AMPL1_ARATH
ID AMPL1_ARATH Reviewed; 520 AA.
AC P30184;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Leucine aminopeptidase 1;
DE EC=3.4.11.1 {ECO:0000269|PubMed:1555602};
DE AltName: Full=Leucyl aminopeptidase 1;
DE Short=AtLAP1 {ECO:0000303|PubMed:22493451};
DE AltName: Full=Proline aminopeptidase 1;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase 1;
GN Name=LAP1 {ECO:0000303|PubMed:22493451};
GN Synonyms=PM25 {ECO:0000303|PubMed:1555602}; OrderedLocusNames=At2g24200;
GN ORFNames=F27D4.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=1555602; DOI=10.1111/j.1432-1033.1992.tb16796.x;
RA Bartling D., Weiler E.W.;
RT "Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a
RT phylogenetically conserved enzyme of protein turnover in higher plants.";
RL Eur. J. Biochem. 205:425-431(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION.
RX PubMed=22493451; DOI=10.1074/jbc.m111.309500;
RA Scranton M.A., Yee A., Park S.Y., Walling L.L.;
RT "Plant leucine aminopeptidases moonlight as molecular chaperones to
RT alleviate stress-induced damage.";
RL J. Biol. Chem. 287:18408-18417(2012).
RN [8]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25716890; DOI=10.1042/bj20141154;
RA Kumar S., Kaur A., Chattopadhyay B., Bachhawat A.K.;
RT "Defining the cytosolic pathway of glutathione degradation in Arabidopsis
RT thaliana: role of the ChaC/GCG family of gamma-glutamyl cyclotransferases
RT as glutathione-degrading enzymes and AtLAP1 as the Cys-Gly peptidase.";
RL Biochem. J. 468:73-85(2015).
CC -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC intracellular proteins. Catalyzes the removal of unsubstituted N-
CC terminal amino acids from various peptides (Probable). Possesses
CC leucine aminopeptidase activity against the model substrate leucine-
CC amido methyl coumarin (PubMed:22493451). Possesses Cys-Gly dipeptidase
CC activity. In addition, can cleave Cys-Leu and Leu-Cys dipeptides
CC (PubMed:25716890). {ECO:0000269|PubMed:22493451,
CC ECO:0000269|PubMed:25716890, ECO:0000305|PubMed:1555602}.
CC -!- FUNCTION: Functions as molecular chaperone to protect proteins from
CC heat-induced damage. {ECO:0000269|PubMed:22493451}.
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 Evidence={ECO:0000269|PubMed:1555602};
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:0000269|PubMed:1555602, ECO:0000269|PubMed:25716890};
CC Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000305|PubMed:1555602};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for L-leucine-p-nitroanilide {ECO:0000269|PubMed:1555602};
CC KM=1.3 mM for Cys-Gly dipeptide {ECO:0000269|PubMed:25716890};
CC KM=1.1 mM for Cys-Leu dipeptide {ECO:0000269|PubMed:25716890};
CC KM=2.4 mM for Leu-Cys dipeptide {ECO:0000269|PubMed:25716890};
CC pH dependence:
CC Optimum pH is 8.5 for leucine aminopeptidase activity.
CC {ECO:0000269|PubMed:1555602};
CC -!- SUBUNIT: Homohexamer (dimer of homotrimers).
CC {ECO:0000250|UniProtKB:Q10712}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P30184-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; X63444; CAA45040.1; -; mRNA.
DR EMBL; AC005967; AAD03381.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07539.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07540.1; -; Genomic_DNA.
DR EMBL; AY062105; AAL32980.1; -; mRNA.
DR EMBL; BT006345; AAP21153.1; -; mRNA.
DR PIR; S22399; S22399.
DR RefSeq; NP_001118375.1; NM_001124903.1. [P30184-1]
DR RefSeq; NP_179997.1; NM_127981.4. [P30184-1]
DR AlphaFoldDB; P30184; -.
DR SMR; P30184; -.
DR BioGRID; 2306; 7.
DR STRING; 3702.AT2G24200.1; -.
DR MEROPS; M17.A03; -.
DR iPTMnet; P30184; -.
DR MetOSite; P30184; -.
DR PaxDb; P30184; -.
DR PRIDE; P30184; -.
DR ProteomicsDB; 244873; -. [P30184-1]
DR EnsemblPlants; AT2G24200.1; AT2G24200.1; AT2G24200. [P30184-1]
DR EnsemblPlants; AT2G24200.2; AT2G24200.2; AT2G24200. [P30184-1]
DR GeneID; 816954; -.
DR Gramene; AT2G24200.1; AT2G24200.1; AT2G24200. [P30184-1]
DR Gramene; AT2G24200.2; AT2G24200.2; AT2G24200. [P30184-1]
DR KEGG; ath:AT2G24200; -.
DR Araport; AT2G24200; -.
DR TAIR; locus:2047500; AT2G24200.
DR eggNOG; KOG2597; Eukaryota.
DR InParanoid; P30184; -.
DR OMA; SMDWIED; -.
DR PhylomeDB; P30184; -.
DR SABIO-RK; P30184; -.
DR PRO; PR:P30184; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P30184; baseline and differential.
DR Genevisible; P30184; AT.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR GO; GO:0016805; F:dipeptidase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Aminopeptidase; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Protease; Reference proteome.
FT CHAIN 1..520
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_0000165823"
FT ACT_SITE 300
FT /evidence="ECO:0000255"
FT ACT_SITE 377
FT /evidence="ECO:0000255"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:1555602"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:1555602"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:1555602"
FT BINDING 313
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:1555602"
FT BINDING 373
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:1555602"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:1555602"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:1555602"
SQ SEQUENCE 520 AA; 54509 MW; D3FA9CCCD312AA92 CRC64;
MAHTLGLTQP NSTEPHKISF TAKEIDVIEW KGDILVVGVT EKDLAKDGNS KFENPILSKV
DAHLSGLLAQ VSSEEDFTGK PGQSTVLRLP GLGSKRIALI GLGQSVSSPV AFHSLGEAVA
TVSKASQSTS AAIVLASSVS DESKLSSVSA LASGIVLGLF EDGRYKSESK KPSLKAVDII
GFGTGAEVEK KLKYAEDVSY GVIFGRELIN SPANVLTPAV LAEEAAKVAS TYSDVFTANI
LNEEQCKELK MGSYLAVAAA SANPPHFIHL VYKPPNGSVK TKLALVGKGL TFDSGGYNIK
TGPGCSIELM KFDMGGSAAV LGAAKAIGEI KPPGVEVHFI VAACENMISG TGMRPGDVIT
ASNGKTIEVN NTDAEGRLTL ADALVYACNQ GVDKIVDLAT LTGACVIALG TSMAGIYTPS
DELAKEVIAA SERSGEKLWR MPLEESYWEM MKSGVADMVN TGGRAGGSIT AALFLKQFVS
EKVQWMHIDM AGPVWNEKKK SGTGFGVATL VEWVQKNSSS
