ID GP63_LEITR Reviewed; 657 AA.
AC Q8MNZ1; Q8MNZ0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 22-FEB-2023, entry version 70.
DE RecName: Full=Leishmanolysin;
DE EC=3.4.24.36;
DE AltName: Full=Cell surface protease;
DE AltName: Full=Major surface glycoprotein;
DE AltName: Full=Major surface protease;
DE AltName: Full=Promastigote surface endopeptidase;
DE AltName: Full=Protein gp63;
DE Flags: Precursor;
GN Name=mspC;
OS Leishmania tropica.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES MSPCLTA1 AND MSPCLTA2).
RC STRAIN=MHOM/SU/1974/K27;
RA Mauricio I.L., Stothard J.R., Miles M.A.;
RT "Genetic diversity in the Leishmania donovani complex.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has an integral role during the infection of macrophages in
CC the mammalian host. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preference for hydrophobic residues at P1 and P1' and basic
CC residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-
CC Tyr-|-Leu-Lys-Lys-.; EC=3.4.24.36;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08148};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR EMBL; AJ495008; CAD42817.1; -; Genomic_DNA.
DR EMBL; AJ495009; CAD42818.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8MNZ1; -.
DR SMR; Q8MNZ1; -.
DR MEROPS; M08.001; -.
DR GlyConnect; 334; 2 N-Linked glycans.
DR GlyCosmos; Q8MNZ1; 7 sites, 4 glycans.
DR VEuPathDB; TriTrypDB:LTRL590_280010900; -.
DR BRENDA; 3.4.24.36; 2957.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.170.20; -; 1.
DR Gene3D; 3.90.132.10; Leishmanolysin , domain 2; 1.
DR Gene3D; 2.10.55.10; Leishmanolysin domain 3; 1.
DR Gene3D; 2.30.34.10; Leishmanolysin domain 4; 1.
DR InterPro; IPR001577; Peptidase_M8.
DR PANTHER; PTHR10942; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR PANTHER; PTHR10942:SF0; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
DR PRINTS; PR00782; LSHMANOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell adhesion; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Signal; Transmembrane;
KW Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT PROPEP 42..102
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028672"
FT CHAIN 103..657
FT /note="Leishmanolysin"
FT /id="PRO_0000028673"
FT TOPO_DOM 44..611
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 127..144
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 193..232
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 316..388
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 395..458
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 408..427
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 417..492
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 469..513
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 518..568
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 538..561
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT VARIANT 596..611
FT /note="Missing (in allele mspCLtA2)"
SQ SEQUENCE 657 AA; 70343 MW; 83FBC04757887E51 CRC64;
MSVDSSSSST HRRRCVAARL VRLAAAGAAV TVAVGTAAAW AHAGALQHRC IHDAMQARVR
QSVARHHTAP GAVSAVGLPY VTLDAAHTAA AADPRPGSAP TVVRAANWST LRVAVSTEDL
TDPAYHCARV GQRVNNHAGA IVTCTAEDIL TDEKRDILRK YLIPQALQLH TERLKARQVQ
GKWKVTGMVD EICGDFKVPQ AHITEGFSNT DFVMYVASVP SEEGVLAWAT TCQVFSDGHP
AVGVINIPAA NIASRYDQLV TRVVTHEMAH ALGFSEEFFT AARIVAHVSN VRHKTLKVPV
VNSSTAVAKA REQYGCGTLE YLEIEDQGGA GSAGSHIKMR NAQDELMAPA AAGGYYTALT
MAVFQDLGFY QADFNKAKVM PWGRNAGCAF LSEKCMEQNI TKWRAMFCNE SEDVMRCPTS
RLSLGTCGIR GYRPPLPRYW QYFTNASLGG YSPFMDYCPV VIGYANGSCN QDASSAAEFL
AAFNVFSEAA RCIDGAFTPK NRTAADGYYA GLCANVRCDT ATRTYSVQVR GSMDYVSCTP
GLRVELSTVS NAFEEGGCIT CPPYVEVCQG NVKGAKDFAG DSDSSSSADD AAGKAAMLRW
NDRMVGLATA ATVLLGMVLS LMALVVVWLL LVSCPWWCCK LGGPPASVTP ACSPETE
//
