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Protein

Legumain

Gene

Lgmn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system (By similarity).By similarity

Catalytic activityi

Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei150 – 1501By similarity
Active sitei191 – 1911NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC13.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Legumain (EC:3.4.22.34)
Alternative name(s):
Asparaginyl endopeptidase
Protease, cysteine 1
Gene namesi
Name:Lgmn
Synonyms:Prsc1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619832. Lgmn.

Subcellular locationi

GO - Cellular componenti

  • lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717By similarityAdd
BLAST
Chaini18 – 325308LegumainPRO_0000026506Add
BLAST
Propeptidei326 – 435110By similarityPRO_0000026507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence analysis
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi380 ↔ 414By similarity
Disulfide bondi392 ↔ 431By similarity

Post-translational modificationi

Activated by autocatalytic processing at pH 4.By similarity
Glycosylated.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei325 – 3262Cleavage; by autolysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9R0J8.
PRIDEiQ9R0J8.

PTM databases

iPTMnetiQ9R0J8.
PhosphoSiteiQ9R0J8.

Miscellaneous databases

PMAP-CutDBQ9R0J8.

Expressioni

Tissue specificityi

Detected in kidney cortex (at protein level).1 Publication

Interactioni

Subunit structurei

Monomer after autocatalytic processing. Homodimer before autocatalytic removal of the propeptide. May interact with integrins (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010101.

Family & Domainsi

Domaini

In the zymogen form, the uncleaved propeptide blocks access to the active site.By similarity

Sequence similaritiesi

Belongs to the peptidase C13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1348. Eukaryota.
COG5206. LUCA.
HOGENOMiHOG000236335.
HOVERGENiHBG031304.
InParanoidiQ9R0J8.
KOiK01369.
PhylomeDBiQ9R0J8.

Family and domain databases

InterProiIPR001096. Peptidase_C13.
[Graphical view]
PANTHERiPTHR12000. PTHR12000. 1 hit.
PfamiPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFiPIRSF019663. Legumain. 1 hit.
PRINTSiPR00776. HEMOGLOBNASE.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R0J8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTWRVAVLLS LVLGAGAVHI GVDDPEDGGK HWVVIVAGSN GWYNYRHQAD
60 70 80 90 100
ACHAYQIIHR NGIPDEQIIV MMYDDIANNE ENPTPGVVIN RPNGTDVYKG
110 120 130 140 150
VPKDYTGEDV TPENFLAVLR GDEEAVKGKG SGKVLKSGPR DHVFVYFTDH
160 170 180 190 200
GATGILVFPN EDLHVKDLNK TIRYMYEHKM YQKMVFYIEA CESGSMMNHL
210 220 230 240 250
PDDIDVYATT AANPNESSYA CYYDEERSTY LGDWYSVNWM EDSDVEDLTK
260 270 280 290 300
ETLHKQYHLV KSHTNTSHVM QYGNKSISTM KVMQFQGMKH RASSPISLPP
310 320 330 340 350
VTHLDLTPSP DVPLTILKRK LLRTNNMKES QVLVGQIQHL LDARHIIEKS
360 370 380 390 400
VQKIVSLLAG FGETAQKHLS ERAMLTAHDC HQEAVTHFRT HCFNWHSVTY
410 420 430
EHALRYLYVL ANLCEKPYPI DRIKMAMDKV CLSHY
Length:435
Mass (Da):49,466
Last modified:May 1, 2000 - v1
Checksum:iE835F21C13F17A98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 43TWR → IWK in AAF73260 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032766 mRNA. Translation: BAA84750.1.
AF154349 mRNA. Translation: AAF73260.1.
RefSeqiNP_071562.2. NM_022226.2.
UniGeneiRn.206021.

Genome annotation databases

GeneIDi63865.
KEGGirno:63865.
UCSCiRGD:619832. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032766 mRNA. Translation: BAA84750.1.
AF154349 mRNA. Translation: AAF73260.1.
RefSeqiNP_071562.2. NM_022226.2.
UniGeneiRn.206021.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010101.

Protein family/group databases

MEROPSiC13.004.

PTM databases

iPTMnetiQ9R0J8.
PhosphoSiteiQ9R0J8.

Proteomic databases

PaxDbiQ9R0J8.
PRIDEiQ9R0J8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi63865.
KEGGirno:63865.
UCSCiRGD:619832. rat.

Organism-specific databases

CTDi5641.
RGDi619832. Lgmn.

Phylogenomic databases

eggNOGiKOG1348. Eukaryota.
COG5206. LUCA.
HOGENOMiHOG000236335.
HOVERGENiHBG031304.
InParanoidiQ9R0J8.
KOiK01369.
PhylomeDBiQ9R0J8.

Miscellaneous databases

PMAP-CutDBQ9R0J8.
PROiQ9R0J8.

Family and domain databases

InterProiIPR001096. Peptidase_C13.
[Graphical view]
PANTHERiPTHR12000. PTHR12000. 1 hit.
PfamiPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFiPIRSF019663. Legumain. 1 hit.
PRINTSiPR00776. HEMOGLOBNASE.
ProtoNetiSearch...

Entry informationi

Entry nameiLGMN_RAT
AccessioniPrimary (citable) accession number: Q9R0J8
Secondary accession number(s): Q9JLN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.