ID LGMN_MACFA Reviewed; 433 AA. AC Q4R4T8; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 19. 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; ORFNames=QccE-20451; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Has a strict specificity for hydrolysis of asparaginyl CC bonds. Can also cleave aspartyl bonds slowly, especially under CC acidic conditions. May be involved in the processing of proteins CC for MHC class II antigen presentation in the lysosomal/endosomal CC system (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins and small molecule CC substrates at -Asn-|-Xaa- bonds. CC -!- SUBCELLULAR LOCATION: Lysosome (By similarity). CC -!- PTM: Glycosylated (Probable). CC -!- SIMILARITY: Belongs to the peptidase C13 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB169806; BAE01887.1; -; mRNA. DR MEROPS; C13.004; -. DR HOVERGEN; Q4R4T8; -. DR BRENDA; 3.4.22.34; 3438. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR001096; Peptidase_C13. DR PANTHER; PTHR12000; Peptidase_C13; 1. DR Pfam; PF01650; Peptidase_C13; 1. DR PRINTS; PR00776; HEMOGLOBNASE. PE 2: Evidence at transcript level; KW Glycoprotein; Hydrolase; Lysosome; Protease; Signal; Thiol protease; KW Zymogen. FT SIGNAL 1 17 By similarity. FT CHAIN 18 323 Legumain. FT /FTId=PRO_0000259472. FT PROPEP 324 433 By similarity. FT /FTId=PRO_0000259473. FT ACT_SITE 148 148 Potential. FT ACT_SITE 189 189 Potential. FT SITE 323 324 Cleavage; by autolysis (By similarity). FT CARBOHYD 91 91 N-linked (GlcNAc...) (Potential). FT CARBOHYD 167 167 N-linked (GlcNAc...) (Potential). FT CARBOHYD 263 263 N-linked (GlcNAc...) (Potential). FT CARBOHYD 272 272 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 433 AA; 49438 MW; 872951A13370D504 CRC64; MVWKVAVFLS VTLGIGAVPI DDPEDGGKHW VVIVAGSNGW YNYRHQADAC HAYQIIHRNG IPDEQIVVMM YDDIAYSEDN PTPGIVINRP NGTDVYQGVP KDYTGEDVTP QNFLAVLRGD AEAVKGIGSG KVLKSGPQDH VFVYFTDHGS TGILVFPNED LHVKDLNETI YYMYKHKMYR KMVFYIEACE SGSMMNHLPD NINVYATTAA NPRESSYACY YDEKRSTYLG DWYSVNWMED SDVEDLTKET LHKQYHLVKS HTNTSHVMQY GNKTISTMKV MQFQGMKHKA SSPLSLPPVT HLDLTPSPDV PLTIMKRKLM NTNDLEESRQ LTEEIQRHLD ARHLIEKSVR KIVSLLAASE AEVEQLLSER APLTGHSCYP EALLHFRTHC FNWHSPTYEY ALRHLYVLVN LCEKPYPLHR IKLSMDHVCL GHY //