR AlphaFoldDB; C5FTZ6; -.
DR SMR; C5FTZ6; -.
DR STRING; 63405.XP_002844235.1; -.
DR EnsemblFungi; EEQ33380; EEQ33380; MCYG_06199.
DR GeneID; 9222474; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_0_2_1; -.
DR OMA; ENRTTWN; -.
DR OrthoDB; 792624at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
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; Reference proteome; Secreted; Signal; Virulence; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..495
FT /note="Leucine aminopeptidase 2"
FT /id="PRO_0000384094"
FT DOMAIN 124..218
FT /note="PA"
FT REGION 464..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 52856 MW; 42F2DA39ECE5D9C9 CRC64;
MKTQLLSLGV ALTAISQGVI AEDALNWPFK PLVNADDLQN KIKLKDLMAG VQKLQDFAYA
HPEKNRVFGG AGHKDTVDWI YNELKATGYY DVKMQPQVHL WSHAEAAVNA NGKDLTASAM
SYSPPADKIT AELVLAKNMG CNATDYPEGT KGKIVLIERG VCSFGEKSAQ AGDAKAIGAI
VYNNVPGSLA GTLGGLDNRH APTAGISQAD GKNLASLVAS GKVTVTMNVI SKFENRTTWN
VIAETKGGDH NNVIMLGSHS DSVDAGPGIN DNGSGTIGIM TVAKALTNFK VNNAVRFGWW
TAEEFGLLGS TFYVDSLDDR ELHKVKLYLN FDMIGSPNFA NQIYDGDGSA YNMTGPAGSA
EIEYLFEKFF DDQGIPHQPT AFTGRSDYSA FIKRNVPAGG LFTGAEVVKT AEQAKLFGGE
AGVAYDKNYH GKGDTVDNIN KGAIYLNTRG IAYATAQYAS SLRGFPTRPK TGKRDVSPRG
QSMPGGGCGH HSVFM
