AMPL1_SOLLC
ID AMPL1_SOLLC Reviewed; 571 AA.
AC Q10712; A0A3Q7JSH2; Q9S9A3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Leucine aminopeptidase 1, chloroplastic;
DE EC=3.4.11.1;
DE AltName: Full=DR57;
DE AltName: Full=Leucyl aminopeptidase 1;
DE Short=LAP 1;
DE AltName: Full=Proline aminopeptidase 1;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase 1;
DE Flags: Precursor;
GN Name=LAPA1; Synonyms=LAP, LAP2;
GN OrderedLocusNames=Solyc12g010020 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Peto 238R; TISSUE=Leaf;
RX PubMed=8824220; DOI=10.1074/jbc.271.42.25880;
RA Gu Y.Q., Chao W.S., Walling L.L.;
RT "Localization and post-translational processing of the wound-induced
RT leucine aminopeptidase proteins of tomato.";
RL J. Biol. Chem. 271:25880-25887(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-571.
RC STRAIN=cv. VF36; TISSUE=Pistil;
RX PubMed=7647301; DOI=10.1007/bf00021194;
RA Milligan S.B., Gasser C.S.;
RT "Nature and regulation of pistil-expressed genes in tomato.";
RL Plant Mol. Biol. 28:691-711(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-571, AND INDUCTION.
RC STRAIN=cv. Peto 238R; TISSUE=Leaf;
RX PubMed=8234334; DOI=10.1073/pnas.90.21.9906;
RA Pautot V., Holzer F.M., Reisch B., Walling L.L.;
RT "Leucine aminopeptidase: an inducible component of the defense response in
RT Lycopersicon esculentum (tomato).";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9906-9910(1993).
RN [5]
RP INDUCTION.
RX PubMed=15231736; DOI=10.1101/gad.297704;
RA Boter M., Ruiz-Rivero O., Abdeen A., Prat S.;
RT "Conserved MYC transcription factors play a key role in jasmonate signaling
RT both in tomato and Arabidopsis.";
RL Genes Dev. 18:1577-1591(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 54-571 IN COMPLEX WITH MAGNESIUM
RP IONS, AND SUBUNIT.
RX PubMed=24914976; DOI=10.1107/s1399004714006245;
RA Duprez K., Scranton M.A., Walling L.L., Fan L.;
RT "Structure of tomato wound-induced leucine aminopeptidase sheds light on
RT substrate specificity.";
RL Acta Crystallogr. D 70:1649-1658(2014).
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24914976};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:24914976};
CC -!- SUBUNIT: Homohexamer (dimer of homotrimers).
CC {ECO:0000269|PubMed:24914976}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: Induced by wounding (PubMed:8234334, PubMed:15231736).
CC Induced by methyl jasmonate (PubMed:15231736).
CC {ECO:0000269|PubMed:15231736, ECO:0000269|PubMed:8234334}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; U50151; AAC49456.1; -; mRNA.
DR EMBL; U50152; AAC49457.1; -; mRNA.
DR EMBL; CM001075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U20593; AAA80498.1; -; mRNA.
DR PIR; S57811; S57811.
DR PIR; T07849; T07849.
DR PIR; T07850; T07850.
DR RefSeq; NP_001233862.2; NM_001246933.2.
DR PDB; 4KSI; X-ray; 2.20 A; A=54-571.
DR PDB; 5D8N; X-ray; 2.15 A; A/B/C=54-571.
DR PDBsum; 4KSI; -.
DR PDBsum; 5D8N; -.
DR AlphaFoldDB; Q10712; -.
DR SMR; Q10712; -.
DR STRING; 4081.Solyc12g010020.1.1; -.
DR MEROPS; M17.002; -.
DR PaxDb; Q10712; -.
DR PRIDE; Q10712; -.
DR GeneID; 544017; -.
DR KEGG; sly:544017; -.
DR eggNOG; KOG2597; Eukaryota.
DR InParanoid; Q10712; -.
DR OrthoDB; 562530at2759; -.
DR BRENDA; 3.4.11.1; 3101.
DR SABIO-RK; Q10712; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q10712; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0034214; P:protein hexamerization; IPI:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Chloroplast; Hydrolase; Magnesium;
KW Metal-binding; Plastid; Protease; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..571
FT /note="Leucine aminopeptidase 1, chloroplastic"
FT /id="PRO_0000026803"
FT ACT_SITE 354
FT /evidence="ECO:0000255"
FT ACT_SITE 431
FT /evidence="ECO:0000255"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24914976,
FT ECO:0007744|PDB:4KSI"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24914976,
FT ECO:0007744|PDB:4KSI"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24914976,
FT ECO:0007744|PDB:4KSI"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24914976,
FT ECO:0007744|PDB:4KSI"
FT BINDING 427
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24914976,
FT ECO:0007744|PDB:4KSI"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24914976,
FT ECO:0007744|PDB:4KSI"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24914976,
FT ECO:0007744|PDB:4KSI"
FT CONFLICT 271
FT /note="P -> N (in Ref. 3; AAA80498)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="T -> S (in Ref. 3; AAA80498)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="G -> R (in Ref. 1; AAC49456)"
FT CONFLICT 509..510
FT /note="SG -> VA (in Ref. 1; AAC49456/AAC49457 and 3;
FT AAA80498)"
FT CONFLICT 515
FT /note="T -> L (in Ref. 1; AAC49457)"
FT /evidence="ECO:0000305"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:5D8N"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 146..156
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 194..212
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 239..263
FT /evidence="ECO:0007829|PDB:5D8N"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:5D8N"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 335..347
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:4KSI"
FT HELIX 369..384
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 387..400
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 430..443
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 475..488
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 499..505
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 508..514
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 521..530
FT /evidence="ECO:0007829|PDB:5D8N"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:5D8N"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:5D8N"
FT TURN 551..554
FT /evidence="ECO:0007829|PDB:5D8N"
FT HELIX 561..569
FT /evidence="ECO:0007829|PDB:5D8N"
SQ SEQUENCE 571 AA; 60154 MW; 5D21AB4C5F2B9E63 CRC64;
MATLRVSSLF ASSSSSLHSN PSVFTKYQSS PKWAFSFPVT PLCSKRSKRI VHCIAGDTLG
LTRPNESDAP KISIGAKDTA VVQWQGDLLA IGATENDMAR DENSKFKNPL LQQLDSELNG
LLSAASSEED FSGKSGQSVN LRFPGGRITL VGLGSSASSP TSYHSLGQAA AAAAKSSQAR
NIAVALASTD GLSAESKINS ASAIATGVVL GSFEDNRFRS ESKKSTLESL DILGLGTGPE
IERKIKYAEH VCAGVILGRE LVNAPANIVT PAVLAEEAKK IASTYSDVIS VNILDAEQCK
ELKMGAYLAV AAAATENPPY FIHLCFKTPT KERKTKLALV GKGLTFDSGG YNLKVGAGSR
IELMKNDMGG AAAVLGAAKA LGEIRPSRVE VHFIVAACEN MISAEGMRPG DIVTASNGKT
IEVNNTDAEG RLTLADALIY ACNQGVEKII DLATLTGAIM VALGPSVAGA FTPNDDLARE
VVEAAEASGE KLWRMPMEES YWESMKSGSG DMINTGPGNG GAITGALFLK QFVDEKVQWL
HLDVAGPVWS DEKKNATGYG VSTLVEWVLR N
