ID   TPPII_ARATH             Reviewed;        1380 AA.
AC   F4JVN6; Q8L640; Q9SUC7;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Tripeptidyl-peptidase 2;
DE            EC=3.4.14.10 {ECO:0000269|PubMed:15908606, ECO:0000269|PubMed:19822524};
DE   AltName: Full=Tripeptidyl-peptidase II;
DE            Short=TPPII;
GN   Name=TPP2; OrderedLocusNames=At4g20850; ORFNames=T13K14.10;
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] OF 35-1380.
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   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=15908606; DOI=10.1104/pp.104.057406;
RA   Book A.J., Yang P., Scalf M., Smith L.M., Vierstra R.D.;
RT   "Tripeptidyl peptidase II. An oligomeric protease complex from
RT   Arabidopsis.";
RL   Plant Physiol. 138:1046-1057(2005).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP   INDUCTION BY CADMIUM.
RX   PubMed=19822524; DOI=10.1074/jbc.m109.035394;
RA   Polge C., Jaquinod M., Holzer F., Bourguignon J., Walling L.,
RA   Brouquisse R.;
RT   "Evidence for the existence in Arabidopsis thaliana of the proteasome
RT   proteolytic pathway: ACTIVATION IN RESPONSE TO CADMIUM.";
RL   J. Biol. Chem. 284:35412-35424(2009).
CC   -!- FUNCTION: Serine protease of the proteasome pathway that may function
CC       with the 20S proteasome to degrade oxidized proteins generated by
CC       environmental stress. {ECO:0000269|PubMed:15908606,
CC       ECO:0000269|PubMed:19822524}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC         EC=3.4.14.10; Evidence={ECO:0000269|PubMed:15908606,
CC         ECO:0000269|PubMed:19822524};
CC   -!- ACTIVITY REGULATION: Inhibited by alanine-alanine-phenylalanine-
CC       chloromethylketone, butabindide and phenylmethanesulfonyl fluoride
CC       (PMSF), but not by leupeptin, N-ethylmaleimide, EDTA, MG132 and
CC       lactacystin.
CC   -!- SUBUNIT: Assembles into a large oligomeric complex containing two
CC       related proteins 153 and 142 kDa that are derived from the single TPP2
CC       gene. The 142 kDa form mainly differs from the 153 kDa form by a
CC       truncation at the C-terminal end. {ECO:0000269|PubMed:15908606}.
CC   -!- INDUCTION: By cadmium (at protein level).
CC       {ECO:0000269|PubMed:19822524}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:15908606}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB45880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79085.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL080282; CAB45880.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161553; CAB79085.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84368.1; -; Genomic_DNA.
DR   EMBL; AY096651; AAM20148.1; -; mRNA.
DR   PIR; T10627; T10627.
DR   RefSeq; NP_193817.2; NM_118203.4.
DR   AlphaFoldDB; F4JVN6; -.
DR   SMR; F4JVN6; -.
DR   BioGRID; 13124; 36.
DR   IntAct; F4JVN6; 1.
DR   STRING; 3702.AT4G20850.1; -.
DR   MEROPS; S08.A56; -.
DR   iPTMnet; F4JVN6; -.
DR   MetOSite; F4JVN6; -.
DR   PaxDb; F4JVN6; -.
DR   PRIDE; F4JVN6; -.
DR   ProMEX; F4JVN6; -.
DR   ProteomicsDB; 245255; -.
DR   EnsemblPlants; AT4G20850.1; AT4G20850.1; AT4G20850.
DR   GeneID; 827833; -.
DR   Gramene; AT4G20850.1; AT4G20850.1; AT4G20850.
DR   KEGG; ath:AT4G20850; -.
DR   Araport; AT4G20850; -.
DR   TAIR; locus:2133039; AT4G20850.
DR   eggNOG; KOG1114; Eukaryota.
DR   HOGENOM; CLU_003084_1_0_1; -.
DR   OMA; SLRDFQC; -.
DR   OrthoDB; 156304at2759; -.
DR   PRO; PR:F4JVN6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JVN6; baseline and differential.
DR   Genevisible; F4JVN6; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IDA:TAIR.
