AMPL3_ARATH
ID AMPL3_ARATH Reviewed; 581 AA.
AC Q8RX72; O65558;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Leucine aminopeptidase 3, chloroplastic;
DE EC=3.4.11.1;
DE AltName: Full=Leucyl aminopeptidase 3;
DE Short=AtLAP3 {ECO:0000303|PubMed:25716890};
DE AltName: Full=Proline aminopeptidase 3;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase 3;
DE Flags: Precursor;
GN Name=LAP3 {ECO:0000303|PubMed:25716890}; OrderedLocusNames=At4g30910;
GN ORFNames=F6I18.180;
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=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 Cys-Gly dipeptidase activity (PubMed:25716890).
CC {ECO:0000250|UniProtKB:P30184, ECO:0000269|PubMed:25716890}.
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=CAA18202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79809.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022198; CAA18202.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161577; CAB79809.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85829.1; -; Genomic_DNA.
DR EMBL; AY090346; AAL91252.1; -; mRNA.
DR EMBL; AY125537; AAM78047.1; -; mRNA.
DR PIR; H85361; H85361.
DR RefSeq; NP_194820.1; NM_119238.5.
DR AlphaFoldDB; Q8RX72; -.
DR SMR; Q8RX72; -.
DR BioGRID; 14502; 7.
DR STRING; 3702.AT4G30910.1; -.
DR MEROPS; M17.A02; -.
DR iPTMnet; Q8RX72; -.
DR PaxDb; Q8RX72; -.
DR PRIDE; Q8RX72; -.
DR ProteomicsDB; 245050; -.
DR EnsemblPlants; AT4G30910.1; AT4G30910.1; AT4G30910.
DR GeneID; 829215; -.
DR Gramene; AT4G30910.1; AT4G30910.1; AT4G30910.
DR KEGG; ath:AT4G30910; -.
DR Araport; AT4G30910; -.
DR TAIR; locus:2126669; AT4G30910.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_5_1_1; -.
DR InParanoid; Q8RX72; -.
DR PhylomeDB; Q8RX72; -.
DR PRO; PR:Q8RX72; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8RX72; baseline and differential.
DR Genevisible; Q8RX72; 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:0016805; F:dipeptidase 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: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.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Chloroplast; Hydrolase; Manganese; Metal-binding; Plastid;
KW Protease; Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..581
FT /note="Leucine aminopeptidase 3, chloroplastic"
FT /id="PRO_0000045811"
FT ACT_SITE 362
FT /evidence="ECO:0000255"
FT ACT_SITE 439
FT /evidence="ECO:0000255"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 355
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 355
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 435
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 437
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P30184"
FT BINDING 437
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P30184"
SQ SEQUENCE 581 AA; 61290 MW; C4B674CFF40F1DC0 CRC64;
MAVTLVTSCA SSSRFHFRSF SSSPSSLSSC FVRFQLLSRL RVSFAITPLY CSSKATAHTI
AHATLGLTQA NSVDHPKISF SGKEIDVTEW KGDILAVGVT EKDMAKDANS KFENPILKKL
DAHLGGLLAD VSAEEDFSGK PGQSTVLRLP GLGSKRVGLI GLGKSASTPS AFQSLGEAVA
AAAKASQASS VAVVLASSES FSDESKLSSA SDIASGTVLG LFEDSRYKSE SKKPSLKSVV
FIGFGTGPEL ENKLKYAEHV SYGVIFTKEL VNSPANVLSP AVLAEEASNL ASMYSNVMTA
NILKEEQCKE LKMGSYLAVA AASANPPHFI HLIYKPSSGP VKTKLALVGK GLTFDSGGYN
IKIGPELIIE LMKIDVGGSA AVLGAAKAIG EIKPPGVEVH FIVAACENMI SGTGMRPGDV
ITASNGKTIE VNDTDSEGRL TLADALVYAC NQGVDKIVDI ATLTGEIIVA LGPSMAGMYT
ASDELAKEVI AASQRSGEKL WRMPMEESYW EMMKSGVADM VNFGGRAGGS ITAALFLKRF
VSENVEWLHI DMAGRVWNEK KKAATGFGVA TLVEWVQNNS S
