LGMN_BOVIN
ID LGMN_BOVIN Reviewed; 433 AA.
AC Q95M12; Q2TA48;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Legumain;
DE EC=3.4.22.34;
DE AltName: Full=Asparaginyl endopeptidase;
DE AltName: Full=Protease, cysteine 1;
DE Flags: Precursor;
GN Name=LGMN; Synonyms=PRSC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-51, FUNCTION, CATALYTIC
RP ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=11983426; DOI=10.1016/s0167-4838(02)00209-1;
RA Yamane T., Takeuchi K., Yamamoto Y., Li Y.-H., Fujiwara M., Nishi K.,
RA Takahashi S., Ohkubo I.;
RT "Legumain from bovine kidney: its purification, molecular cloning,
RT immunohistochemical localization and degradation of annexin II and vitamin
RT D-binding protein.";
RL Biochim. Biophys. Acta 1596:108-120(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has a strict specificity for hydrolysis of asparaginyl bonds.
CC Can also cleave aspartyl bonds slowly, especially under acidic
CC conditions. Required for normal degradation of internalized EGFR. Plays
CC a role in the regulation of cell proliferation via its role in EGFR
CC degradation (By similarity). Required for normal lysosomal protein
CC degradation in renal proximal tubules. May be involved in the
CC processing of proteins for MHC class II antigen presentation in the
CC lysosomal/endosomal system. {ECO:0000250, ECO:0000269|PubMed:11983426}.
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:0000269|PubMed:11983426};
CC -!- SUBUNIT: Monomer after autocatalytic processing. Homodimer before
CC autocatalytic removal of the propeptide. May interact with integrins
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:11983426}.
CC -!- TISSUE SPECIFICITY: Detected in kidney (at protein level).
CC {ECO:0000269|PubMed:11983426}.
CC -!- DOMAIN: In the zymogen form, the uncleaved propeptide blocks access to
CC the active site. {ECO:0000250}.
CC -!- PTM: Activated by autocatalytic processing at pH 4. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR EMBL; AB060129; BAB69947.1; -; mRNA.
DR EMBL; BC111117; AAI11118.1; -; mRNA.
DR RefSeq; NP_776526.1; NM_174101.2.
DR AlphaFoldDB; Q95M12; -.
DR SMR; Q95M12; -.
DR STRING; 9913.ENSBTAP00000053922; -.
DR ChEMBL; CHEMBL3286062; -.
DR MEROPS; C13.004; -.
DR PaxDb; Q95M12; -.
DR PeptideAtlas; Q95M12; -.
DR PRIDE; Q95M12; -.
DR GeneID; 281281; -.
DR KEGG; bta:281281; -.
DR CTD; 5641; -.
DR eggNOG; KOG1348; Eukaryota.
DR HOGENOM; CLU_024160_2_0_1; -.
DR InParanoid; Q95M12; -.
DR OrthoDB; 826971at2759; -.
DR TreeFam; TF313403; -.
DR BRENDA; 3.4.22.34; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:1901185; P:negative regulation of ERBB signaling pathway; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISS:UniProtKB.
DR GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
DR GO; GO:0003014; P:renal system process; ISS:UniProtKB.
DR InterPro; IPR043577; AE.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; PTHR12000; 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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Protease; Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT PROPEP 18..25
FT /evidence="ECO:0000269|PubMed:11983426"
FT /id="PRO_0000259469"
FT CHAIN 26..323
FT /note="Legumain"
FT /id="PRO_0000259470"
FT PROPEP 324..433
FT /evidence="ECO:0000250"
FT /id="PRO_0000259471"
FT ACT_SITE 148
FT /evidence="ECO:0000250"
FT ACT_SITE 189
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 323..324
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 378..412
FT /evidence="ECO:0000250"
FT DISULFID 390..429
FT /evidence="ECO:0000250"
FT CONFLICT 5
FT /note="F -> V (in Ref. 2; AAI11118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 49284 MW; 48B2CF9844206AB4 CRC64;
MIWEFTVLLS LVLGTGAVPL EDPEDGGKHW VVIVAGSNGW YNYRHQADAC HAYQIVHRNG
IPDEQIIVMM YDDIANSEDN PTPGIVINRP NGSDVYQGVL KDYTGEDVTP KNFLAVLRGD
AEAVKGVGSG KVLKSGPRDH VFVYFTDHGA TGILVFPNED LHVKDLNETI RYMYEHKMYQ
KMVFYIEACE SGSMMNHLPP DINVYATTAA NPRESSYACY YDEQRSTFLG DWYSVNWMED
SDVEDLTKET LHKQYQLVKS HTNTSHVMQY GNKSISAMKL MQFQGLKHQA SSPISLPAVS
RLDLTPSPEV PLSIMKRKLM STNDLQESRR LVQKIDRHLE ARNIIEKSVR KIVTLVSGSA
AEVDRLLSQR APLTEHACYQ TAVSHFRSHC FNWHNPTYEY ALRHLYVLVN LCENPYPIDR
IKLSMNKVCH GYY
