ID G5EBF4_CAEEL Unreviewed; 462 AA.
AC G5EBF4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=legumain {ECO:0000256|ARBA:ARBA00012628};
DE EC=3.4.22.34 {ECO:0000256|ARBA:ARBA00012628};
GN Name=lgmn-1 {ECO:0000313|EMBL:CAA99935.1};
GN ORFNames=CELE_T28H10.3 {ECO:0000313|EMBL:CAA99935.1}, T28H10.3
GN {ECO:0000313|WormBase:T28H10.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA99935.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA99935.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA99935.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins and small molecule substrates at
CC -Asn-|-Xaa- bonds.; EC=3.4.22.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000810};
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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DR EMBL; BX284605; CAA99935.1; -; Genomic_DNA.
DR PIR; T19231; T19231.
DR RefSeq; NP_506137.1; NM_073736.5.
DR AlphaFoldDB; G5EBF4; -.
DR SMR; G5EBF4; -.
DR STRING; 6239.T28H10.3.1; -.
DR MEROPS; C13.A02; -.
DR EPD; G5EBF4; -.
DR PaxDb; 6239-T28H10-3; -.
DR PeptideAtlas; G5EBF4; -.
DR EnsemblMetazoa; T28H10.3.1; T28H10.3.1; WBGene00012144.
DR GeneID; 179714; -.
DR KEGG; cel:CELE_T28H10.3; -.
DR AGR; WB:WBGene00012144; -.
DR WormBase; T28H10.3; CE14367; WBGene00012144; -.
DR eggNOG; KOG1348; Eukaryota.
DR GeneTree; ENSGT00940000154782; -.
DR HOGENOM; CLU_024160_0_0_1; -.
DR InParanoid; G5EBF4; -.
DR OMA; ALPDICM; -.
DR OrthoDB; 2951493at2759; -.
DR PhylomeDB; G5EBF4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012144; Expressed in larva and 3 other cell types or tissues.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
DR CDD; cd21115; legumain_C; 1.
DR Gene3D; 1.10.132.130; -; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR043577; AE.
DR InterPro; IPR048501; Legum_prodom.
DR InterPro; IPR046427; Legumain_prodom_sf.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR12000:SF42; LEGUMAIN; 1.
DR Pfam; PF20985; Legum_prodom; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Proteomics identification {ECO:0007829|EPD:G5EBF4,
KW ECO:0007829|PeptideAtlas:G5EBF4};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..462
FT /note="legumain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003475838"
FT DOMAIN 350..431
FT /note="Legumain prodomain"
FT /evidence="ECO:0000259|Pfam:PF20985"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 202
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 462 AA; 53238 MW; 0181C69A4B63CA96 CRC64;
MRPLALLICI IVLFLVTEAR YNPRKGLAAG RQRKHKYQDE GEAFVVLVAG SNGWYNYRHQ
ADVAHAYHTL RNHGIPEENI ITMMYDDVAN NPLNPYKGKL FNRPHGKDLY KGLKIDYKGA
SVTPENFLNV LKGNASGIDG GNGRVLETND NDRVFVYFTD HGAVGMISFP DGILTVKQLN
DVLVWMHKNK KYSQLTFYLE ACESGSMFEE VLRSDMDIYA ISAANSHESS WGTFCENDMN
LPCLGDLFSV NWMTDSDGED LKTETLEFQY ELVKKETNLS HVMQFGDKDI AKEAVALFQG
DKEDREYVED FGLSASKSVN WPARDIELNH LISQHRKSND LLSSNKLEYK INRIKETRRA
IKRNVHMIVQ KFFDGESEDL ISRVLTQTRP VLDLRCHHIA VHLFKKYCIN FNEYEYAMKY
VKVINNMCIY RRIEEIVLAL PDICMDIDIE QEVAIRLEKE FL
//