AMPL2_SOLLC
ID AMPL2_SOLLC Reviewed; 569 AA.
AC Q42876;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Leucine aminopeptidase 2, chloroplastic;
DE EC=3.4.11.1;
DE AltName: Full=Leucyl aminopeptidase 2;
DE Short=LAP 2;
DE AltName: Full=Proline aminopeptidase 2;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase 2;
DE Flags: Precursor;
GN Name=LAPA2;
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. 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).
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.
CC -!- INDUCTION: By wounding.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; U20594; AAA80499.1; -; mRNA.
DR PIR; S57812; S57812.
DR AlphaFoldDB; Q42876; -.
DR SMR; Q42876; -.
DR STRING; 4081.Solyc12g010040.1.1; -.
DR MEROPS; M17.A03; -.
DR PaxDb; Q42876; -.
DR PRIDE; Q42876; -.
DR ProMEX; Q42876; -.
DR eggNOG; KOG2597; Eukaryota.
DR InParanoid; Q42876; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q42876; baseline.
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; ISS: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: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; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..569
FT /note="Leucine aminopeptidase 2, chloroplastic"
FT /id="PRO_0000026804"
FT ACT_SITE 351
FT /evidence="ECO:0000255"
FT ACT_SITE 428
FT /evidence="ECO:0000255"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 364
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 424
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
SQ SEQUENCE 569 AA; 59549 MW; E8DADAC26A3DC47B CRC64;
MNGVLCSSSS SFHSYPSIFT KFQSSPIWSF SISVTPLCSR RAKRMAHSIA RDTLGLTHTN
QSDAPKISFA AKEIDLVEWK GDILTVGATE KDLARDGNSK FQNPLLQKLD SKLSGLLSEA
SSEEDFSGKA GQSTILRLPG LGSKRIALVG LGSPTSSTAA YRCLGEAAAA AAKSAQASNI
AIALASTDGL SAELKLSSAS AITTGAVLGT FEDNRFKSES KKPTLKSLDI LGLGTGPEIE
KKIKYAADVC AGVILGRELV NAPANVLTPA VLAEEAKKIA STYSDVFSAN ILDVEQCKEL
KMGSYLRVAA ASANPAHFIH LCYKPSSGEI KKKIALVGKG LTFDSGGYNI KTGPGCSIEL
MKFDMGGAAA VLGAAKALGQ IKPAGVEVHF IVAACENMIS GTGMRPGDII TASNGKTIEV
NNTDAEGRLT LSVGISCNQG VEKIVDLATL TGACVVALGP SIAGIFTPSD DLAKEVVAAS
EVSGEKLWRL PMEDSYWDSM KSGVADMVNT GGRPGGAITA ALFLKQFVNE KVQWMHIDLA
GPVWSDKKKN ATGFGVSTLV EWVLKNSTN
