CEP1_ARATH
ID CEP1_ARATH Reviewed; 361 AA.
AC Q9FGR9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=KDEL-tailed cysteine endopeptidase CEP1;
DE EC=3.4.22.-;
DE AltName: Full=Cysteine proteinase CP56;
DE Short=AtCP56;
DE Flags: Precursor;
GN Name=CEP1 {ECO:0000303|PubMed:21632425}; Synonyms=CP56 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At5g50260 {ECO:0000312|Araport:AT5G50260};
GN ORFNames=K6A12.12 {ECO:0000312|EMBL:BAB09397.1};
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].
RA Lv X., Li F., Lu H.;
RT "Function analysis of an Arabidopsis cysteine proteinase gene AtCP56 and
RT the promoter ProCP56 in anther development.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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].
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 FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21632425; DOI=10.3732/ajb.2007404;
RA Helm M., Schmid M., Hierl G., Terneus K., Tan L., Lottspeich F.,
RA Kieliszewski M.J., Gietl C.;
RT "KDEL-tailed cysteine endopeptidases involved in programmed cell death,
RT intercalation of new cells, and dismantling of extensin scaffolds.";
RL Am. J. Bot. 95:1049-1062(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24605116; DOI=10.3389/fpls.2014.00058;
RA Hoewing T., Huesmann C., Hoefle C., Nagel M.K., Isono E., Hueckelhoven R.,
RA Gietl C.;
RT "Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis
RT (AtCEP1) is involved in pathogen defense.";
RL Front. Plant Sci. 5:58-58(2014).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=25035401; DOI=10.1105/tpc.114.127282;
RA Zhang D., Liu D., Lv X., Wang Y., Xun Z., Liu Z., Li F., Lu H.;
RT "The cysteine protease CEP1, a key executor involved in tapetal programmed
RT cell death, regulates pollen development in Arabidopsis.";
RL Plant Cell 26:2939-2961(2014).
CC -!- FUNCTION: Possesses protease activity in vitro (PubMed:25035401).
CC Involved in the final stage of developmental programmed cell death and
CC in intercalation of new cells. Cleaves extensins, thus probably
CC supporting the final cell collapse (PubMed:21632425). During the
CC compatible interaction with the biotrophic powdery mildew fungus
CC Erysiphe cruciferarum, involved in the control of late epidermal cell
CC death that limits growth and susceptibility to the parasite
CC (PubMed:24605116). During anther development, involved in tapetal
CC programmed cell death (PCD), leading to degeneration of tapetal cells
CC and functional pollen formation (PubMed:25035401).
CC {ECO:0000269|PubMed:21632425, ECO:0000269|PubMed:24605116,
CC ECO:0000269|PubMed:25035401}.
CC -!- ACTIVITY REGULATION: Inhibited by leupeptin and the cysteine protease
CC inhibitor E-64. {ECO:0000269|PubMed:25035401}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.92 uM for Z-Phe-Arg-NHMec {ECO:0000269|PubMed:25035401};
CC KM=159.62 uM for Z-Arg-NHMec {ECO:0000269|PubMed:25035401};
CC Vmax=235.14 pmol/sec/mg enzyme toward Z-Phe-Arg-NHMec
CC {ECO:0000269|PubMed:25035401};
CC Vmax=537.93 pmol/sec/mg enzyme toward Z-Arg-NHMec
CC {ECO:0000269|PubMed:25035401};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:24605116}. Vacuole
CC {ECO:0000269|PubMed:25035401}. Note=During anther development, detected
CC as a proenzyme in precursor protease vesicles in tapetum cells and then
CC transported to the vacuole and transformed into the mature enzyme
CC before rupture of the vacuole. {ECO:0000269|PubMed:25035401}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers, buds and green
CC siliques. Found within columella, lateral root cap cells, and in the
CC endodermis, the cortex and the epidermis during lateral root formation.
CC Expressed in the abscission zones of the flower organs.
CC {ECO:0000269|PubMed:21632425}.
CC -!- DEVELOPMENTAL STAGE: Expressed when organs wither and separate from the
CC fruit or the green silique. Expressed in unpollinated, degrading ovules
CC (PubMed:21632425). Expressed specifically in the tapetum from stages 5
CC to 11 of anther development (PubMed:25035401).
CC {ECO:0000269|PubMed:21632425, ECO:0000269|PubMed:25035401}.
CC -!- DISRUPTION PHENOTYPE: Reduced male fertility due to impaired pollen
CC development and abnormal pollen exine (PubMed:25035401). Enhanced
CC susceptibility to powdery mildew caused by the biotrophic ascomycete
CC Erysiphe cruciferarum (PubMed:24605116). {ECO:0000269|PubMed:24605116,
CC ECO:0000269|PubMed:25035401}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; HM367092; ADO14465.1; -; mRNA.
DR EMBL; AB024031; BAB09397.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95919.1; -; Genomic_DNA.
DR EMBL; AY091087; AAM13907.1; -; mRNA.
DR RefSeq; NP_568722.1; NM_124405.3.
DR AlphaFoldDB; Q9FGR9; -.
DR SMR; Q9FGR9; -.
DR STRING; 3702.AT5G50260.1; -.
DR MEROPS; C01.A03; -.
DR MEROPS; I29.003; -.
DR iPTMnet; Q9FGR9; -.
DR PaxDb; Q9FGR9; -.
DR PRIDE; Q9FGR9; -.
DR ProteomicsDB; 220472; -.
DR EnsemblPlants; AT5G50260.1; AT5G50260.1; AT5G50260.
DR GeneID; 835091; -.
DR Gramene; AT5G50260.1; AT5G50260.1; AT5G50260.
DR KEGG; ath:AT5G50260; -.
DR Araport; AT5G50260; -.
DR TAIR; locus:2157712; AT5G50260.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9FGR9; -.
DR OMA; HEFTSHY; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9FGR9; -.
DR SABIO-RK; Q9FGR9; -.
DR PRO; PR:Q9FGR9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGR9; baseline and differential.
DR Genevisible; Q9FGR9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0048658; P:anther wall tapetum development; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IGI:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:TAIR.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Hydrolase; Plant defense; Protease;
KW Reference proteome; Signal; Thiol protease; Vacuole; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..125
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436321"
FT CHAIN 126..361
FT /note="KDEL-tailed cysteine endopeptidase CEP1"
FT /id="PRO_0000403789"
FT MOTIF 358..361
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 150
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:0000255|PROSITE-ProRule:PRU10090"
FT DISULFID 147..189
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 181..222
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 280..332
FT /evidence="ECO:0000250|UniProtKB:P84346"
SQ SEQUENCE 361 AA; 40708 MW; A622234BC3E7367A CRC64;
MKRFIVLALC MLMVLETTKG LDFHNKDVES ENSLWELYER WRSHHTVARS LEEKAKRFNV
FKHNVKHIHE TNKKDKSYKL KLNKFGDMTS EEFRRTYAGS NIKHHRMFQG EKKATKSFMY
ANVNTLPTSV DWRKNGAVTP VKNQGQCGSC WAFSTVVAVE GINQIRTKKL TSLSEQELVD
CDTNQNQGCN GGLMDLAFEF IKEKGGLTSE LVYPYKASDE TCDTNKENAP VVSIDGHEDV
PKNSEDDLMK AVANQPVSVA IDAGGSDFQF YSEGVFTGRC GTELNHGVAV VGYGTTIDGT
KYWIVKNSWG EEWGEKGYIR MQRGIRHKEG LCGIAMEASY PLKNSNTNPS RLSLDSLKDE
L
