GP63_LEICH
ID GP63_LEICH Reviewed; 599 AA.
AC P15706;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 chagasi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=44271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2320059; DOI=10.1016/0166-6851(90)90065-t;
RA Miller R.A., Reed S.G., Parsons M.;
RT "Leishmania gp63 molecule implicated in cellular adhesion lacks an Arg-Gly-
RT Asp sequence.";
RL Mol. Biochem. Parasitol. 39:267-274(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1370484; DOI=10.1016/s0021-9258(18)46030-9;
RA Ramamoorthy R., Donelson J.E., Paetz K.E., Maybodi M., Roberts S.C.,
RA Wilson M.E.;
RT "Three distinct RNAs for the surface protease gp63 are differentially
RT expressed during development of Leishmania donovani chagasi promastigotes
RT to an infectious form.";
RL J. Biol. Chem. 267:1888-1895(1992).
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; M80672; AAA29238.1; -; mRNA.
DR EMBL; M28527; AAA29235.1; -; Genomic_DNA.
DR PIR; A44951; A44951.
DR AlphaFoldDB; P15706; -.
DR SMR; P15706; -.
DR MEROPS; M08.001; -.
DR BRENDA; 3.4.24.36; 8755.
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 2: Evidence at transcript level;
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..97
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028658"
FT CHAIN 98..574
FT /note="Leishmanolysin"
FT /id="PRO_0000028659"
FT PROPEP 575..599
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028660"
FT ACT_SITE 262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 574
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 122..139
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 188..227
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 311..383
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 390..452
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 403..422
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 412..486
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 463..507
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 512..562
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 532..555
FT /evidence="ECO:0000250|UniProtKB:P08148"
SQ SEQUENCE 599 AA; 63848 MW; 746730AE8E2A2E7C CRC64;
MSVDSSSTHR HRSVAARLVR LAAAGAAVIA AVGTAAAWAH AGAVQHRCIH DAMQARVRQS
VARHHTAPGA VSAVGLPYVT LDTAAAADRR PGSAPTVVRA ANWGALRIAV STEDLTDPAY
HCARVGQHIK RRLGGVDICT AEDILTDEKR DILVKHLIPQ ALQLHTERLK VRQVQDKWKV
TGMGDDVCSD FKVPPAHITD GLSNTDFVMY VASVPSEEGV LAWATTCQVF SDGHPAVGVI
NIPAANIASR YDQLVTRVVT HEMAHALGFS VGFFEGARIL ESISNVRHKD FDVPVINSST
AVAKAREQYG CDTLEYLEIE DQGGAGSAGS HIKMRNAQDE LMAPAAAAGY YSALTMAIFQ
DLGFYQADFS KAEVMPWGRN AGCAFLSEKC MERNITKWPA MFCNENEVTM RCPTSRLSLG
KCGVTRHPDL PPYWQYFTDP SLAGISAFMD CCPVVEPYGD GSCAQRASEA GAPFKGFNVF
SDAARCIDGA FRPKTSHGII KSYAGLCANV RCDTATRTYS VQVHGGSGYA NCTPGLRVEL
STVSSAFEEG GYITCPPYVE VCQGNVQAAK DGGNAAAGRR GPRAAATALL VAALLAVAL
