ID Q6NYJ7_DANRE Unreviewed; 438 AA. AC Q6NYJ7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-JUN-2021, entry version 87. DE RecName: Full=Asparaginyl endopeptidase {ECO:0000256|ARBA:ARBA00014845}; DE EC=3.4.22.34 {ECO:0000256|ARBA:ARBA00012628}; DE AltName: Full=Legumain {ECO:0000256|ARBA:ARBA00021147}; DE AltName: Full=Protease, cysteine 1 {ECO:0000256|ARBA:ARBA00014121}; GN Name=lgmn {ECO:0000313|EMBL:AAH66568.1, GN ECO:0000313|ZFIN:ZDB-GENE-021030-1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH66568.1}; RN [1] {ECO:0000313|EMBL:AAH66568.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney {ECO:0000313|EMBL:AAH66568.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC066568; AAH66568.1; -; mRNA. DR RefSeq; NP_999924.1; NM_214759.1. DR MEROPS; C13.A03; -. DR GeneID; 406625; -. DR KEGG; dre:406625; -. DR CTD; 5641; -. DR ZFIN; ZDB-GENE-021030-1; lgmn. DR OMA; IRYMYEH; -. DR OrthoDB; 826971at2759; -. DR PhylomeDB; Q6NYJ7; -. DR GO; GO:0005773; C:vacuole; IEA:GOC. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0031103; P:axon regeneration; IMP:ZFIN. DR GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central. DR GO; GO:0042246; P:tissue regeneration; IMP:ZFIN. DR GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central. 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 2: Evidence at transcript level; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..438 FT /note="Asparaginyl endopeptidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004278774" FT ACT_SITE 150 FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1" FT ACT_SITE 191 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1" SQ SEQUENCE 438 AA; 49192 MW; C6261245030222B4 CRC64; MSPKTVAVLG LALSLGLVVS GFPAEQPENG KHWVVIVAGS NGWYNYRHQA DVCHAYQIVH KNGIPDEQIV VMMYDDLAES PDNPTKGVVI NRPNGSDVYK GVLKDYIGDD VTPENFLAVL KGDAASVKGG SGKVLKSGPN DHVFVYFTDH GAPGLLAFPN DDLHVDDLMD TIKYMHSNNK YKKMVFYVEA CESGSMMKPL PVDINVYATT AANPDESSYA CYYDEARDTY LGDWYSVNWM EDSDVEDLSK ETLAKQFKIV KAKTNTSHVM QYGNKTLSHM KVMAFQGSSK GLDKAVEPVS LPVIAEHDLM SSPDVPLAIL KRKLQKTNDV DAVVGYLNEI HAHLQVRELL GNTMRKIVEH VVQDKEEVQD YLDGRSDLTQ YNCYKTAVRH YKKHCFNWHE QKFEYALRHL YALVNLCEGG YQAHRITAAM DDVCYFRD //