ID CYSEP_RICCO Reviewed; 360 AA. AC O65039; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=Vignain; DE EC=3.4.22.- {ECO:0000250|UniProtKB:P80884}; DE AltName: Full=Cysteine endopeptidase; DE Flags: Precursor; GN Name=CYSEP; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae; OC Ricinus. OX NCBI_TaxID=3988; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Endosperm; RX PubMed=9763713; DOI=10.1007/s004250050423; RA Schmid M., Simpson D., Kalousek F., Gietl C.; RT "A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor RT bean endosperm is a marker enzyme for the ricinosome, a putative lytic RT compartment."; RL Planta 206:466-475(1998). RN [2] RP PROTEIN SEQUENCE OF 337-360, PROTEOLYTIC PROCESSING, AND SUBCELLULAR RP LOCATION. RX PubMed=11296243; DOI=10.1073/pnas.061038298; RA Schmid M., Simpson D.J., Sarioglu H., Lottspeich F., Gietl C.; RT "The ricinosomes of senescing plant tissue bud from the endoplasmic RT reticulum."; RL Proc. Natl. Acad. Sci. U.S.A. 98:5353-5358(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 125-350 IN COMPLEX WITH RP CHLOROMETHYLKETONE (CMK) INHIBITOR, AND DISULFIDE BONDS. RX PubMed=15037072; DOI=10.1016/j.jmb.2003.12.075; RA Than M.E., Helm M., Simpson D.J., Lottspeich F., Huber R., Gietl C.; RT "The 2.0 A crystal structure and substrate specificity of the KDEL-tailed RT cysteine endopeptidase functioning in programmed cell death of Ricinus RT communis endosperm."; RL J. Mol. Biol. 336:1103-1116(2004). CC -!- FUNCTION: Involved in programmed cell death. Shows a pronounced CC preference for hydrophobic residues in the P2 position and no obvious CC preference in the P1 position of the cleavage site. Accepts proline at CC the P1 and P1' positions. CC -!- ACTIVITY REGULATION: Low pH triggers activation of the protease and CC removal of the propeptide and the KDEL motif. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle CC {ECO:0000269|PubMed:11296243}. Note=The pro-endopeptidase accumulates CC in the ricinosomes. CC -!- DEVELOPMENTAL STAGE: Released during the final stage of cellular CC desintegration in the senescing endosperm of germinating bean. CC -!- PTM: The potential N-glycosylation site at Asn-115 is not glycosylated. CC -!- MISCELLANEOUS: The pro-endopeptidase goes directly from the ER lumen to CC the ricinosome, and the secretory pathway via the Golgi apparatus is CC not involved in the ricinosome biogenesis. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF050756; AAC62396.1; -; mRNA. DR PIR; T08122; T08122. DR RefSeq; NP_001310675.1; NM_001323746.1. DR PDB; 1S4V; X-ray; 2.00 A; A/B=125-353. DR PDBsum; 1S4V; -. DR AlphaFoldDB; O65039; -. DR SMR; O65039; -. DR MEROPS; C01.010; -. DR GeneID; 8278243; -. DR KEGG; rcu:8278243; -. DR eggNOG; KOG1543; Eukaryota. DR OrthoDB; 5472443at2759; -. DR BRENDA; 3.4.22.B1; 1204. DR EvolutionaryTrace; O65039; -. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. 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:SF1001; KDEL-TAILED CYSTEINE ENDOPEPTIDASE CEP1; 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 3D-structure; Cytoplasmic vesicle; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease. FT SIGNAL 1..20 FT PROPEP 21..124 FT /note="Activation peptide" FT /evidence="ECO:0000250|UniProtKB:P00785" FT /id="PRO_0000026442" FT CHAIN 125..353 FT /note="Vignain" FT /id="PRO_0000026443" FT PROPEP 354..360 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:V5LU01" FT /id="PRO_0000026444" FT REGION 341..360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..360 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000250" FT ACT_SITE 150 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088" FT ACT_SITE 286 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089" FT ACT_SITE 307 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090" FT CARBOHYD 115 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 147..189 FT /evidence="ECO:0000269|PubMed:15037072, FT ECO:0007744|PDB:1S4V" FT DISULFID 181..222 FT /evidence="ECO:0000269|PubMed:15037072, FT ECO:0007744|PDB:1S4V" FT DISULFID 280..332 FT /evidence="ECO:0000269|PubMed:15037072, FT ECO:0007744|PDB:1S4V" FT TURN 132..136 FT /evidence="ECO:0007829|PDB:1S4V" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:1S4V" FT HELIX 150..167 FT /evidence="ECO:0007829|PDB:1S4V" FT HELIX 175..181 FT /evidence="ECO:0007829|PDB:1S4V" FT HELIX 194..204 FT /evidence="ECO:0007829|PDB:1S4V" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:1S4V" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:1S4V" FT STRAND 236..239 FT /evidence="ECO:0007829|PDB:1S4V" FT HELIX 245..254 FT /evidence="ECO:0007829|PDB:1S4V" FT STRAND 257..261 FT /evidence="ECO:0007829|PDB:1S4V" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:1S4V" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:1S4V" FT STRAND 286..295 FT /evidence="ECO:0007829|PDB:1S4V" FT STRAND 301..306 FT /evidence="ECO:0007829|PDB:1S4V" FT STRAND 318..322 FT /evidence="ECO:0007829|PDB:1S4V" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:1S4V" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:1S4V" SQ SEQUENCE 360 AA; 40111 MW; 6EC61C1A010FE8A1 CRC64; MQKFILLALS LALVLAITES FDFHEKELES EESLWGLYER WRSHHTVSRS LHEKQKRFNV FKHNAMHVHN ANKMDKPYKL KLNKFADMTN HEFRNTYSGS KVKHHRMFRG GPRGNGTFMY EKVDTVPASV DWRKKGAVTS VKDQGQCGSC WAFSTIVAVE GINQIKTNKL VSLSEQELVD CDTDQNQGCN GGLMDYAFEF IKQRGGITTE ANYPYEAYDG TCDVSKENAP AVSIDGHENV PENDENALLK AVANQPVSVA IDAGGSDFQF YSEGVFTGSC GTELDHGVAI VGYGTTIDGT KYWTVKNSWG PEWGEKGYIR MERGISDKEG LCGIAMEASY PIKKSSNNPS GIKSSPKDEL //