LAP1_PENRW
ID LAP1_PENRW Reviewed; 385 AA.
AC B6H3H1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
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; ORFNames=Pc13g06380;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC proteinaceous substrates. {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000305}.
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DR EMBL; AM920428; CAP91707.1; -; Genomic_DNA.
DR RefSeq; XP_002559072.1; XM_002559026.1.
DR AlphaFoldDB; B6H3H1; -.
DR SMR; B6H3H1; -.
DR STRING; 1108849.XP_002559072.1; -.
DR MEROPS; M28.022; -.
DR EnsemblFungi; CAP91707; CAP91707; PCH_Pc13g06380.
DR GeneID; 8305510; -.
DR KEGG; pcs:Pc13g06380; -.
DR VEuPathDB; FungiDB:PCH_Pc13g06380; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_025866_0_0_1; -.
DR OMA; QNFMDIT; -.
DR OrthoDB; 1257666at2759; -.
DR BioCyc; PCHR:PC13G06380-MON; -.
DR Proteomes; UP000000724; Contig Pc00c13.
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 3: Inferred from homology;
KW Aminopeptidase; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT PROPEP 15..85
FT /evidence="ECO:0000250"
FT /id="PRO_0000412437"
FT CHAIN 86..385
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_5000409004"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 319..323
FT /evidence="ECO:0000250"
SQ SEQUENCE 385 AA; 42899 MW; 5B3971156B2F98B0 CRC64;
MKFLTLALSA TATAMIIVNP EQQPLAPSIV QNPQHKSLIE LAPYRTRWVT EEEKWSLKLD
GVNFIDVTDE YQSGSYGTLH TTRVVHYPGA MEHAHEILPL TETLDKSNMR SNLEHFTSFY
TRYYKSQTGI ESATWLFDQV TAAVHESGAS DHGATVERFA HPWGQFSIIA RIPGQTDNTV
ILGSHQDSIN LFLPSILAAP GADDDGSGTV TILEALRALL RSETIAHGQA RNTIEFHWYS
AEEGGLLGSQ AVYANYKKNQ RNVKAMLQQD MTGYVQGTLD AGEKESVGVI IDYVDQGLTA
FIKEVITTYC DVPYVETKCG YACSDHASAS RYGYPSAFVI ESQFENSDKR IHTTEDKIEY
LSFDHMLQHA KMSLAFAYEL AFAPF
