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KDEL-tailed cysteine endopeptidase CEP1 (EC 3.4.22.-) (Cysteine proteinase CP56) (AtCP56)

 CEP1_ARATH              Reviewed;         361 AA.
Q9FGR9;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-JUN-2017, entry version 105.
RecName: Full=KDEL-tailed cysteine endopeptidase CEP1;
EC=3.4.22.-;
AltName: Full=Cysteine proteinase CP56;
Short=AtCP56;
Flags: Precursor;
Name=CEP1 {ECO:0000303|PubMed:21632425};
Synonyms=CP56 {ECO:0000303|Ref.1};
OrderedLocusNames=At5g50260 {ECO:0000312|Araport:AT5G50260};
ORFNames=K6A12.12 {ECO:0000312|EMBL:BAB09397.1};
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].
Lv X., Li F., Lu H.;
"Function analysis of an Arabidopsis cysteine proteinase gene AtCP56
and the promoter ProCP56 in anther development.";
Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=21632425; DOI=10.3732/ajb.2007404;
Helm M., Schmid M., Hierl G., Terneus K., Tan L., Lottspeich F.,
Kieliszewski M.J., Gietl C.;
"KDEL-tailed cysteine endopeptidases involved in programmed cell
death, intercalation of new cells, and dismantling of extensin
scaffolds.";
Am. J. Bot. 95:1049-1062(2008).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=24605116; DOI=10.3389/fpls.2014.00058;
Hoewing T., Huesmann C., Hoefle C., Nagel M.K., Isono E.,
Hueckelhoven R., Gietl C.;
"Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of
Arabidopsis (AtCEP1) is involved in pathogen defense.";
Front. Plant Sci. 5:58-58(2014).
[7]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION,
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=25035401; DOI=10.1105/tpc.114.127282;
Zhang D., Liu D., Lv X., Wang Y., Xun Z., Liu Z., Li F., Lu H.;
"The cysteine protease CEP1, a key executor involved in tapetal
programmed cell death, regulates pollen development in Arabidopsis.";
Plant Cell 26:2939-2961(2014).
-!- FUNCTION: Possesses protease activity in vitro (PubMed:25035401).
Involved in the final stage of developmental programmed cell death
and in intercalation of new cells. Cleaves extensins, thus
probably supporting the final cell collapse (PubMed:21632425).
During the compatible interaction with the biotrophic powdery
mildew fungus Erysiphe cruciferarum, involved in the control of
late epidermal cell death that limits growth and susceptibility to
the parasite (PubMed:24605116). During anther development,
involved in tapetal programmed cell death (PCD), leading to
degeneration of tapetal cells and functional pollen formation
(PubMed:25035401). {ECO:0000269|PubMed:21632425,
ECO:0000269|PubMed:24605116, ECO:0000269|PubMed:25035401}.
-!- ENZYME REGULATION: Inhibited by leupeptin and the cysteine
protease inhibitor E-64. {ECO:0000269|PubMed:25035401}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13.92 uM for Z-Phe-Arg-NHMec {ECO:0000269|PubMed:25035401};
KM=159.62 uM for Z-Arg-NHMec {ECO:0000269|PubMed:25035401};
Vmax=235.14 pmol/sec/mg enzyme toward Z-Phe-Arg-NHMec
{ECO:0000269|PubMed:25035401};
Vmax=537.93 pmol/sec/mg enzyme toward Z-Arg-NHMec
{ECO:0000269|PubMed:25035401};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
ProRule:PRU10138, ECO:0000269|PubMed:24605116}. Vacuole
{ECO:0000269|PubMed:25035401}. Note=During anther development,
detected as a proenzyme in precursor protease vesicles in tapetum
cells and then transported to the vacuole and transformed into the
mature enzyme before rupture of the vacuole.
{ECO:0000269|PubMed:25035401}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers, buds and
green siliques. Found within columella, lateral root cap cells,
and in the endodermis, the cortex and the epidermis during lateral
root formation. Expressed in the abscission zones of the flower
organs. {ECO:0000269|PubMed:21632425}.
-!- DEVELOPMENTAL STAGE: Expressed when organs wither and separate
from the fruit or the green silique. Expressed in unpollinated,
degrading ovules (PubMed:21632425). Expressed specifically in the
tapetum from stages 5 to 11 of anther development
(PubMed:25035401). {ECO:0000269|PubMed:21632425,
ECO:0000269|PubMed:25035401}.
-!- DISRUPTION PHENOTYPE: Reduced male fertility due to impaired
pollen development and abnormal pollen exine (PubMed:25035401).
Enhanced susceptibility to powdery mildew caused by the biotrophic
ascomycete Erysiphe cruciferarum (PubMed:24605116).
{ECO:0000269|PubMed:24605116, ECO:0000269|PubMed:25035401}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-----------------------------------------------------------------------
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EMBL; HM367092; ADO14465.1; -; mRNA.
EMBL; AB024031; BAB09397.1; -; Genomic_DNA.
EMBL; CP002688; AED95919.1; -; Genomic_DNA.
EMBL; AY091087; AAM13907.1; -; mRNA.
RefSeq; NP_568722.1; NM_124405.3.
UniGene; At.7918; -.
ProteinModelPortal; Q9FGR9; -.
SMR; Q9FGR9; -.
STRING; 3702.AT5G50260.1; -.
MEROPS; I29.003; -.
iPTMnet; Q9FGR9; -.
PaxDb; Q9FGR9; -.
EnsemblPlants; AT5G50260.1; AT5G50260.1; AT5G50260.
GeneID; 835091; -.
Gramene; AT5G50260.1; AT5G50260.1; AT5G50260.
KEGG; ath:AT5G50260; -.
Araport; AT5G50260; -.
TAIR; locus:2157712; AT5G50260.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
HOGENOM; HOG000230773; -.
InParanoid; Q9FGR9; -.
KO; K16292; -.
OMA; FRYIKDN; -.
OrthoDB; EOG09360FGY; -.
PhylomeDB; Q9FGR9; -.
Reactome; R-ATH-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-ATH-2132295; MHC class II antigen presentation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q9FGR9; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9FGR9; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005764; C:lysosome; IBA:GO_Central.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:TAIR.
GO; GO:0048658; P:anther wall tapetum development; IMP:TAIR.
GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
GO; GO:0009555; P:pollen development; IMP:TAIR.
GO; GO:0010623; P:programmed cell death involved in cell development; IMP:TAIR.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Endoplasmic reticulum; Hydrolase;
Plant defense; Protease; Reference proteome; Signal; Thiol protease;
Vacuole; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 125 Activation peptide. {ECO:0000305}.
/FTId=PRO_0000436321.
CHAIN 126 361 KDEL-tailed cysteine endopeptidase CEP1.
/FTId=PRO_0000403789.
MOTIF 358 361 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
ACT_SITE 150 150 {ECO:0000255|PROSITE-ProRule:PRU10088}.
ACT_SITE 286 286 {ECO:0000255|PROSITE-ProRule:PRU10089}.
ACT_SITE 307 307 {ECO:0000255|PROSITE-ProRule:PRU10090}.
DISULFID 147 189 {ECO:0000250|UniProtKB:P84346}.
DISULFID 181 222 {ECO:0000250|UniProtKB:P84346}.
DISULFID 280 332 {ECO:0000250|UniProtKB:P84346}.
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


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