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Cathepsin B-like protease 3 (EC 3.4.22.-) (Cathepsin B3) (AtCathB3)

 CATB3_ARATH             Reviewed;         359 AA.
Q94K85; Q9ZSI0;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
10-OCT-2018, entry version 140.
RecName: Full=Cathepsin B-like protease 3 {ECO:0000305};
EC=3.4.22.- {ECO:0000305};
AltName: Full=Cathepsin B3 {ECO:0000305};
Short=AtCathB3 {ECO:0000303|PubMed:19453434};
Flags: Precursor;
Name=CATHB3 {ECO:0000303|PubMed:19453434};
OrderedLocusNames=At4g01610 {ECO:0000312|Araport:AT4G01610};
ORFNames=T15B16.17a {ECO:0000312|EMBL:AAC72872.1};
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 [MRNA] (ISOFORM 1).
Stracke R., Palme K.;
"Signal peptide selection derived cDNAs from Arabidopsis thaliana
leaves and guard cells.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[2]
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).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=15539469; DOI=10.1105/tpc.104.027078;
Carter C., Pan S., Zouhar J., Avila E.L., Girke T., Raikhel N.V.;
"The vegetative vacuole proteome of Arabidopsis thaliana reveals
predicted and unexpected proteins.";
Plant Cell 16:3285-3303(2004).
[7]
FUNCTION, AND INDUCTION.
PubMed=19453434; DOI=10.1111/j.1469-8137.2009.02865.x;
McLellan H., Gilroy E.M., Yun B.W., Birch P.R., Loake G.J.;
"Functional redundancy in the Arabidopsis cathepsin B gene family
contributes to basal defence, the hypersensitive response and
senescence.";
New Phytol. 183:408-418(2009).
[8]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=24600022; DOI=10.1093/jxb/eru055;
Iglesias-Fernandez R., Wozny D., Iriondo-de Hond M., Onate-Sanchez L.,
Carbonero P., Barrero-Sicilia C.;
"The AtCathB3 gene, encoding a cathepsin B-like protease, is expressed
during germination of Arabidopsis thaliana and transcriptionally
repressed by the basic leucine zipper protein GBF1.";
J. Exp. Bot. 65:2009-2021(2014).
[9]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVITY REGULATION, CLEAVAGE OF SIGNAL PEPTIDE AFTER
LYS-26, CLEAVAGE OF ACTIVATION PROPEPTIDE AFTER LYS-102, CLEAVAGE OF
C-TERMINUS PROPEPTIDE AFTER LYS-342, AND MUTAGENESIS OF CYS-131.
PubMed=27058316; DOI=10.1038/cdd.2016.34;
Ge Y., Cai Y.M., Bonneau L., Rotari V., Danon A., McKenzie E.A.,
McLellan H., Mach L., Gallois P.;
"Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed
cell death in Arabidopsis.";
Cell Death Differ. 23:1493-1501(2016).
-!- FUNCTION: Thiol protease that possesses high activity toward the
cathepsin synthetic substrate Arg-Arg-7-amino-4-methylcoumarin
(RR-AMC) and the papain substrate Gly-Arg-Arg-AMC (GRR-AMC). Can
cleave the papain substrate Phe-Arg-AMC (FR-AMC) and the caspase-3
substrate Asp-Glu-Val-Asp-rhodamine 110 (DEVD-R110). Has no
activity towards the caspase-6 substrate VEID-AMC, caspase-8
substrate IETD-AMC and caspase-1 substrate YVAD-AMC
(PubMed:27058316). Plays a central role in plant programmed cell
death (PCD). In addition to its role in protein degradation, may
cleave and/or degrade a number of target proteins, activating
signaling towards PCD. Contributes to the increase of caspase-3-
like activity after UV-C-induced PCD and is required for abiotic
stress-induced PCD (PubMed:27058316). Functions redundantly with
CATHB1 and CATHB2 in basal defense and distinct forms of plant
programmed cell death (PCD). Participates to the establishment of
basal resistance against the bacterial pathogen Pseudomonase
syringae pv. tomato DC3000. Required for full levels of PCD during
resistance (R) gene-mediated hypersensitive response (HR).
Involved in the regulation of senescence, a developmental form of
PCD in plants (PubMed:19453434). May be involved in the
degradation of seed storage proteins during seed germination
(PubMed:24600022). {ECO:0000269|PubMed:19453434,
ECO:0000269|PubMed:24600022, ECO:0000269|PubMed:27058316}.
-!- ACTIVITY REGULATION: Inhibited by the cathepsin B inhibitors Ac-
LVK-CHO, CA-074 and Z-FA-FMK, and the caspase-3 inhibitor Z-DEVD-
CHO. {ECO:0000269|PubMed:27058316}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5. {ECO:0000269|PubMed:27058316};
-!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:15539469}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q94K85-1; Sequence=Displayed;
Name=2;
IsoId=Q94K85-2; Sequence=VSP_058851;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in root tips, root vasculature,
emerging lateral root, hydathodes, vascular tissue of leaves,
vasculature of sepals and anthers, stigma, and vascular bundles at
the base and the upper part of the siliques.
{ECO:0000269|PubMed:24600022}.
-!- DEVELOPMENTAL STAGE: Expressed in developing siliques 13 to 15
days after pollination (DAP). In germinating seeds, expressed from
12 to 48 hours after imbibition with a peak of expression at 24
hours. {ECO:0000269|PubMed:24600022}.
-!- INDUCTION: By dark-induced senescence. Induced by infection with
an avirulent strain of the bacterial pathogen Pseudomonase
syringae pv. tomato DC3000. {ECO:0000269|PubMed:19453434}.
