CYSEP_VIGMU
ID CYSEP_VIGMU Reviewed; 362 AA.
AC P12412;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Vignain;
DE EC=3.4.22.-;
DE AltName: Full=Bean endopeptidase;
DE AltName: Full=Cysteine proteinase;
DE AltName: Full=Sulfhydryl-endopeptidase;
DE Short=SH-EP;
DE Contains:
DE RecName: Full=Vignain-1;
DE Contains:
DE RecName: Full=Vignain-2;
DE Flags: Precursor;
OS Vigna mungo (Black gram) (Phaseolus mungo).
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; Vigna.
OX NCBI_TaxID=3915;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 132-140.
RC TISSUE=Seed cotyledon;
RX PubMed=2780300; DOI=10.1093/nar/17.16.6733;
RA Akasofu H., Yamauchi D., Mitsuhashi W., Minamikawa T.;
RT "Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from
RT cotyledons of germinating Vigna mungo seeds.";
RL Nucleic Acids Res. 17:6733-6733(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=2336365; DOI=10.1093/nar/18.7.1892;
RA Akasofu H., Yamauchi D., Minamikawa T.;
RT "Nucleotide sequence of the gene for the Vigna mungo sulfhydryl-
RT endopeptidase (SH-EP).";
RL Nucleic Acids Res. 18:1892-1892(1990).
RN [3]
RP PROTEIN SEQUENCE OF 127-140; 197-216; 324-333 AND 339-352, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8076688; DOI=10.1016/0014-5793(94)00809-4;
RA Okamoto T., Nakayama H., Seta K., Isobe T., Minamikawa T.;
RT "Posttranslational processing of a carboxy-terminal propeptide containing a
RT KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP).";
RL FEBS Lett. 351:31-34(1994).
RN [4]
RP ERRATUM OF PUBMED:8076688.
RA Okamoto T., Nakayama H., Seta K., Isobe T., Minamikawa T.;
RL FEBS Lett. 356:152-152(1994).
CC -!- FUNCTION: Thought to be involved in the hydrolysis of stored seed
CC proteins. In vitro, catalyzes the hydrolysis of proteins, such as
CC azocasein. Shows a preferential cleavage for Asn-|-Xaa in small
CC molecule substrates such as Boc-Asn-|-OPHNO(2).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:8076688}. Vacuole, aleurone grain
CC {ECO:0000269|PubMed:8076688}.
CC -!- PTM: The mature protein is not glycosylated.
CC -!- PTM: The precursor stored in the endoplasmic reticulum lumen is
CC processed during the transport to proteins bodies to two dominant
CC mature forms that differ by a single amino acid residue at the N-
CC terminus.
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; X15732; CAA33753.1; -; mRNA.
DR EMBL; X51900; CAA36181.1; -; Genomic_DNA.
DR PIR; S12581; S12581.
DR AlphaFoldDB; P12412; -.
DR SMR; P12412; -.
DR MEROPS; C01.010; -.
DR MEROPS; I29.003; -.
DR BRENDA; 3.4.22.B1; 4742.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; 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 Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Protease; Signal; Thiol protease; Vacuole;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..126
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8076688"
FT /id="PRO_0000026445"
FT CHAIN 127..352
FT /note="Vignain-1"
FT /id="PRO_0000026446"
FT CHAIN 128..352
FT /note="Vignain-2"
FT /id="PRO_0000026447"
FT PROPEP 353..362
FT /id="PRO_0000026448"
FT MOTIF 359..362
FT /note="Prevents secretion from ER"
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 DISULFID 149..191
FT /evidence="ECO:0000250"
FT DISULFID 183..224
FT /evidence="ECO:0000250"
FT DISULFID 282..334
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 40222 MW; B7C3B92868D5E3C8 CRC64;
MAMKKLLWVV LSLSLVLGVA NSFDFHEKDL ESEESLWDLY ERWRSHHTVS RSLGEKHKRF
NVFKANVMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA GSKVNHHKMF RGSQHGSGTF
MYEKVGSVPA SVDWRKKGAV TDVKDQGQCG SCWAFSTIVA VEGINQIKTN KLVSLSEQEL
VDCDKEENQG CNGGLMESAF EFIKQKGGIT TESNYPYTAQ EGTCDESKVN DLAVSIDGHE
NVPVNDENAL LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCNTDLNHGV AIVGYGTTVD
GTNYWIVRNS WGPEWGEQGY IRMQRNISKK EGLCGIAMMA SYPIKNSSDN PTGSLSSPKD
EL
