CATB2_ARATH
ID CATB2_ARATH Reviewed; 362 AA.
AC Q93VC9; B9DHV8;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cathepsin B-like protease 2 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Cathepsin B2 {ECO:0000305};
DE Short=AtCathB2 {ECO:0000303|PubMed:19453434};
DE Flags: Precursor;
GN Name=CATHB2 {ECO:0000303|PubMed:19453434};
GN OrderedLocusNames=At1g02305 {ECO:0000312|Araport:AT1G02305};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-362.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 [6]
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 [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [8]
RP FUNCTION.
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 plays a central role in plant programmed
CC cell death (PCD). In addition to its role in protein degradation, may
CC cleave and/or degrade a number of target proteins, activating signaling
CC towards PCD. Contributes to the increase of caspase-3-like activity
CC after UV-C-induced PCD and is required for abiotic stress-induced PCD
CC (PubMed:27058316). Functions redundantly with CATHB1 and CATHB3 in
CC basal defense and distinct forms of plant programmed cell death (PCD).
CC Participates in the establishment of basal resistance against the
CC bacterial pathogen Pseudomonase syringae pv. tomato DC3000. Required
CC for full levels of PCD during resistance (R) gene-mediated
CC hypersensitive response (HR). Involved in the regulation of senescence,
CC a developmental form of PCD in plants (PubMed:19453434).
CC {ECO:0000269|PubMed:19453434, ECO:0000269|PubMed:27058316}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:15539469}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:24600022}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing siliques 13 to 15 days
CC after pollination (DAP). {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 -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR EMBL; AC064879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE27413.1; -; Genomic_DNA.
DR EMBL; AF428337; AAL16267.1; -; mRNA.
DR EMBL; AY039887; AAK63991.1; -; mRNA.
DR EMBL; BT002227; AAN72238.1; -; mRNA.
DR EMBL; AK317665; BAH20325.1; -; mRNA.
DR RefSeq; NP_563648.1; NM_100111.3.
DR AlphaFoldDB; Q93VC9; -.
DR SMR; Q93VC9; -.
DR IntAct; Q93VC9; 1.
DR STRING; 3702.AT1G02305.1; -.
DR MEROPS; C01.049; -.
DR PaxDb; Q93VC9; -.
DR PRIDE; Q93VC9; -.
DR ProMEX; Q93VC9; -.
DR ProteomicsDB; 240285; -.
DR EnsemblPlants; AT1G02305.1; AT1G02305.1; AT1G02305.
DR GeneID; 839538; -.
DR Gramene; AT1G02305.1; AT1G02305.1; AT1G02305.
DR KEGG; ath:AT1G02305; -.
DR Araport; AT1G02305; -.
DR TAIR; locus:505006093; AT1G02305.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_3_0_1; -.
DR InParanoid; Q93VC9; -.
DR OMA; DEKIPYW; -.
DR OrthoDB; 865289at2759; -.
DR PhylomeDB; Q93VC9; -.
DR BRENDA; 3.4.22.B6; 399.
DR PRO; PR:Q93VC9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93VC9; baseline and differential.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
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: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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Plant defense; Protease;
KW Reference proteome; Signal; Thiol protease; Vacuole.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..105
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439418"
FT CHAIN 106..345
FT /note="Cathepsin B-like protease 2"
FT /id="PRO_0000439419"
FT PROPEP 346..362
FT /evidence="ECO:0000305"
FT /id="PRO_0000439420"
FT ACT_SITE 134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 310
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 119..148
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 131..174
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 165..219
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 166..170
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 196..223
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 205..210
FT /evidence="ECO:0000250|UniProtKB:P07858"
SQ SEQUENCE 362 AA; 40033 MW; CDCB7D1AA33A0D6E CRC64;
MADNCIRLLH SASVFFCLGL LISSFNLLQG IAAENLSKQK LTSWILQNEI VKEVNENPNA
GWKASFNDRF ANATVAEFKR LLGVKPTPKT EFLGVPIVSH DISLKLPKEF DARTAWSQCT
SIGRILDQGH CGSCWAFGAV ESLSDRFCIK YNMNVSLSVN DLLACCGFLC GQGCNGGYPI
AAWRYFKHHG VVTEECDPYF DNTGCSHPGC EPAYPTPKCA RKCVSGNQLW RESKHYGVSA
YKVRSHPDDI MAEVYKNGPV EVAFTVYEDF AHYKSGVYKH ITGTNIGGHA VKLIGWGTSD
DGEDYWLLAN QWNRSWGDDG YFKIRRGTNE CGIEHGVVAG LPSDRNVVKG ITTSDDLLVS
SF
