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Database: UniProt
Entry: G5EBF4_CAEEL
LinkDB: G5EBF4_CAEEL
Original site: G5EBF4_CAEEL 
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
//
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