ID   CEP2_ARATH              Reviewed;         361 AA.
AC   Q9STL4;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=KDEL-tailed cysteine endopeptidase CEP2;
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:P80884};
DE   Flags: Precursor;
GN   Name=CEP2 {ECO:0000303|PubMed:21632425};
GN   OrderedLocusNames=At3g48340 {ECO:0000312|Araport:AT3G48340};
GN   ORFNames=T29H11.140 {ECO:0000312|EMBL:CAB41164.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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 TISSUE SPECIFICITY.
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=24287716; DOI=10.1007/s11103-013-0157-6;
RA   Hierl G., Hoewing T., Isono E., Lottspeich F., Gietl C.;
RT   "Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine
RT   endopeptidase 2 (AtCEP2) pro-enzyme and its storage in endoplasmic
RT   reticulum derived organelles.";
RL   Plant Mol. Biol. 84:605-620(2014).
CC   -!- FUNCTION: Involved in the final stage of developmental programmed cell
CC       death and in intercalation of new cells. Cleaves extensins, thus
CC       probably supporting the final cell collapse.
CC       {ECO:0000269|PubMed:21632425}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC       ProRule:PRU10138, ECO:0000269|PubMed:24287716}. Note=Detected in ER
CC       bodies and another type of ER-derived vesicles.
CC       {ECO:0000269|PubMed:24287716}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, rosette and cauline
CC       leaves, flowers, buds and green siliques. Found in the tip of young
CC       primary leaves, in very young root tips and at later stages in all
CC       tissues of lateral root, including the vascular bundle. Not expressed
CC       in lateral root primordia, while directly emerging through the
CC       epidermis. {ECO:0000269|PubMed:21632425}.
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; AL049659; CAB41164.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78403.1; -; Genomic_DNA.
DR   PIR; T06708; T06708.
DR   RefSeq; NP_680113.3; NM_148860.5.
DR   AlphaFoldDB; Q9STL4; -.
DR   SMR; Q9STL4; -.
DR   BioGRID; 9311; 1.
DR   IntAct; Q9STL4; 1.
DR   STRING; 3702.Q9STL4; -.
DR   MEROPS; C01.A01; -.
DR   MEROPS; I29.003; -.
DR   GlyCosmos; Q9STL4; 2 sites, No reported glycans.
DR   PaxDb; 3702-AT3G48340-1; -.
DR   ProteomicsDB; 223980; -.
DR   EnsemblPlants; AT3G48340.1; AT3G48340.1; AT3G48340.
DR   GeneID; 823992; -.
DR   Gramene; AT3G48340.1; AT3G48340.1; AT3G48340.
DR   KEGG; ath:AT3G48340; -.
DR   Araport; AT3G48340; -.
DR   TAIR; AT3G48340; CEP2.
DR   eggNOG; KOG1543; Eukaryota.
DR   HOGENOM; CLU_012184_1_0_1; -.
DR   InParanoid; Q9STL4; -.
DR   OMA; GKCDASK; -.
DR   OrthoDB; 5472443at2759; -.
DR   PhylomeDB; Q9STL4; -.
DR   PRO; PR:Q9STL4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9STL4; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF901; KDEL-TAILED CYSTEINE ENDOPEPTIDASE CEP2; 1.
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; Cysteine proteinases; 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; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..127
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P00785"
FT                   /id="PRO_0000436322"
FT   CHAIN           128..361
FT                   /note="KDEL-tailed cysteine endopeptidase CEP2"
FT                   /id="PRO_0000403790"
FT   MOTIF           358..361
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        149..191
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        183..224
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        282..333
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
SQ   SEQUENCE   361 AA;  40371 MW;  FEF1381FFE780C6E CRC64;
     MKKLLLIFLF SLVILQTACG FDYDDKEIES EEGLSTLYDR WRSHHSVPRS LNEREKRFNV
     FRHNVMHVHN TNKKNRSYKL KLNKFADLTI NEFKNAYTGS NIKHHRMLQG PKRGSKQFMY
     DHENLSKLPS SVDWRKKGAV TEIKNQGKCG SCWAFSTVAA VEGINKIKTN KLVSLSEQEL
     VDCDTKQNEG CNGGLMEIAF EFIKKNGGIT TEDSYPYEGI DGKCDASKDN GVLVTIDGHE
     DVPENDENAL LKAVANQPVS VAIDAGSSDF QFYSEGVFTG SCGTELNHGV AAVGYGSERG
     KKYWIVRNSW GAEWGEGGYI KIEREIDEPE GRCGIAMEAS YPIKLSSSNP TPKDGDVKDE
     L
//