ID Q6NYJ7_DANRE Unreviewed; 438 AA. AC Q6NYJ7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 22-FEB-2023, entry version 93. DE RecName: Full=Legumain {ECO:0000256|ARBA:ARBA00021147}; DE EC=3.4.22.34 {ECO:0000256|ARBA:ARBA00012628}; DE AltName: Full=Asparaginyl endopeptidase {ECO:0000256|ARBA:ARBA00031588}; DE AltName: Full=Protease, cysteine 1 {ECO:0000256|ARBA:ARBA00030799}; GN Name=sb:cb173 {ECO:0000313|RefSeq:NP_999924.1}; GN Synonyms=cb173 {ECO:0000313|RefSeq:NP_999924.1}, cb460 GN {ECO:0000313|RefSeq:NP_999924.1}, wu:fa98g05 GN {ECO:0000313|RefSeq:NP_999924.1}, wu:fj92g08 GN {ECO:0000313|RefSeq:NP_999924.1}, zgc:76953 GN {ECO:0000313|RefSeq:NP_999924.1}; GN OrderedLocusNames=lgmn {ECO:0000313|EMBL:AAH66568.1, GN ECO:0000313|RefSeq:NP_999924.1, 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. RN [2] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16109975; RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R., RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.; RT "The zebrafish gene map defines ancestral vertebrate chromosomes."; RL Genome Res. 15:1307-1314(2005). RN [3] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19389629; RA Kalen M., Wallgard E., Asker N., Nasevicius A., Athley E., Billgren E., RA Larson J.D., Wadman S.A., Norseng E., Clark K.J., He L., RA Karlsson-Lindahl L., Hager A.K., Weber H., Augustin H., Samuelsson T., RA Kemmet C.K., Utesch C.M., Essner J.J., Hackett P.B., Hellstrom M.; RT "Combination of reverse and chemical genetic screens reveals angiogenesis RT inhibitors and targets."; RL Chem. Biol. 16:432-441(2009). RN [4] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23958499; DOI=10.1016/j.molimm.2013.07.012; RA Pietretti D., Spaink H.P., Falco A., Forlenza M., Wiegertjes G.F.; RT "Accessory molecules for Toll-like receptors in Teleost fish. RT Identification of TLR4 interactor with leucine-rich repeats (TRIL)."; RL Mol. Immunol. 56:745-756(2013). RN [5] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24683187; RA Briolat V., Jouneau L., Carvalho R., Palha N., Langevin C., Herbomel P., RA Schwartz O., Spaink H.P., Levraud J.P., Boudinot P.; RT "Contrasted innate responses to two viruses in zebrafish: insights into the RT ancestral repertoire of vertebrate IFN-stimulated genes."; RL J. Immunol. 192:4328-4341(2014). RN [6] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24747977; RA Ma L., Shen Y.Q., Khatri H.P., Schachner M.; RT "The asparaginyl endopeptidase legumain is essential for functional RT recovery after spinal cord injury in adult zebrafish."; RL PLoS ONE 9:e95098-e95098(2014). RN [7] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26469318; RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M., RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D., RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E., RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M., RA Reith W., Hertzano R.; RT "RFX transcription factors are essential for hearing in mice."; RL Nat. Commun. 6:8549-8549(2015). RN [8] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=27189481; RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I., RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y., RA Bobe J.; RT "Gene evolution and gene expression after whole genome duplication in fish: RT the PhyloFish database."; RL BMC Genomics 17:368-368(2016). RN [9] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28758957; RA Xu H., Liu E., Li Y., Li X., Ding C.; RT "Transcriptome Analysis Reveals Increases in Visceral Lipogenesis and RT Storage and Activation of the Antigen Processing and Presentation Pathway RT during the Mouth-Opening Stage in Zebrafish Larvae."; RL Int. J. Mol. Sci. 18:E1634-E1634(2017). RN [10] {ECO:0000313|RefSeq:NP_999924.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28162997; RA Jafari A., Qanie D., Andersen T.L., Zhang Y., Chen L., Postert B., RA Parsons S., Ditzel N., Khosla S., Johansen H.T., Kjaersgaard-Andersen P., RA Delaisse J.M., Abdallah B.M., Hesselson D., Solberg R., Kassem M.; RT "Legumain Regulates Differentiation Fate of Human Bone Marrow Stromal Cells RT and Is Altered in Postmenopausal Osteoporosis."; RL Stem Cell Reports 8:373-386(2017). RN [11] {ECO:0000313|RefSeq:NP_999924.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (APR-2022) to UniProtKB. 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 AlphaFoldDB; Q6NYJ7; -. DR MEROPS; C13.A03; -. DR GeneID; 406625; -. DR KEGG; dre:406625; -. DR CTD; 5641; -. DR ZFIN; ZDB-GENE-021030-1; lgmn. DR OrthoDB; 2951493at2759; -. DR PhylomeDB; Q6NYJ7; -. DR Proteomes; UP000000437; Chromosome 13. 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 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 Gene3D; 1.10.132.130; -; 1. DR Gene3D; 3.40.50.1460; -; 1. DR InterPro; IPR043577; AE. DR InterPro; IPR046427; Legumain_prodom_sf. DR InterPro; IPR001096; Peptidase_C13. DR PANTHER; PTHR12000:SF23; ASPARAGINYL ENDOPEPTIDASE; 1. DR PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 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|PeptideAtlas:Q6NYJ7}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP, FT ECO:0000313|RefSeq:NP_999924.1" FT CHAIN 22..438 FT /note="Legumain" FT /evidence="ECO:0000256|SAM:SignalP, FT ECO:0000313|RefSeq:NP_999924.1" 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 //