GP63_LEIDO
ID GP63_LEIDO Reviewed; 590 AA.
AC P23223;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=gp63;
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/ET/67/HU3 / LV9;
RX PubMed=1762629; DOI=10.1016/0166-6851(91)90113-k;
RA Webb J.R., Button L.L., McMaster R.W.;
RT "Heterogeneity of the genes encoding the major surface glycoprotein of
RT Leishmania donovani.";
RL Mol. Biochem. Parasitol. 48:173-184(1991).
CC -!- FUNCTION: Has an integral role during the infection of macrophages in
CC the mammalian host.
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: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR EMBL; M60048; AAA29244.1; -; Genomic_DNA.
DR PIR; A45621; A45621.
DR AlphaFoldDB; P23223; -.
DR SMR; P23223; -.
DR MEROPS; M08.001; -.
DR GlyConnect; 336; 2 N-Linked glycans.
DR VEuPathDB; TriTrypDB:LdBPK_100510.1; -.
DR VEuPathDB; TriTrypDB:LdBPK_280600.1; -.
DR VEuPathDB; TriTrypDB:LdCL_100011600; -.
DR VEuPathDB; TriTrypDB:LDHU3_10.0760; -.
DR BRENDA; 3.4.24.36; 2947.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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 InterPro; IPR001577; Peptidase_M8.
DR PANTHER; PTHR10942; PTHR10942; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
DR PRINTS; PR00782; LSHMANOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT PROPEP 40..87
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028661"
FT CHAIN 88..565
FT /note="Leishmanolysin"
FT /id="PRO_0000028662"
FT PROPEP 566..590
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028663"
FT ACT_SITE 252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 565
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 112..129
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 178..217
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 301..373
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 380..443
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 393..412
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 402..477
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 454..498
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 503..553
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 523..546
FT /evidence="ECO:0000250|UniProtKB:P08148"
SQ SEQUENCE 590 AA; 62950 MW; 0FB315D299659F58 CRC64;
MSVDSSSTHR HRSVAARLVR LAAAGAAVIA AVGTAAAWAH AGAVQHRCIH DAMQARVRQS
VARHHTAPGA VSAVGLSYVT LGAAPTVVRA ANWGALRIAV STEDLTDSAY HCARVGQRIS
TRDGRFAICT AEDILTDEKR DILVKYLIPQ ALQLHTERLK VRQVQDKWKV TGMGNEICGH
FKVPPAHITD GLSNTDFVMY VASVPSEGDV LAWATTCQVF SDGHPAVGVI NIPAANIASR
YDQLVTRVVT HEMAHALGFS VVFFRDARIL ESISNVRHKD FDVPVINSST AVAKAREQYG
CGTLEYLEME DQGGAGSAGS HIKMRNAQDE LMAPASDAGY YSALTMAIFQ DLGFYQADFS
KAEEMPWGRN AGCAFLSEKC MEDGITKWPA MFCNENEVTM RCHTGRLSLG VCGLSSSDIP
LPPYWQYFTD PLLAGISAFM DYCPVVVPFG DGSCAQRASE AGAPFKGFNV FSDAARCIDG
AFRPKTTETV TNSYAGLCAN VRCDTATRTY SVQVHGGSGY ANCTPGLRVE LSTVSSAFEE
GGYITCPPYV EVCQGNVQAA KDGGNAAAGR RGPRAAATAL LVAALLAVAL
