AMPL2_ARATH
ID AMPL2_ARATH Reviewed; 583 AA.
AC Q944P7; O65557;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Leucine aminopeptidase 2, chloroplastic;
DE EC=3.4.11.1;
DE AltName: Full=Leucyl aminopeptidase 2;
DE Short=AtLAP2 {ECO:0000303|PubMed:22493451};
DE AltName: Full=Proline aminopeptidase 2;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase 2;
DE Flags: Precursor;
GN Name=LAP2 {ECO:0000303|PubMed:22493451}; OrderedLocusNames=At4g30920;
GN ORFNames=F6I18.170;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION.
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 (By similarity). Possesses
CC leucine aminopeptidase activity against the model substrate leucine-
CC amido methyl coumarin (PubMed:22493451). Does not seem to possess Cys-
CC Gly dipeptidase activity (PubMed:25716890).
CC {ECO:0000250|UniProtKB:P30184, ECO:0000269|PubMed:22493451,
CC ECO:0000269|PubMed:25716890}.
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 -!- 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:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18201.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79810.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022198; CAA18201.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161577; CAB79810.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85830.1; -; Genomic_DNA.
DR EMBL; AF424634; AAL11627.1; -; mRNA.
DR EMBL; BT002652; AAO11568.1; -; mRNA.
DR PIR; A85362; A85362.
DR RefSeq; NP_194821.1; NM_119239.3.
DR AlphaFoldDB; Q944P7; -.
DR SMR; Q944P7; -.
DR BioGRID; 14503; 6.
DR STRING; 3702.AT4G30920.1; -.
DR MEROPS; M17.A01; -.
DR PaxDb; Q944P7; -.
DR PRIDE; Q944P7; -.
DR ProteomicsDB; 244413; -.
DR EnsemblPlants; AT4G30920.1; AT4G30920.1; AT4G30920.
DR GeneID; 829216; -.
DR Gramene; AT4G30920.1; AT4G30920.1; AT4G30920.
DR KEGG; ath:AT4G30920; -.
DR Araport; AT4G30920; -.
DR TAIR; locus:2126684; AT4G30920.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_5_1_1; -.
DR InParanoid; Q944P7; -.
DR OMA; MPLWKYF; -.
DR OrthoDB; 562530at2759; -.
DR PhylomeDB; Q944P7; -.
DR PRO; PR:Q944P7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q944P7; baseline and differential.
DR Genevisible; Q944P7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
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:0010150; P:leaf senescence; IMP:TAIR.
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..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 71..583
FT /note="Leucine aminopeptidase 2, chloroplastic"
FT /id="PRO_0000045812"
FT ACT_SITE 363
FT /evidence="ECO:0000255"
FT ACT_SITE 440
FT /evidence="ECO:0000255"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 376
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT CONFLICT 91
FT /note="W -> G (in Ref. 3; AAL11627/AAO11568)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="D -> G (in Ref. 3; AAL11627/AAO11568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 61307 MW; 1045CC6F326644AB CRC64;
MAVTLVTSFA SSSSRFHFRS FSSSPSSLSS CFVRFQFPSR LRLAFAVTPL YSSSRAMAHT
ISHATLGLTQ ANSVDHPKIS FSGKEIDVTE WKGDILAVGV TEKDMAKDVN SKFENPILKK
LDAHLGGLLA DVSSEEDFSG KPGQSTVLRL PGLGSKRVGL IGLGKSASTP SAFQSLGEAV
AAAAKASQAS SVAVVLASSE SVSNESKLCS ASAIASGTVL GLFEDSRYKS ESKKPSLKSV
DIIGFGSGPE LEKKLKYAEH VSYGVIFGKE LVNSPANVLT PAVLAEEALN LASMYSDVMT
ANILNEEQCK ELKMGSYLAV AAASANPPHF IHLIYKPSSG PVKTKLALVG KGLTFDSGGY
NIKTGPGCLI ELMKFDMGGS AAVLGAAKAI GQIKPPGVEV HFIVAACENM ISGTGMRPGD
VLTASNGKTI EVNNTDAEGR LTLADALVYA CNQGVDKVVD LATLTGACII ALGTSMAGIY
TPSDKLAKEV IAASERSGEK LWRMPMEESY WEMMKSGVAD MVNTGGRAGG SITAALFLKQ
FVSEDVEWMH IDMAGPVWNE KKKAATGFGV ATLVEWVQNH SSS
