ID   CEP3_ARATH              Reviewed;         364 AA.
AC   Q9STL5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=KDEL-tailed cysteine endopeptidase CEP3;
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:P80884};
DE   Flags: Precursor;
GN   Name=CEP3 {ECO:0000303|PubMed:21632425};
GN   OrderedLocusNames=At3g48350 {ECO:0000312|Araport:AT3G48350};
GN   ORFNames=T29H11.130 {ECO:0000312|EMBL:CAB41163.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
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).
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}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers, buds, green
CC       siliques, trichomes and near the stomata of cotyledons but not of true
CC       leaves. Found at the hypocotyl-root transition zone, in the vascular
CC       tissue, along primary and lateral roots, but not in root tips. Never
CC       found in the abscission zone of flower organs.
CC       {ECO:0000269|PubMed:21632425}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during silique development, but limited
CC       to the carpels and the pedicel. {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; CAB41163.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78406.1; -; Genomic_DNA.
DR   EMBL; AK119026; BAC43602.1; -; mRNA.
DR   PIR; T06707; T06707.
DR   RefSeq; NP_566901.1; NM_114696.4.
DR   AlphaFoldDB; Q9STL5; -.
DR   SMR; Q9STL5; -.
DR   BioGRID; 9312; 1.
DR   STRING; 3702.Q9STL5; -.
DR   MEROPS; C01.A02; -.
DR   GlyCosmos; Q9STL5; 1 site, No reported glycans.
DR   PaxDb; 3702-AT3G48350-1; -.
DR   ProteomicsDB; 223950; -.
DR   EnsemblPlants; AT3G48350.1; AT3G48350.1; AT3G48350.
DR   GeneID; 823993; -.
DR   Gramene; AT3G48350.1; AT3G48350.1; AT3G48350.
DR   KEGG; ath:AT3G48350; -.
DR   Araport; AT3G48350; -.
DR   TAIR; AT3G48350; CEP3.
DR   eggNOG; KOG1543; Eukaryota.
DR   HOGENOM; CLU_012184_1_0_1; -.
DR   InParanoid; Q9STL5; -.
DR   OMA; CDNEENQ; -.
DR   OrthoDB; 808912at2759; -.
DR   PhylomeDB; Q9STL5; -.
DR   PRO; PR:Q9STL5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9STL5; 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   GO; GO:0031667; P:response to nutrient levels; IMP:TAIR.
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:SF622; KDEL-TAILED CYSTEINE ENDOPEPTIDASE CEP3; 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.
DR   Genevisible; Q9STL5; AT.
PE   2: Evidence at transcript 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..125
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P00785"
FT                   /id="PRO_0000436323"
FT   CHAIN           126..364
FT                   /note="KDEL-tailed cysteine endopeptidase CEP3"
FT                   /id="PRO_0000403791"
FT   REGION          343..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           361..364
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        287
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        147..189
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        181..223
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
FT   DISULFID        281..333
FT                   /evidence="ECO:0000250|UniProtKB:P84346"
SQ   SEQUENCE   364 AA;  40971 MW;  81C725D07DCE2E78 CRC64;
     MKLFFIVLIS FLSLLQASKG FDFDEKELET EENVWKLYER WRGHHSVSRA SHEAIKRFNV
     FRHNVLHVHR TNKKNKPYKL KINRFADITH HEFRSSYAGS NVKHHRMLRG PKRGSGGFMY
     ENVTRVPSSV DWREKGAVTE VKNQQDCGSC WAFSTVAAVE GINKIRTNKL VSLSEQELVD
     CDTEENQGCA GGLMEPAFEF IKNNGGIKTE ETYPYDSSDV QFCRANSIGG ETVTIDGHEH
     VPENDEEELL KAVAHQPVSV AIDAGSSDFQ LYSEGVFIGE CGTQLNHGVV IVGYGETKNG
     TKYWIVRNSW GPEWGEGGYV RIERGISENE GRCGIAMEAS YPTKLSSTPS THESVVRDDV
     KDEL
//