CATB3_ARATH
ID CATB3_ARATH Reviewed; 359 AA.
AC Q94K85; Q9ZSI0;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cathepsin B-like protease 3 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Cathepsin B3 {ECO:0000305};
DE Short=AtCathB3 {ECO:0000303|PubMed:19453434};
DE Flags: Precursor;
GN Name=CATHB3 {ECO:0000303|PubMed:19453434};
GN OrderedLocusNames=At4g01610 {ECO:0000312|Araport:AT4G01610};
GN ORFNames=T15B16.17a {ECO:0000312|EMBL:AAC72872.1};
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 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=15539469; DOI=10.1105/tpc.104.027078;
RA Carter C., Pan S., Zouhar J., Avila E.L., Girke T., Raikhel N.V.;
RT "The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted
RT and unexpected proteins.";
RL Plant Cell 16:3285-3303(2004).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=19453434; DOI=10.1111/j.1469-8137.2009.02865.x;
RA McLellan H., Gilroy E.M., Yun B.W., Birch P.R., Loake G.J.;
RT "Functional redundancy in the Arabidopsis cathepsin B gene family
RT contributes to basal defence, the hypersensitive response and senescence.";
RL New Phytol. 183:408-418(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24600022; DOI=10.1093/jxb/eru055;
RA Iglesias-Fernandez R., Wozny D., Iriondo-de Hond M., Onate-Sanchez L.,
RA Carbonero P., Barrero-Sicilia C.;
RT "The AtCathB3 gene, encoding a cathepsin B-like protease, is expressed
RT during germination of Arabidopsis thaliana and transcriptionally repressed
RT by the basic leucine zipper protein GBF1.";
RL J. Exp. Bot. 65:2009-2021(2014).
RN [9]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, CLEAVAGE OF SIGNAL PEPTIDE AFTER LYS-26,
RP CLEAVAGE OF ACTIVATION PROPEPTIDE AFTER LYS-102, CLEAVAGE OF C-TERMINUS
RP PROPEPTIDE AFTER LYS-342, AND MUTAGENESIS OF CYS-131.
RX PubMed=27058316; DOI=10.1038/cdd.2016.34;
RA Ge Y., Cai Y.M., Bonneau L., Rotari V., Danon A., McKenzie E.A.,
RA McLellan H., Mach L., Gallois P.;
RT "Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed cell
RT death in Arabidopsis.";
RL Cell Death Differ. 23:1493-1501(2016).
CC -!- FUNCTION: Thiol protease that possesses high activity toward the
CC cathepsin synthetic substrate Arg-Arg-7-amino-4-methylcoumarin (RR-AMC)
CC and the papain substrate Gly-Arg-Arg-AMC (GRR-AMC). Can cleave the
CC papain substrate Phe-Arg-AMC (FR-AMC) and the caspase-3 substrate Asp-
CC Glu-Val-Asp-rhodamine 110 (DEVD-R110). Has no activity towards the
CC caspase-6 substrate VEID-AMC, caspase-8 substrate IETD-AMC and caspase-
CC 1 substrate YVAD-AMC (PubMed:27058316). Plays a central role in plant
CC programmed cell death (PCD). In addition to its role in protein
CC degradation, may cleave and/or degrade a number of target proteins,
CC activating signaling towards PCD. Contributes to the increase of
CC caspase-3-like activity after UV-C-induced PCD and is required for
CC abiotic stress-induced PCD (PubMed:27058316). Functions redundantly
CC with CATHB1 and CATHB2 in basal defense and distinct forms of plant
CC programmed cell death (PCD). Participates in the establishment of basal
CC resistance against the bacterial pathogen Pseudomonase syringae pv.
CC tomato DC3000. Required for full levels of PCD during resistance (R)
CC gene-mediated hypersensitive response (HR). Involved in the regulation
CC of senescence, a developmental form of PCD in plants (PubMed:19453434).
CC May be involved in the degradation of seed storage proteins during seed
CC germination (PubMed:24600022). {ECO:0000269|PubMed:19453434,
CC ECO:0000269|PubMed:24600022, ECO:0000269|PubMed:27058316}.
CC -!- ACTIVITY REGULATION: Inhibited by the cathepsin B inhibitors Ac-LVK-
CC CHO, CA-074 and Z-FA-FMK, and the caspase-3 inhibitor Z-DEVD-CHO.
