CATB1_ARATH
ID CATB1_ARATH Reviewed; 379 AA.
AC F4HVZ1; O23681;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cathepsin B-like protease 1 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Cathepsin B1 {ECO:0000305};
DE Short=AtCathB1 {ECO:0000303|PubMed:19453434};
DE Flags: Precursor;
GN Name=CATHB1 {ECO:0000303|PubMed:19453434};
GN OrderedLocusNames=At1g02300 {ECO:0000312|Araport:AT1G02300};
GN ORFNames=T7I23.12 {ECO:0000312|EMBL:AAC24376.1};
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 [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 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 [4]
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 CATHB2 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 -!- INDUCTION: By dark-induced senescence. Down-regulated by infection with
CC an 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:PRU10089}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24376.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U89959; AAC24376.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27412.1; -; Genomic_DNA.
DR RefSeq; NP_563647.1; NM_100110.3.
DR AlphaFoldDB; F4HVZ1; -.
DR SMR; F4HVZ1; -.
DR STRING; 3702.AT1G02300.1; -.
DR iPTMnet; F4HVZ1; -.
DR PaxDb; F4HVZ1; -.
DR PRIDE; F4HVZ1; -.
DR ProteomicsDB; 223924; -.
DR EnsemblPlants; AT1G02300.1; AT1G02300.1; AT1G02300.
DR GeneID; 839576; -.
DR Gramene; AT1G02300.1; AT1G02300.1; AT1G02300.
DR KEGG; ath:AT1G02300; -.
DR Araport; AT1G02300; -.
DR TAIR; locus:2204873; AT1G02300.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_3_0_1; -.
DR InParanoid; F4HVZ1; -.
DR OMA; YPINAWK; -.
DR OrthoDB; 865289at2759; -.
DR PRO; PR:F4HVZ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HVZ1; 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: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; 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; 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.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..102
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439416"
FT CHAIN 103..362
FT /note="Cathepsin B-like protease 1"
FT /id="PRO_5009031914"
FT PROPEP 363..379
FT /evidence="ECO:0000305"
FT /id="PRO_0000439417"
FT ACT_SITE 151
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT ACT_SITE 306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 327
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 116..165
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 148..191
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 182..236
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 183..187
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 213..240
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 222..227
FT /evidence="ECO:0000250|UniProtKB:P07858"
SQ SEQUENCE 379 AA; 42263 MW; CD76CF08426CD949 CRC64;
MADSCCIRLH LLASVFLLLF SSFNLQGIAA ENLSKQKLTS LILQNEIVKE VNENPNAGWK
AAFNDRFANA TVAEFKRLLG VIQTPKTAYL GVPIVRHDLS LKLPKEFDAR TAWSHCTSIR
RILVGYILNN VLLWSTITLW FWFLLGHCGS CWAFGAVESL SDRFCIKYNL NVSLSANDVI
ACCGLLCGFG CNGGFPMGAW LYFKYHGVVT QECDPYFDNT GCSHPGCEPT YPTPKCERKC
VSRNQLWGES KHYGVGAYRI NPDPQDIMAE VYKNGPVEVA FTVYEDFAHY KSGVYKYITG
TKIGGHAVKL IGWGTSDDGE DYWLLANQWN RSWGDDGYFK IRRGTNECGI EQSVVAGLPS
EKNVFKGITT SDDLLVSSV
