LEGU_CANEN
ID LEGU_CANEN Reviewed; 475 AA.
AC P49046;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Legumain;
DE EC=3.4.22.34;
DE AltName: Full=Asparaginyl endopeptidase;
DE Flags: Precursor;
OS Canavalia ensiformis (Jack bean) (Dolichos ensiformis).
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; Canavalia.
OX NCBI_TaxID=3823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seed;
RX PubMed=7852272; DOI=10.1093/oxfordjournals.jbchem.a124559;
RA Takeda O., Miura Y., Mitta M., Matsushita H., Kato I., Abe Y., Yokosawa H.,
RA Ishii S.;
RT "Isolation and analysis of cDNA encoding a precursor of Canavalia
RT ensiformis asparaginyl endopeptidase (legumain).";
RL J. Biochem. 116:541-546(1994).
RN [2]
RP PROTEIN SEQUENCE OF 36-60, AND CHARACTERIZATION.
RX PubMed=8429028; DOI=10.1016/s0021-9258(18)53726-1;
RA Abe Y., Shirane K., Yokosawa H., Matsushita H., Mitta M., Kato I.,
RA Ishii S.;
RT "Asparaginyl endopeptidase of jack bean seeds. Purification,
RT characterization, and high utility in protein sequence analysis.";
RL J. Biol. Chem. 268:3525-3529(1993).
RN [3]
RP REVIEW.
RX PubMed=7845236; DOI=10.1016/0076-6879(94)44044-1;
RA Ishii S.;
RT "Legumain: asparaginyl endopeptidase.";
RL Methods Enzymol. 244:604-615(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins and small molecule substrates at
CC -Asn-|-Xaa- bonds.; EC=3.4.22.34;
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR EMBL; D31787; BAA06596.1; -; mRNA.
DR PIR; JX0344; JX0344.
DR PDB; 6XT5; X-ray; 2.69 A; A/B=36-475.
DR PDBsum; 6XT5; -.
DR AlphaFoldDB; P49046; -.
DR SMR; P49046; -.
DR MEROPS; C13.001; -.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR InterPro; IPR043577; AE.
DR InterPro; IPR033165; Legumain_beta.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; PTHR12000; 1.
DR PANTHER; PTHR12000:SF25; PTHR12000:SF25; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500139; AE; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..35
FT /evidence="ECO:0000269|PubMed:8429028"
FT /id="PRO_0000026514"
FT CHAIN 36..475
FT /note="Legumain"
FT /id="PRO_0000026515"
FT ACT_SITE 158
FT /evidence="ECO:0000255"
FT ACT_SITE 200
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 54..69
FT /evidence="ECO:0007829|PDB:6XT5"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:6XT5"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6XT5"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 212..222
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:6XT5"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:6XT5"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:6XT5"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6XT5"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 357..396
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 447..458
FT /evidence="ECO:0007829|PDB:6XT5"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:6XT5"
SQ SEQUENCE 475 AA; 52763 MW; 6D1C1D6872C5504C CRC64;
MVMMLVMLSL HGTAARLNRR EWDSVIQLPT EPVDDEVGTR WAVLVAGSNG YGNYRHQADV
CHAYQLLIKG GVKEENIVVF MYDDIAYNAM NPRPGVIINH PQGPDVYAGV PKDYTGEDVT
PENLYAVILG DKSKVKGGSG KVINSNPEDR IFIFYSDHGG PGVLGMPNAP FVYAMDFIDV
LKKKHASGGY KEMVIYIEAC ESGSIFEGIM PKDLNIYVTT ASNAQENSFG TYCPGMNPPP
PEEYVTCLGD LYSVSWMEDS ETHNLKRETV QQQYQSVRKR TSNSNSYRFG SHVMQYGDTN
ITAEKLYLYH GFDPATVNFP PHNGNLEAKM EVVNQRDAEL LFMWQMYQRS NHQPEKKTHI
LEQITETVKH RNHLDGSVEL IGVLLYGPGK SSSVLHSVRA PGLPLVDDWT CLKSMVRVFE
THCGSLTQYG MKHMRAFGNV CNSGVSKASM EEACKAACGG YDAGLLYPSN TGYSA
