ID   AMPL_SOLTU              Reviewed;         573 AA.
AC   P31427;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 128.
DE   RecName: Full=Leucine aminopeptidase, chloroplastic;
DE            EC=3.4.11.1;
DE   AltName: Full=Leucyl aminopeptidase;
DE            Short=LAP;
DE   AltName: Full=Proline aminopeptidase;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE   Flags: Precursor;
GN   Name=LAP;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree;
RX   PubMed=7765119; DOI=10.1007/bf00196392;
RA   Herbers K., Prat S., Willmitzer L.;
RT   "Functional analysis of a leucine aminopeptidase from Solanum tuberosum
RT   L.";
RL   Planta 194:230-240(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 19-573.
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=1392612; DOI=10.1105/tpc.4.9.1157;
RA   Hildmann T., Ebneth M., Pena-Cortes H., Sanchez-Serrano J.J.,
RA   Willmitzer L., Prat S.;
RT   "General roles of abscisic and jasmonic acids in gene activation as a
RT   result of mechanical wounding.";
RL   Plant Cell 4:1157-1170(1992).
CC   -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC       intracellular proteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC         is preferably Leu, but may be other amino acids including Pro
CC         although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC         methyl esters are also readily hydrolyzed, but rates on arylamides
CC         are exceedingly low.; EC=3.4.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P30184};
CC       Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:P30184};
CC   -!- SUBUNIT: Homohexamer (dimer of homotrimers).
CC       {ECO:0000250|UniProtKB:Q10712}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: In tubers and floral buds of untreated plants.
CC       After abscisic acid (ABA) treatment or mechanical wounding is mostly
CC       accumulated in leaves, to a lesser extent in stems, but not in roots.
CC   -!- INDUCTION: By abscisic acid (ABA), jasmonic acid (JA) and wounding.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR   EMBL; X77015; CAA54314.1; -; mRNA.
DR   EMBL; X67845; CAA48038.1; -; mRNA.
DR   PIR; S41376; S41376.
DR   RefSeq; NP_001305566.1; NM_001318637.1.
DR   AlphaFoldDB; P31427; -.
DR   SMR; P31427; -.
DR   STRING; 4113.P31427; -.
DR   MEROPS; M17.002; -.
DR   PaxDb; 4113-P31427; -.
DR   GeneID; 102595887; -.
DR   KEGG; sot:102595887; -.
DR   InParanoid; P31427; -.
DR   OrthoDB; 412814at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0009611; P:response to wounding; IEA:UniProtKB-ARBA.
DR   CDD; cd00433; Peptidase_M17; 1.
DR   FunFam; 3.40.220.10:FF:000011; Leucine aminopeptidase 2, chloroplastic; 1.
DR   FunFam; 3.40.630.10:FF:000033; M17 leucyl aminopeptidase; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   NCBIfam; NF002076; PRK00913.2-3; 1.
DR   PANTHER; PTHR11963:SF43; LEUCINE AMINOPEPTIDASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   2: Evidence at transcript level;
KW   Aminopeptidase; Chloroplast; Hydrolase; Manganese; Metal-binding; Plastid;
KW   Protease; Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..53
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           54..573
FT                   /note="Leucine aminopeptidase, chloroplastic"
FT                   /id="PRO_0000026805"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255"
FT   BINDING         342
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P30184"
FT   BINDING         347
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P30184"
FT   BINDING         347
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P30184"
FT   BINDING         367
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P30184"
FT   BINDING         427
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P30184"
FT   BINDING         429
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P30184"
FT   BINDING         429
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P30184"
SQ   SEQUENCE   573 AA;  60122 MW;  3152145A4A7FB291 CRC64;
     MATLRVSSLL ASSPSSLHCN PSVFTKCQSS PRWAFSFSVT PLCSRRSKRI VHCIAGDTLG
     LTRPNESDAP KISIGAKDTD VVQWQGDLLA IGATENDLAR DDNSKFKNPL LQRLDSKLNG
     LLSAASSEED FSGKSGQSIN LRLPGGRITL VGLGSSASSP TSYHSLGEAA AAAAKSAQAR
     NIAVSLASTD GLSAESKINS ASAIATGVML GIFEDNRFRS ESKTPALESL DILGLGTGPE
     IESKIKYAEH VCAGVILGRE LVNAPANIVT PGALAEEAKK IASTYSDVIT VNILDAEQCK
     ELKMGAYLGV AAAATENPPY FIHLCFKTNS RERKTKIALV GKGLTFDSGG YNLKTGAGSK
     IELMKNDMGG AAAVLGAAKA LGEIKPRGVE VHFIVAACEN MISGAGMRPG DIVTASNGKT
     IEVNNTDAEG RLTLADALIY ACNQGVEKII DLATLTGAIV TALGPSVAGA FTPSDGLARE
     VVVAAEASGE KLWRMPMEES YWESMKSGVA DMINTGPRDG GAITGALFLK QFVDEKVQWL
     HLDIAGPVWS DEKKNATGYG VSTLVEWVLR NSL
//