DR   GO; GO:0006508; P:proteolysis; IDA:TAIR.
DR   CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR   Gene3D; 3.40.50.200; -; 2.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR022229; Peptidase_S8A_TPPII.
DR   InterPro; IPR034051; TPP_II_domain.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF12580; TPPII; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Coiled coil; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Stress response.
FT   CHAIN           1..1380
FT                   /note="Tripeptidyl-peptidase 2"
FT                   /id="PRO_0000429313"
FT   DOMAIN          110..619
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          1099..1143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1152..1181
FT                   /evidence="ECO:0000255"
FT   COILED          1238..1300
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        145
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        372
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        558
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1380 AA;  152368 MW;  552DECB8D9FCDE53 CRC64;
     MDLSLQLQIH GALINKGPSC TSYWASSSSL SLPRDFISSS TFLLHRRLRR RSCSRSRGIR
     LRRSGFSAMP CSSSDTLTAS RVGCGGGGGG GAVGGGAENA SVANFKLNES TFIASLMPKK
     EIRADCFIEA HPEYDGRGVV IAIFDSGFDP SAAGLHVTSD GKPKVLDVID CTGSGDIDTS
     TVVKANEDGH IRGASGATLV VNSSWKNPTG EWRVGSKLVY QLFTDDLTSR VKKERRKSWD
     EKNQEEIAKA VNNLYDFDQK HSKVEDAKLK KTREDLQSKV DFLKKQADKY EDKGPVIDAV
     VWHDGEVWRV ALDTQSLEED PDSGKLADFS PLTNYRIERK YGVFSRLDAC SFVANVYDEG
     KVLSIVTDSS PHGTHVAGIA TAHHPEEHLL NGVAPGAQII SCKIGDSRLG SMETGTGLTR
     ALIAALEHNC DLVNMSYGEP ALLPDYGRFV DLVTEAVNKR RLIFVSSAGN SGPALTTVGA
     PGGTTSSIIG VGAYVSPAMA AGAHSVVEPP SEGLEYTWSS RGPTSDGDLG VCISAPGGAV
     APVPTWTLQR RMLMNGTSMA SPSACGAIAL LLSAMKAEGI PVSPYSVRRA LENTSTPVGD
     LPEDKLTTGQ GLMQVDKAYE YLKQFQDYPC VFYQIKVNLS GKTIPTSRGI YLREGTACRQ
     STEWTIQVDP KFHEGASNLK ELVPFEECLE LHSTDEGVVR VPDYLLLTNN GRGFNVVVDP
     TNLGDGVHYF EVYGIDCKAP ERGPLFRIPV TIIIPKTVAN QPPVISFQQM SFISGHIERR
     YIEVPHGATW AEATMRTSGF DTTRRFYIDT LQVCPLRRPI KWESAPTFAS PSAKSFVFPV
     VSGQTMELAI AQFWSSGLGS REPTIVDFEI EFHGVGVDKE ELLLDGSEAP IKVEAEALLA
     SEKLVPIAVL NKIRVPYQPI DAQLKTLSTG RDRLLSGKQI LALTLTYKFK LEDSAEVKPY
     IPLLNNRIYD TKFESQFFMI SDTNKRVYAM GDVYPESSKL PKGEYKLQLY LRHENVELLE
     KLKQLTVFIE RNMGEIRLNL HSEPDGPFTG NGAFKSSVLM PGVKEAFYLG PPTKDKLPKN
     TPQGSMLVGE ISYGKLSFDE KEGKNPKDNP VSYPISYVVP PNKPEEDKKA ASAPTCSKSV
     SERLEQEVRD TKIKFLGNLK QETEEERSEW RKLCTCLKSE YPDYTPLLAK ILEGLLSRSD
     AGDKISHHEE IIEAANEVVR SVDVDELARF LLDKTEPEDD EAEKLKKKME VTRDQLADAL
     YQKGLAMARI ENLKGEKEGE GEEESSQKDK FEENFKELTK WVDVKSSKYG TLTVLREKRL
     SRLGTALKVL DDLIQNENET ANKKLYELKL DLLEEIGWSH LVTYEKQWMQ VRFPKSLPLF