AMPP1_ARATH
ID AMPP1_ARATH Reviewed; 645 AA.
AC F4JQH3; O23206; Q6Q8B7; Q8H1P6;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Aminopeptidase P1 {ECO:0000303|PubMed:11891249};
DE Short=AtAPP1 {ECO:0000303|PubMed:11891249};
DE EC=3.4.11.9 {ECO:0000269|PubMed:11891249};
GN Name=APP1 {ECO:0000303|PubMed:11891249};
GN OrderedLocusNames=At4g36760 {ECO:0000312|Araport:AT4G36760};
GN ORFNames=AP22.64 {ECO:0000312|EMBL:CAB80342.1},
GN C7A10.600 {ECO:0000312|EMBL:CAB16823.1};
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] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 231-244,
RP FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, BINDING TO NPA, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=11891249; DOI=10.1104/pp.010519;
RA Murphy A.S., Hoogner K.R., Peer W.A., Taiz L.;
RT "Identification, purification, and molecular cloning of N-1-
RT naphthylphthalmic acid-binding plasma membrane-associated aminopeptidases
RT from Arabidopsis.";
RL Plant Physiol. 128:935-950(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides, such as Arg-Pro-Pro (By similarity).
CC Aminopeptidase that binds to the auxin transport inhibitor N-1-
CC naphthylphthalamic acid (NPA). May play a negative role in the
CC regulation of PIN auxin transport proteins (PubMed:11891249).
CC {ECO:0000250|UniProtKB:Q9VJG0, ECO:0000269|PubMed:11891249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9; Evidence={ECO:0000269|PubMed:11891249};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11891249};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11891249};
CC Note=Binds 2 manganese or zinc ions per subunit.
CC {ECO:0000269|PubMed:11891249};
CC -!- ACTIVITY REGULATION: Inhibited by EGTA and apstatin, and, to some
CC extent, by the flavonoid kaempferol. {ECO:0000269|PubMed:11891249}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=36 nmol/min/mg enzyme for Tyr-aminofluoromethylcoumarin
CC {ECO:0000269|PubMed:11891249};
CC Vmax=20 nmol/min/mg enzyme for Trp-aminofluoromethylcoumarin
CC {ECO:0000269|PubMed:11891249};
CC Vmax=74 nmol/min/mg enzyme for Ala-Pro-aminofluoromethylcoumarin
CC {ECO:0000269|PubMed:11891249};
CC Vmax=29 nmol/min/mg enzyme for Pro-aminofluoromethylcoumarin
CC {ECO:0000269|PubMed:11891249};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with N-1-
CC naphthylphthalamic acid (NPA) (PubMed:11891249).
CC {ECO:0000250|UniProtKB:Q9NQW7, ECO:0000269|PubMed:11891249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891249}. Cell
CC membrane {ECO:0000269|PubMed:11891249}; Peripheral membrane protein
CC {ECO:0000303|PubMed:11891249}. Microsome membrane
CC {ECO:0000269|PubMed:11891249}; Peripheral membrane protein
CC {ECO:0000303|PubMed:11891249}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JQH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JQH3-2; Sequence=VSP_059579;
CC -!- TISSUE SPECIFICITY: Ubiquitous with preferential expression in 5 days-
CC old seedlings, roots, flowers, inflorescences and rosette leaves (at
CC protein levels). {ECO:0000269|PubMed:11891249}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 3 days and peaks at 5 days.
CC After, expression levels remain constant from 7 to 10 days.
CC {ECO:0000269|PubMed:11891249}.
CC -!- PTM: Glycosylated. Also present in a non-glycosylated form.
CC {ECO:0000269|PubMed:11891249}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; AY143575; AAN41402.1; -; mRNA.
DR EMBL; AY552784; AAS58497.1; -; mRNA.
DR EMBL; Z99708; CAB16823.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80342.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86698.1; -; Genomic_DNA.
DR EMBL; BT046181; ACI49780.1; -; mRNA.
DR PIR; B85434; B85434.
DR RefSeq; NP_195394.4; NM_119840.7. [F4JQH3-1]
DR AlphaFoldDB; F4JQH3; -.
DR SMR; F4JQH3; -.
DR STRING; 3702.AT4G36760.1; -.
DR MEROPS; M24.037; -.
DR iPTMnet; F4JQH3; -.
DR MetOSite; F4JQH3; -.
DR PaxDb; F4JQH3; -.
DR PRIDE; F4JQH3; -.
DR ProteomicsDB; 244419; -. [F4JQH3-1]
DR EnsemblPlants; AT4G36760.1; AT4G36760.1; AT4G36760. [F4JQH3-1]
DR GeneID; 829829; -.
DR Gramene; AT4G36760.1; AT4G36760.1; AT4G36760. [F4JQH3-1]
DR KEGG; ath:AT4G36760; -.
DR Araport; AT4G36760; -.
DR TAIR; locus:2115370; AT4G36760.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_0_1; -.
DR InParanoid; F4JQH3; -.
DR PRO; PR:F4JQH3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JQH3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:TAIR.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0010013; F:N-1-naphthylphthalamic acid binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0009926; P:auxin polar transport; TAS:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.40.350.10; -; 2.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Aminopeptidase; Cell membrane;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Manganese; Membrane; Metal-binding; Metalloprotease; Microsome;
KW Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..645
FT /note="Aminopeptidase P1"
FT /id="PRO_0000444155"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 440
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 451
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 451
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 514
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 514
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 523
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 549
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 563
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 563
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /id="VSP_059579"
FT CONFLICT 394
FT /note="Missing (in Ref. 1; AAN41402/AAS58497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 71993 MW; D72850FDAD5F53A2 CRC64;
MSEILSSLRS LMASHSPPLD ALVVPSEDYH QSEYVSARDK RREFVSGFSG SAGLALITKK
EARLWTDGRY FLQALQQLSD EWTLMRMGED PLVEVWMSDN LPEEANIGVD SWCVSVDTAN
RWGKSFAKKN QKLITTTTDL VDEVWKSRPP SEMSPVVVHP LEFAGRSVSH KFEDLRAKLK
QEGARGLVIA ALDEVAWLYN IRGTDVAYCP VVHAFAILTT DSAFLYVDKK KVSDEANSYF
NGLGVEVREY TDVISDVALL ASDRLISSFA SKTVQHEAAK DMEIDSDQPD RLWVDPASCC
YALYSKLDAE KVLLQPSPIS LSKALKNPVE LEGIKNAHVR DGAAVVQYLV WLDNQMQELY
GASGYFLEAE ASKKKPSETS KLTEVTVSDK LESLRASKEH FRGLSFPTIS SVGSNAAVIH
YSPEPEACAE MDPDKIYLCD SGAQYLDGTT DITRTVHFGK PSAHEKECYT AVFKGHVALG
NARFPKGTNG YTLDILARAP LWKYGLDYRH GTGHGVGSYL CVHEGPHQVS FRPSARNVPL
QATMTVTDEP GYYEDGNFGI RLENVLVVND AETEFNFGDK GYLQFEHITW APYQVKLIDL
DELTREEIDW LNTYHSKCKD ILAPFMNQTE MEWLKKATEP VSVSA
