LAP2_ASPOR
ID LAP2_ASPOR Reviewed; 496 AA.
AC Q2ULM2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=probable leucine aminopeptidase 2;
DE EC=3.4.11.-;
DE AltName: Full=Aminopeptidase II;
DE AltName: Full=Leucyl aminopeptidase 2;
DE Short=LAP2;
DE Flags: Precursor;
GN Name=lap2; ORFNames=AO090003000354;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP PROTEIN SEQUENCE OF 17-46; 108-142 AND 176-195, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, COFACTOR, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10899618; DOI=10.1016/s0167-4838(00)00064-9;
RA Blinkovsky A.M., Byun T., Brown K.M., Golightly E.J., Klotz A.V.;
RT "A non-specific aminopeptidase from Aspergillus.";
RL Biochim. Biophys. Acta 1480:171-181(2000).
CC -!- FUNCTION: Extracellular aminopeptidase that releases a wide variety of
CC amino acids from natural peptides. {ECO:0000269|PubMed:10899618}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10899618};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10899618};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 mM for Leu-paranitroanilide {ECO:0000269|PubMed:10899618};
CC KM=9 mM for Lys-paranitroanilide {ECO:0000269|PubMed:10899618};
CC KM=3.5 mM for Ala-paranitroanilide {ECO:0000269|PubMed:10899618};
CC KM=1.5 mM for Glu-paranitroanilide {ECO:0000269|PubMed:10899618};
CC KM=13 mM for Val-paranitroanilide {ECO:0000269|PubMed:10899618};
CC KM=15 mM for Pro-paranitroanilide {ECO:0000269|PubMed:10899618};
CC KM=51 mM for Ile-paranitroanilide {ECO:0000269|PubMed:10899618};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:10899618};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. Retains 65 and 46 percent
CC residual activity after a 20 min incubation at 70 and 75 degrees
CC Celsius, respectively. {ECO:0000269|PubMed:10899618};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10899618}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; AP007155; BAE57543.1; -; Genomic_DNA.
DR RefSeq; XP_001819545.1; XM_001819493.2.
DR AlphaFoldDB; Q2ULM2; -.
DR SMR; Q2ULM2; -.
DR STRING; 510516.Q2ULM2; -.
DR EnsemblFungi; BAE57543; BAE57543; AO090003000354.
DR GeneID; 5991528; -.
DR KEGG; aor:AO090003000354; -.
DR VEuPathDB; FungiDB:AO090003000354; -.
DR HOGENOM; CLU_024336_0_1_1; -.
DR OMA; ENRTTWN; -.
DR SABIO-RK; Q2ULM2; -.
DR Proteomes; UP000006564; Chromosome 2.
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; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:10899618"
FT CHAIN 17..496
FT /note="probable leucine aminopeptidase 2"
FT /id="PRO_0000397769"
FT DOMAIN 111..205
FT /note="PA"
FT REGION 475..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 248
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 260
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 260
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 293
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 321
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 419
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 418
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 53557 MW; 266767E9527E399E CRC64;
MRSLLWASLL SGVLAGRALV SPDEFPEDIQ LEDLLEGSQQ LEDFAYAYPE RNRVFGGKAH
DDTVNYLYEE LKKTGYYDVY KQPQVHLWSN ADQTLKVGDE EIEAKTMTYS PSVEVTADVA
VVKNLGCSEA DYPSDVEGKV ALIKRGECPF GDKSVLAAKA KAAASIVYNN VAGSMAGTLG
AAQSDKGPYS AIVGISLEDG QKLIKLAEAG SVSVDLWVDS KQENRTTYNV VAQTKGGDPN
NVVALGGHTD SVEAGPGIND DGSGIISNLV IAKALTQYSV KNAVRFLFWT AEEFGLLGSN
YYVSHLNATE LNKIRLYLNF DMIASPNYAL MIYDGDGSAF NQSGPAGSAQ IEKLFEDYYD
SIDLPHIPTQ FDGRSDYEAF ILNGIPSGGL FTGAEGIMSE ENASRWGGQA GVAYDANYHA
AGDNMTNLNH EAFLINSKAT AFAVATYAND LSSIPKRNTT SSLHRRARTM RPFGKRAPKT
HAHVSGSGCW HSQVEA