CC {ECO:0000269|PubMed:27058316}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:27058316};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:15539469}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94K85-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94K85-2; Sequence=VSP_058851;
CC -!- TISSUE SPECIFICITY: Expressed in root tips, root vasculature, emerging
CC lateral root, hydathodes, vascular tissue of leaves, vasculature of
CC sepals and anthers, stigma, and vascular bundles at the base and the
CC upper part of the siliques. {ECO:0000269|PubMed:24600022}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing siliques 13 to 15 days
CC after pollination (DAP). In germinating seeds, expressed from 12 to 48
CC hours after imbibition with a peak of expression at 24 hours.
CC {ECO:0000269|PubMed:24600022}.
CC -!- INDUCTION: By dark-induced senescence. Induced by infection with an
CC avirulent strain of the bacterial pathogen Pseudomonase syringae pv.
CC tomato DC3000. {ECO:0000269|PubMed:19453434}.
CC -!- DISRUPTION PHENOTYPE: Delayed germination and decreased germination
CC rate. {ECO:0000269|PubMed:24600022}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR EMBL; AF083797; AAN60355.1; -; mRNA.
DR EMBL; AF104919; AAC72872.1; -; Genomic_DNA.
DR EMBL; AL161492; CAB77732.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82052.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82053.1; -; Genomic_DNA.
DR EMBL; AF370193; AAK44008.1; -; mRNA.
DR EMBL; AY065167; AAL38343.1; -; mRNA.
DR EMBL; AY114015; AAM45063.1; -; mRNA.
DR EMBL; BT001190; AAN65077.1; -; mRNA.
DR EMBL; AK175280; BAD43043.1; -; mRNA.
DR EMBL; AK175481; BAD43244.1; -; mRNA.
DR EMBL; AK175539; BAD43302.1; -; mRNA.
DR EMBL; AK176165; BAD43928.1; -; mRNA.
DR EMBL; AK176244; BAD44007.1; -; mRNA.
DR EMBL; AK176281; BAD44044.1; -; mRNA.
DR EMBL; AK176330; BAD44093.1; -; mRNA.
DR EMBL; AK176416; BAD44179.1; -; mRNA.
DR EMBL; AK176433; BAD44196.1; -; mRNA.
DR EMBL; AK176487; BAD44250.1; -; mRNA.
DR EMBL; AK221398; BAD94342.1; -; mRNA.
DR EMBL; AK230235; BAF02040.1; -; mRNA.
DR EMBL; AY086034; AAM63244.1; -; mRNA.
DR PIR; T02011; T02011.
DR RefSeq; NP_567215.1; NM_116392.4. [Q94K85-1]
DR RefSeq; NP_849281.1; NM_178950.2. [Q94K85-2]
DR AlphaFoldDB; Q94K85; -.
DR SMR; Q94K85; -.
DR STRING; 3702.AT4G01610.1; -.
DR MEROPS; C01.144; -.
DR PaxDb; Q94K85; -.
DR PRIDE; Q94K85; -.
DR ProteomicsDB; 223912; -. [Q94K85-1]
DR EnsemblPlants; AT4G01610.1; AT4G01610.1; AT4G01610. [Q94K85-1]
DR EnsemblPlants; AT4G01610.2; AT4G01610.2; AT4G01610. [Q94K85-2]
DR GeneID; 826792; -.
DR Gramene; AT4G01610.1; AT4G01610.1; AT4G01610. [Q94K85-1]
DR Gramene; AT4G01610.2; AT4G01610.2; AT4G01610. [Q94K85-2]
DR KEGG; ath:AT4G01610; -.
DR Araport; AT4G01610; -.
DR TAIR; locus:2133402; AT4G01610.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_3_0_1; -.
DR InParanoid; Q94K85; -.
DR OMA; VHNIEGI; -.
DR OrthoDB; 865289at2759; -.
DR PhylomeDB; Q94K85; -.
DR BRENDA; 3.4.22.B6; 399.
DR PRO; PR:Q94K85; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94K85; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR012599; Propeptide_C1A.
DR Pfam; PF00112; Peptidase_C1; 1.
DR Pfam; PF08127; Propeptide_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW Plant defense; Protease; Reference proteome; Signal; Thiol protease;
KW Vacuole.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:27058316"
FT PROPEP 27..102
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:27058316"
FT /id="PRO_0000439421"
FT CHAIN 102..342
FT /note="Cathepsin B-like protease 3"
FT /id="PRO_0000439457"
FT PROPEP 343..359
FT /evidence="ECO:0000269|PubMed:27058316"
FT /id="PRO_0000439422"
FT ACT_SITE 131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 307
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 116..145
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 128..171
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 162..216
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 163..167
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 193..220
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 202..207
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT VAR_SEQ 124..125
FT /note="DQ -> GL (in isoform 2)"
FT /id="VSP_058851"
FT MUTAGEN 131
FT /note="C->A: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:27058316"
SQ 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
