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Database: UniProt
Entry: K7FJF9_PELSI
LinkDB: K7FJF9_PELSI
Original site: K7FJF9_PELSI 
ID   K7FJF9_PELSI            Unreviewed;       411 AA.
AC   K7FJF9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Legumain {ECO:0000256|ARBA:ARBA00021147};
DE            EC=3.4.22.34 {ECO:0000256|ARBA:ARBA00012628};
DE   AltName: Full=Protease, cysteine 1 {ECO:0000256|ARBA:ARBA00030799};
GN   Name=LGMN {ECO:0000313|Ensembl:ENSPSIP00000008169.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000008169.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000008169.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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}.
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DR   EMBL; AGCU01156127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01156128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01156129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01156130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01156131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K7FJF9; -.
DR   STRING; 13735.ENSPSIP00000008169; -.
DR   Ensembl; ENSPSIT00000008212.1; ENSPSIP00000008169.1; ENSPSIG00000007301.1.
DR   eggNOG; KOG1348; Eukaryota.
DR   GeneTree; ENSGT00940000154782; -.
DR   HOGENOM; CLU_024160_2_0_1; -.
DR   OMA; YPIDRIC; -.
DR   TreeFam; TF313403; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061133; F:endopeptidase activator activity; IEA:Ensembl.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl.
DR   GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0097061; P:dendritic spine organization; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:1901185; P:negative regulation of ERBB signaling pathway; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IEA:Ensembl.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IEA:Ensembl.
DR   GO; GO:0051604; P:protein maturation; IEA:Ensembl.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR   GO; GO:0032801; P:receptor catabolic process; IEA:Ensembl.
DR   GO; GO:0003014; P:renal system process; IEA:Ensembl.
DR   GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
DR   GO; GO:0097264; P:self proteolysis; IEA:Ensembl.
DR   CDD; cd21115; legumain_C; 1.
DR   Gene3D; 1.10.132.130; -; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR043577; AE.
DR   InterPro; IPR048501; Legum_prodom.
DR   InterPro; IPR046427; Legumain_prodom_sf.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR12000:SF42; LEGUMAIN; 1.
DR   Pfam; PF20985; Legum_prodom; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PIRSF; PIRSF500139; AE; 2.
DR   PIRSF; PIRSF019663; Legumain; 2.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..411
FT                   /note="Legumain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003901781"
FT   DOMAIN          313..408
FT                   /note="Legumain prodomain"
FT                   /evidence="ECO:0000259|Pfam:PF20985"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT   ACT_SITE        189
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ   SEQUENCE   411 AA;  46870 MW;  583F8B04B1616D81 CRC64;
     MILKAVVLLG YILGISTFPL EDPEDGGKHW VVIVAGSNGW YNYRHQADVC HAYQIVHRNG
     IPDEQIIIMM YDDIAENEEN PTKGIIINRP NGTDVYKGVP KDYVQEDVTP KNFLAVLRGD
     AEAMKGIGSG KVLKSGPKDH VFVYFTDHGA PGLLAFPNDD LHVKDLNKTI YYMYHNKKYQ
     KLVFYIEACE SGSMMNHLAE NINVYATTAA NPKESSYACY YDDKRQTYLG DWYSVNWMED
     SDVEDLGKET LHKQFLIVKK HTNTSHVMQY GNKSISSMKV SQFQSMGKKS SPIPLPPVAR
     YDLTPSPKKI AGEMKTHLEA KRIIQESMRK IILFVTASEE RTEQILSDRL TISDYDCYQS
     AVNHFKAHCF NWHSPLYEYA LRQLYALVNV CEGGYPIDRI QLAMYHVCLG Y
//
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