CEP3_ARATH
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 03-AUG-2022, entry version 122.
DE RecName: Full=KDEL-tailed cysteine endopeptidase CEP3;
DE EC=3.4.22.-;
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.AT3G48350.1; -.
DR MEROPS; C01.A02; -.
DR PaxDb; Q9STL5; -.
DR PRIDE; Q9STL5; -.
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; locus:505006391; AT3G48350.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9STL5; -.
DR OMA; IGECGTQ; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9STL5; -.
DR PRO; PR:Q9STL5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STL5; baseline and differential.
DR Genevisible; Q9STL5; AT.
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 GO; GO:0031667; P:response to nutrient levels; IMP:TAIR.
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 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:0000305"
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
