AMPL_SOLTU
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 03-AUG-2022, entry version 116.
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=10.2307/3869484;
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 MEROPS; M17.002; -.
DR PRIDE; P31427; -.
DR GeneID; 102595887; -.
DR KEGG; sot:102595887; -.
DR InParanoid; P31427; -.
DR OrthoDB; 562530at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P31427; baseline.
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:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 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 PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 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
