ID   CYSEP_PHAVU             Reviewed;         362 AA.
AC   P25803;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Vignain;
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:P80884};
DE   AltName: Full=Bean endopeptidase;
DE   AltName: Full=Cysteine proteinase EP-C1;
DE   Flags: Precursor;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Saxa; TISSUE=Seedling;
RX   PubMed=1627783; DOI=10.1007/bf00026797;
RA   Ogushi Y., Tanaka T., Yamauchi D., Minamikawa T.;
RT   "Nucleotide sequence of a gene for an endopeptidase (EP-C1) from Phaseolus
RT   vulgaris.";
RL   Plant Mol. Biol. 19:705-706(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-362.
RC   STRAIN=cv. Goldstar; TISSUE=Fruit;
RX   PubMed=1863761; DOI=10.1007/bf00016081;
RA   Tanaka T., Yamauchi D., Minamikawa T.;
RT   "Nucleotide sequence of cDNA for an endopeptidase (EP-C1) from pods of
RT   maturing Phaseolus vulgaris fruits.";
RL   Plant Mol. Biol. 16:1083-1084(1991).
CC   -!- FUNCTION: Thought to be involved in the hydrolysis of stored seed
CC       proteins.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
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; X63102; CAA44816.1; -; Genomic_DNA.
DR   EMBL; X56753; CAA40073.1; -; mRNA.
DR   PIR; S22502; S22502.
DR   AlphaFoldDB; P25803; -.
DR   SMR; P25803; -.
DR   MEROPS; C01.010; -.
DR   MEROPS; I29.003; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; 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   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   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..131
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P00785"
FT                   /id="PRO_0000026440"
FT   CHAIN           132..362
FT                   /note="Vignain"
FT                   /id="PRO_0000026441"
FT   MOTIF           359..362
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        309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        149..191
FT                   /evidence="ECO:0000250|UniProtKB:P07858"
FT   DISULFID        183..224
FT                   /evidence="ECO:0000250|UniProtKB:P25250"
FT   DISULFID        282..334
FT                   /evidence="ECO:0000250|UniProtKB:P25250"
FT   CONFLICT        107
FT                   /note="P -> H (in Ref. 2; CAA40073)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   362 AA;  40212 MW;  9AAF24A557FAF806 CRC64;
     MATKKLLWVV LSFSLVLGVA NSFDFHDKDL ASEESLWDLY ERWRSHHTVS RSLGEKHKRF
     NVFKANLMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA GSKVNHPRMF RGTPHENGAF
     MYEKVVSVPP SVDWRKKGAV TDVKDQGQCG SCWAFSTVVA VEGINQIKTN KLVALSEQEL
     VDCDKEENQG CNGGLMESAF EFIKQKGGIT TESNYPYKAQ EGTCDASKVN DLAVSIDGHE
     NVPANDEDAL LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCSTDLNHGV AIVGYGTTVD
     GTNYWIVRNS WGPEWGEHGY IRMQRNISKK EGLCGIAMLP SYPIKNSSDN PTGSFSSPKD
     EL
//