LAP2_ARTBC
ID LAP2_ARTBC Reviewed; 495 AA.
AC D4AWC9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Probable leucine aminopeptidase 2;
DE EC=3.4.11.-;
DE AltName: Full=Leucyl aminopeptidase 2;
DE Short=LAP2;
DE Flags: Precursor;
GN Name=LAP2; ORFNames=ARB_00494;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: Extracellular aminopeptidase that releases a wide variety of
CC amino acids from natural peptides and contributes to pathogenicity.
CC {ECO:0000250}.
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:0000269|PubMed:21247460}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; ABSU01000014; EFE32669.1; -; Genomic_DNA.
DR RefSeq; XP_003013309.1; XM_003013263.1.
DR AlphaFoldDB; D4AWC9; -.
DR SMR; D4AWC9; -.
DR STRING; 663331.D4AWC9; -.
DR EnsemblFungi; EFE32669; EFE32669; ARB_00494.
DR GeneID; 9519263; -.
DR KEGG; abe:ARB_00494; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_0_2_1; -.
DR OMA; ENRTTWN; -.
DR Proteomes; UP000008866; 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 1: Evidence at protein level;
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="Probable leucine aminopeptidase 2"
FT /id="PRO_0000397767"
FT DOMAIN 130..216
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, 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, 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; 53243 MW; 00C1363FF0787B33 CRC64;
MKSQLLSLAV AVTTISQGVV GQEPFGWPFK PMVTQDDLQN KIKLKDIMAG VEKLQSFSDA
HPEKNRVFGG NGHKDTVEWI YNEIKATGYY DVKKQEQVHL WSHAEAAVSA NGKELKASAM
SYSPPASKIM AELVVAKNNG CNATDYPENT QGKIVLVERG VCSFGEKSSQ AGDAKAAGAI
VYNNVPGSLA GTLGGLDKRH VPTAGLSQED GKNLATLIAS GKVDVTMNVI SLFENRTTWN
VIAETKGGDH NNVVMLGAHS DSVDAGPGIN DNGSGSIGIM TVAKALTNFK LNNAVRFAWW
TAEEFGLLGS TFYVNSLDDR ELHKVKLYLN FDMIGSPNFA NQIYDGDGSA YNMTGPAGSA
EIEYLFEKFF DDQGIPHQPT AFTGRSDYSA FIKRNVPAGG LFTGAEVVKT PEQVKLFGGE
AGVAYDKNYH GKGDTVANIN KGAIFLNTRA IAYAIAEYAR SLKGFPTRPK TGKRDVNPQY
SKMPGGGCGH HTVFM
