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 24-JAN-2024, entry version 86.
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.F4JVN6; -.
DR MEROPS; S08.A56; -.
DR iPTMnet; F4JVN6; -.
DR MetOSite; F4JVN6; -.
DR PaxDb; 3702-AT4G20850-1; -.
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; AT4G20850; TPP2.
DR eggNOG; KOG1114; Eukaryota.
DR HOGENOM; CLU_003084_1_0_1; -.
DR InParanoid; F4JVN6; -.
DR OMA; SLRDFQC; -.
DR OrthoDB; 2441948at2759; -.
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; 1.25.40.710; -; 1.
DR Gene3D; 2.60.40.3170; -; 1.
DR Gene3D; 6.10.250.3080; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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; IPR034051; TPP_II_domain.
DR InterPro; IPR046939; TPPII_C_sf.
DR InterPro; IPR048384; TPPII_GBD.
DR InterPro; IPR048383; TPPII_Ig-like-1.
DR InterPro; IPR022229; TPPII_Ig-like-2.
DR InterPro; IPR046940; TPPII_Ig-like_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR Pfam; PF21316; TPPII_GBD; 1.
DR Pfam; PF21223; TPPII_Ig-like-1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 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
//