-!- DISRUPTION PHENOTYPE: Delayed germination and decreased
germination rate. {ECO:0000269|PubMed:24600022}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089}.
-----------------------------------------------------------------------
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EMBL; AF083797; AAN60355.1; -; mRNA.
EMBL; AF104919; AAC72872.1; -; Genomic_DNA.
EMBL; AL161492; CAB77732.1; -; Genomic_DNA.
EMBL; CP002687; AEE82052.1; -; Genomic_DNA.
EMBL; CP002687; AEE82053.1; -; Genomic_DNA.
EMBL; AF370193; AAK44008.1; -; mRNA.
EMBL; AY065167; AAL38343.1; -; mRNA.
EMBL; AY114015; AAM45063.1; -; mRNA.
EMBL; BT001190; AAN65077.1; -; mRNA.
EMBL; AK175280; BAD43043.1; -; mRNA.
EMBL; AK175481; BAD43244.1; -; mRNA.
EMBL; AK175539; BAD43302.1; -; mRNA.
EMBL; AK176165; BAD43928.1; -; mRNA.
EMBL; AK176244; BAD44007.1; -; mRNA.
EMBL; AK176281; BAD44044.1; -; mRNA.
EMBL; AK176330; BAD44093.1; -; mRNA.
EMBL; AK176416; BAD44179.1; -; mRNA.
EMBL; AK176433; BAD44196.1; -; mRNA.
EMBL; AK176487; BAD44250.1; -; mRNA.
EMBL; AK221398; BAD94342.1; -; mRNA.
EMBL; AK230235; BAF02040.1; -; mRNA.
EMBL; AY086034; AAM63244.1; -; mRNA.
PIR; T02011; T02011.
RefSeq; NP_567215.1; NM_116392.4. [Q94K85-1]
RefSeq; NP_849281.1; NM_178950.2. [Q94K85-2]
UniGene; At.24471; -.
ProteinModelPortal; Q94K85; -.
SMR; Q94K85; -.
STRING; 3702.AT4G01610.1; -.
MEROPS; C01.144; -.
PaxDb; Q94K85; -.
PRIDE; Q94K85; -.
EnsemblPlants; AT4G01610.1; AT4G01610.1; AT4G01610. [Q94K85-1]
EnsemblPlants; AT4G01610.2; AT4G01610.2; AT4G01610. [Q94K85-2]
GeneID; 826792; -.
Gramene; AT4G01610.1; AT4G01610.1; AT4G01610. [Q94K85-1]
Gramene; AT4G01610.2; AT4G01610.2; AT4G01610. [Q94K85-2]
KEGG; ath:AT4G01610; -.
Araport; AT4G01610; -.
TAIR; locus:2133402; AT4G01610.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
HOGENOM; HOG000241341; -.
InParanoid; Q94K85; -.
KO; K01363; -.
OMA; ADDINAC; -.
OrthoDB; EOG09360E2K; -.
PhylomeDB; Q94K85; -.
Reactome; R-ATH-2132295; MHC class II antigen presentation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q94K85; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q94K85; baseline and differential.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005764; C:lysosome; IBA:GO_Central.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:TAIR.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR012599; Propeptide_C1A.
PANTHER; PTHR12411; PTHR12411; 2.
Pfam; PF00112; Peptidase_C1; 1.
Pfam; PF08127; Propeptide_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Plant defense; Protease; Reference proteome; Signal;
Thiol protease; Vacuole.
SIGNAL 1 26 {ECO:0000269|PubMed:27058316}.
PROPEP 27 102 Activation peptide.
{ECO:0000269|PubMed:27058316}.
/FTId=PRO_0000439421.
CHAIN 102 342 Cathepsin B-like protease 3.
/FTId=PRO_0000439457.
PROPEP 343 359 {ECO:0000269|PubMed:27058316}.
/FTId=PRO_0000439422.
ACT_SITE 131 131 {ECO:0000255|PROSITE-ProRule:PRU10088}.
ACT_SITE 286 286 {ECO:0000255|PROSITE-ProRule:PRU10089}.
ACT_SITE 307 307 {ECO:0000250|UniProtKB:P07858}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 116 145 {ECO:0000250|UniProtKB:P07858}.
DISULFID 128 171 {ECO:0000250|UniProtKB:P07858}.
DISULFID 162 216 {ECO:0000250|UniProtKB:P07858}.
DISULFID 163 167 {ECO:0000250|UniProtKB:P07858}.
DISULFID 193 220 {ECO:0000250|UniProtKB:P07858}.
DISULFID 202 207 {ECO:0000250|UniProtKB:P07858}.
VAR_SEQ 124 125 DQ -> GL (in isoform 2).
/FTId=VSP_058851.
MUTAGEN 131 131 C->A: Loss of protease activity.
{ECO:0000269|PubMed:27058316}.
SEQUENCE 359 AA; 39418 MW; D3199ABA3FEA831E CRC64;
MAVYNTKLCL ASVFLLLGLL LAFDLKGIEA ESLTKQKLDS KILQDEIVKK VNENPNAGWK
AAINDRFSNA TVAEFKRLLG VKPTPKKHFL GVPIVSHDPS LKLPKAFDAR TAWPQCTSIG
NILDQGHCGS CWAFGAVESL SDRFCIQFGM NISLSVNDLL ACCGFRCGDG CDGGYPIAAW
QYFSYSGVVT EECDPYFDNT GCSHPGCEPA YPTPKCSRKC VSDNKLWSES KHYSVSTYTV
KSNPQDIMAE VYKNGPVEVS FTVYEDFAHY KSGVYKHITG SNIGGHAVKL IGWGTSSEGE
DYWLMANQWN RGWGDDGYFM IRRGTNECGI EDEPVAGLPS SKNVFRVDTG SNDLPVASV


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