AMPP2_ARATH
ID AMPP2_ARATH Reviewed; 710 AA.
AC Q8RY11; Q9MA84;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Aminopeptidase P2 {ECO:0000303|PubMed:11891249};
DE Short=AtAPP2 {ECO:0000303|PubMed:11891249};
DE EC=3.4.11.9 {ECO:0000250|UniProtKB:F4JQH3};
DE Flags: Precursor;
GN Name=APP2 {ECO:0000303|PubMed:11891249};
GN OrderedLocusNames=At3g05350 {ECO:0000312|Araport:AT3G05350};
GN ORFNames=T12H1.32 {ECO:0000312|EMBL:AAF27041.1};
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 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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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).
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides, such as Arg-Pro-Pro.
CC {ECO:0000250|UniProtKB:Q9VJG0}.
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:0000250|UniProtKB:F4JQH3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NQW7};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q9NQW7};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NQW7}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27041.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009177; AAF27041.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74224.1; -; Genomic_DNA.
DR EMBL; AY079018; AAL84973.1; -; mRNA.
DR EMBL; BT001080; AAN46861.1; -; mRNA.
DR RefSeq; NP_187186.5; NM_111408.7.
DR AlphaFoldDB; Q8RY11; -.
DR SMR; Q8RY11; -.
DR IntAct; Q8RY11; 2.
DR STRING; 3702.AT3G05350.1; -.
DR MEROPS; M24.A04; -.
DR PaxDb; Q8RY11; -.
DR PRIDE; Q8RY11; -.
DR ProteomicsDB; 244479; -.
DR EnsemblPlants; AT3G05350.1; AT3G05350.1; AT3G05350.
DR GeneID; 819699; -.
DR Gramene; AT3G05350.1; AT3G05350.1; AT3G05350.
DR KEGG; ath:AT3G05350; -.
DR Araport; AT3G05350; -.
DR TAIR; locus:2096319; AT3G05350.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_1_1; -.
DR InParanoid; Q8RY11; -.
DR OMA; YRPGKWG; -.
DR OrthoDB; 417805at2759; -.
DR PhylomeDB; Q8RY11; -.
DR PRO; PR:Q8RY11; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RY11; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
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 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.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Chloroplast; Hydrolase; Manganese; Metal-binding;
KW Metalloprotease; Plastid; Protease; Reference proteome; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..710
FT /note="Aminopeptidase P2"
FT /id="PRO_0000444156"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 506
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 517
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 517
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 580
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 580
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 589
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 614
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 614
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 628
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
FT BINDING 628
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW7"
SQ SEQUENCE 710 AA; 78709 MW; 9C888095DEFDB0A1 CRC64;
MIPLTLSSPS LNRLVLSTSR YSHSLFLSNF NSLSLIHRKL PYKPLFGARC HASSSSSSSS
SFTAKSSKEI RKAQTKVVVD EKLSSIRRLF SEPGVGIDAY IIPSQDAHQS EFIAECYARR
AYISGFTGSA GTAVVTKDKA ALWTDGRYFL QAEKQLNSSW ILMRAGNPGV PTASEWIADV
LAPGGRVGID PFLFSADAAE ELKEVIAKKN HELVYLYNVN LVDEIWKDSR PKPPSRQIRI
HDLKYAGLDV ASKLLSLRNQ IMDAGTSAIV ISMLDEIAWV LNLRGSDVPH SPVMYAYLIV
EVDQAQLFVD NSKVTVEVKD HLKNAGIELR PYDSILQGID SLAARGAQLL MDPSTLNVAI
ISTYKSACER YSRNFESEAK VKTKFTDSSS GYTANPSGIY MQSPISWAKA IKNDAELKGM
KNSHLRDAAA LAHFWAWLEE EVHKNANLTE VDVADRLLEF RSMQDGFMDT SFDTISGSGA
NGAIIHYKPE PESCSRVDPQ KLFLLDSGAQ YVDGTTDITR TVHFSEPSAR EKECFTRVLQ
GHIALDQAVF PEGTPGFVLD GFARSSLWKI GLDYRHGTGH GVGAALNVHE GPQSISFRYG
NMTPLQNGMI VSNEPGYYED HAFGIRIENL LHVRDAETPN RFGGATYLGF EKLTFFPIQT
KMVDVSLLSD TEVDWLNSYH AEVWEKVSPL LEGSTTQQWL WNNTRPLAKP
