CYSEP_RICCO
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 03-AUG-2022, entry version 102.
DE RecName: Full=Vignain;
DE EC=3.4.22.-;
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 (2.0 ANGSTROMS) OF 125-350 IN COMPLEX WITH
RP CHLOROMETHYLKETONE (CMK) INHIBITOR.
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}.
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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 STRING; 3988.XP_002511277.1; -.
DR MEROPS; C01.010; -.
DR GeneID; 8278243; -.
DR KEGG; rcu:8278243; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; O65039; -.
DR OrthoDB; 1275401at2759; -.
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 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 3D-structure; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Protease; Signal; Thiol protease.
FT SIGNAL 1..20
FT PROPEP 21..124
FT /note="Activation peptide"
FT /id="PRO_0000026442"
FT CHAIN 125..353
FT /note="Vignain"
FT /id="PRO_0000026443"
FT PROPEP 354..360
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 ACT_SITE 286
FT ACT_SITE 307
FT DISULFID 147..189
FT DISULFID 181..222
FT DISULFID 280..332
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
