CYSEP_PHAVU
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 03-AUG-2022, entry version 103.
DE RecName: Full=Vignain;
DE EC=3.4.22.-;
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 STRING; 3885.XP_007137980.1; -.
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 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 Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..131
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
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:0000250"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT ACT_SITE 309
FT /evidence="ECO:0000250"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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