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Tripeptidyl-peptidase 2 (EC 3.4.14.10) (Tripeptidyl-peptidase II) (TPPII)

 TPPII_ARATH             Reviewed;        1380 AA.
F4JVN6; Q8L640; Q9SUC7;
11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
25-OCT-2017, entry version 57.
RecName: Full=Tripeptidyl-peptidase 2;
EC=3.4.14.10;
AltName: Full=Tripeptidyl-peptidase II;
Short=TPPII;
Name=TPP2; OrderedLocusNames=At4g20850; ORFNames=T13K14.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-1380.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, AND DISRUPTION
PHENOTYPE.
PubMed=15908606; DOI=10.1104/pp.104.057406;
Book A.J., Yang P., Scalf M., Smith L.M., Vierstra R.D.;
"Tripeptidyl peptidase II. An oligomeric protease complex from
Arabidopsis.";
Plant Physiol. 138:1046-1057(2005).
[5]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INDUCTION BY
CADMIUM.
PubMed=19822524; DOI=10.1074/jbc.M109.035394;
Polge C., Jaquinod M., Holzer F., Bourguignon J., Walling L.,
Brouquisse R.;
"Evidence for the existence in Arabidopsis thaliana of the proteasome
proteolytic pathway: ACTIVATION IN RESPONSE TO CADMIUM.";
J. Biol. Chem. 284:35412-35424(2009).
-!- FUNCTION: Serine protease of the proteasome pathway that may
function with the 20S proteasome to degrade oxidized proteins
generated by environmental stress. {ECO:0000269|PubMed:15908606,
ECO:0000269|PubMed:19822524}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal tripeptide from a
polypeptide. {ECO:0000270|PROSITE-ProRule:PRU10081,
ECO:0000270|PROSITE-ProRule:PRU10082}.
-!- ENZYME REGULATION: Inhibited by alanine-alanine-phenylalanine-
chloromethylketone, butabindide and phenylmethanesulfonyl fluoride
(PMSF), but not by leupeptin, N-ethylmaleimide, EDTA, MG132 and
lactacystin.
-!- SUBUNIT: Assembles into a large oligomeric complex containing two
related proteins 153 and 142 kDa that are derived from the single
TPP2 gene. The 142 kDa form mainly differs from the 153 kDa form
by a truncation at the C-terminal end.
{ECO:0000269|PubMed:15908606}.
-!- INDUCTION: By cadmium (at protein level).
{ECO:0000269|PubMed:19822524}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions. {ECO:0000269|PubMed:15908606}.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000320}.
-!- SEQUENCE CAUTION:
Sequence=CAB45880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000320};
Sequence=CAB79085.1; Type=Erroneous gene model prediction; Evidence={ECO:0000320};
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EMBL; AL080282; CAB45880.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161553; CAB79085.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE84368.1; -; Genomic_DNA.
EMBL; AY096651; AAM20148.1; -; mRNA.
PIR; T10627; T10627.
RefSeq; NP_193817.2; NM_118203.4.
UniGene; At.44849; -.
ProteinModelPortal; F4JVN6; -.
BioGrid; 13124; 2.
STRING; 3702.AT4G20850.1; -.
MEROPS; S08.A56; -.
iPTMnet; F4JVN6; -.
PaxDb; F4JVN6; -.
PRIDE; F4JVN6; -.
ProMEX; F4JVN6; -.
EnsemblPlants; AT4G20850.1; AT4G20850.1; AT4G20850.
GeneID; 827833; -.
Gramene; AT4G20850.1; AT4G20850.1; AT4G20850.
KEGG; ath:AT4G20850; -.
Araport; AT4G20850; -.
TAIR; locus:2133039; AT4G20850.
eggNOG; KOG1114; Eukaryota.
eggNOG; COG1404; LUCA.
HOGENOM; HOG000008178; -.
KO; K01280; -.
OMA; RIDVINM; -.
OrthoDB; EOG0936009S; -.
Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation.
PRO; PR:F4JVN6; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; F4JVN6; baseline and differential.
Genevisible; F4JVN6; AT.
GO; GO:0009507; C:chloroplast; HTP:TAIR.
GO; GO:0005737; C:cytoplasm; HTP:TAIR.
GO; GO:0022626; C:cytosolic ribosome; HTP:TAIR.
GO; GO:0016020; C:membrane; HTP:TAIR.
GO; GO:0005774; C:vacuolar membrane; HTP:TAIR.
GO; GO:0005773; C:vacuole; HTP:TAIR.
GO; GO:0004177; F:aminopeptidase activity; RCA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; RCA:InterPro.
GO; GO:0008240; F:tripeptidyl-peptidase activity; HTP:TAIR.
GO; GO:0006508; P:proteolysis; HTP:TAIR.
CDD; cd04857; Peptidases_S8_Tripeptidyl_Amin; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR022229; Peptidase_S8A_TPPII.
InterPro; IPR034051; TPP_II_domain.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF12580; TPPII; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 2.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Aminopeptidase; Coiled coil; Complete proteome; Hydrolase; Protease;
Reference proteome; Serine protease; Stress response.
CHAIN 1 1380 Tripeptidyl-peptidase 2.
/FTId=PRO_0000429313.
DOMAIN 140 620 Peptidase S8.
COILED 1152 1181 {ECO:0000270}.
COILED 1238 1300 {ECO:0000270}.
COMPBIAS 83 91 Poly-Gly.
ACT_SITE 145 145 Charge relay system. {ECO:0007001}.
ACT_SITE 372 372 Charge relay system. {ECO:0007001}.
ACT_SITE 558 558 Charge relay system. {ECO:0007001}.
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


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