LAP1_ASPSO
ID LAP1_ASPSO Reviewed; 377 AA.
AC Q8J2N2;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 46.
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;
OS Aspergillus sojae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41058;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 78-90; 101-117;
RP 128-131; 133-139 AND 288-307, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND GLYCOSYLATION.
RC STRAIN=ATCC 42249;
RX PubMed=12031491; DOI=10.1016/s0167-4781(02)00307-x;
RA Chien H.C., Lin L.L., Chao S.H., Chen C.C., Wang W.C., Shaw C.Y.,
RA Tsai Y.C., Hu H.Y., Hsu W.H.;
RT "Purification, characterization, and genetic analysis of a leucine
RT aminopeptidase from Aspergillus sojae.";
RL Biochim. Biophys. Acta 1576:119-126(2002).
CC -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC proteinaceous substrates. {ECO:0000269|PubMed:12031491}.
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 -!- ACTIVITY REGULATION: Activity is strongly inhibited by metalchelating
CC agents, such as EDTA and dipicolinic acid.
CC {ECO:0000269|PubMed:12031491}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.1-10. {ECO:0000269|PubMed:12031491};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:12031491};
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; AF419160; AAN31395.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8J2N2; -.
DR SMR; Q8J2N2; -.
DR MEROPS; M28.022; -.
DR BRENDA; 3.4.11.1; 529.
DR BRENDA; 3.4.11.22; 529.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..77
FT /evidence="ECO:0000269|PubMed:12031491"
FT /id="PRO_0000412397"
FT CHAIN 78..377
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_0000412398"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..314
FT /evidence="ECO:0000250"
SQ SEQUENCE 377 AA; 41179 MW; 9592ECC70292C28C CRC64;
MRFLPCIATL AATASALAIG DHIRSDDQYV LELGPGETKV VTEAEKWALR AEGKRFFDIT
GRTSSLELAS NKKQKLAVTY PDSVQHNETV QNLINSLDKK NFETVLQPFS EFHNRYYKSD
NGKKSSEWLQ GKIQEIISAS GAKGVTVEPF KHFFPQSSLI AKIPGKSDKT IVLGAHQDSI
NLNSPSEGRA PSADDDGSGV VTILEAFRVL LTDEKVAAGE APNTVEFHFY AGEEGGLLGS
QDIFEQYLQK SRDVKAMLQQ DMTGYTKGTT DAGKPESIGI ITDNVDENLT KFLKIIVDAY
CTIPTVDSKC GYGCSDHASA TKYGYPAAFA FESAFGDDSP YIHSADDTIE TVNFDHVLQH
GRLTLGFAYE LAFADSL
