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Database: UniProt
Entry: M3W8K5_FELCA
LinkDB: M3W8K5_FELCA
Original site: M3W8K5_FELCA 
ID   M3W8K5_FELCA            Unreviewed;       433 AA.
AC   M3W8K5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-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:ENSFCAP00000007305.2,
GN   ECO:0000313|VGNC:VGNC:69086};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000007305.2, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000007305.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007305.2,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000007305.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007305.2,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000007305.2}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007305.2};
RG   Ensembl;
RL   Submitted (SEP-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; AANG04004659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003987980.1; XM_003987931.3.
DR   AlphaFoldDB; M3W8K5; -.
DR   STRING; 9685.ENSFCAP00000007305; -.
DR   MEROPS; C13.004; -.
DR   PaxDb; 9685-ENSFCAP00000007305; -.
DR   Ensembl; ENSFCAT00000007891.5; ENSFCAP00000007305.2; ENSFCAG00000007889.5.
DR   GeneID; 101098470; -.
DR   KEGG; fca:101098470; -.
DR   CTD; 5641; -.
DR   VGNC; VGNC:69086; LGMN.
DR   eggNOG; KOG1348; Eukaryota.
DR   GeneTree; ENSGT00940000154782; -.
DR   HOGENOM; CLU_024160_2_0_1; -.
DR   InParanoid; M3W8K5; -.
DR   OMA; YPIDRIC; -.
DR   OrthoDB; 2951493at2759; -.
DR   Proteomes; UP000011712; Chromosome B3.
DR   Bgee; ENSFCAG00000007889; Expressed in adult mammalian kidney and 11 other cell types or tissues.
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; IBA:GO_Central.
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:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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   GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
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; 1.
DR   PIRSF; PIRSF019663; Legumain; 1.
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:UP000011712};
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..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..433
FT                   /note="Legumain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004041711"
FT   DOMAIN          334..429
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   433 AA;  49157 MW;  D4469C005CCABD7E CRC64;
     MIWEGAVLLS VVLGIGAVPM DDPEDGGKHW VVIVAGSNGW YNYRHQADAC HAYQIVHRNG
     IPDEQIIVMM YDDIANSEDN PTPGIVINRP NGSDVYAGVL KDYTGEDVTP ENFLAVLRGD
     EEAVKGKGSG KVLKSGPRDH VFVYFTDHGA TGILVFPNDD LHVKDLNKTI QYMYKHKMYQ
     KMVFYIEACE SGSMMRHLPS DINVYATTAA NPTESSYACY YDEKRSTYLG DWYSVNWMED
     SDVEDLTKET LHKQYQLVKS HTNTSHVMQY GNKSISSMKV MQFQGMKHKA SSPISLPPVK
     DLDLTPSPEV PLTIMKRKLM STNDLQESRN LVEKIHRHLD ARHVIEKSVQ KIVSLIARSG
     AEAEGLLSER AELTAHDCYQ AAVSHFRTHC FNWHSPTYEY ALRHLYVLVN LCEKPYPIDR
     IKLSMDKVCL HYY
//
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