CEP2_ARATH
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 03-AUG-2022, entry version 118.
DE RecName: Full=KDEL-tailed cysteine endopeptidase CEP2;
DE EC=3.4.22.-;
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.AT3G48340.1; -.
DR MEROPS; C01.A01; -.
DR MEROPS; I29.003; -.
DR PaxDb; Q9STL4; -.
DR PRIDE; Q9STL4; -.
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; locus:504955641; AT3G48340.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9STL4; -.
DR OMA; YHDNELE; -.
DR OrthoDB; 1275401at2759; -.
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: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; IBA:GO_Central.
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; 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:0000305"
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
