GP63_LEIAM
ID GP63_LEIAM Reviewed; 597 AA.
AC Q27673;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 amazonensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5659;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/BR/73/LV78;
RX PubMed=8626468; DOI=10.1074/jbc.271.14.7903;
RA McGwire B.S., Chang K.-P.;
RT "Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63).
RT The effects of site-specific mutagenesis of catalytic, zinc binding, N-
RT glycosylation, and glycosyl phosphatidylinositol addition sites on N-
RT terminal end cleavage, intracellular stability, and extracellular exit.";
RL J. Biol. Chem. 271:7903-7909(1996).
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 {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR EMBL; L46798; AAA82695.1; -; Genomic_DNA.
DR AlphaFoldDB; Q27673; -.
DR SMR; Q27673; -.
DR MEROPS; M08.001; -.
DR GlyConnect; 337; 4 N-Linked glycans.
DR VEuPathDB; TriTrypDB:LAMA_000560400; -.
DR BRENDA; 3.4.24.36; 2945.
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..99
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028655"
FT CHAIN 100..574
FT /note="Leishmanolysin"
FT /id="PRO_0000028656"
FT PROPEP 575..597
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028657"
FT ACT_SITE 264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 332
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 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 124..141
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 190..229
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 313..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 597 AA; 63053 MW; A3ECA2264CAC0BAD CRC64;
MSVDSSSTHR HRCVAARLVP LAAAGAAVTV AVGTAAAWAH AGAVQHRCIH DAMQARVRQS
VAAQRMAPSA VSAVGLPHVT LDAGNTAAGA DPSTGTANVV RAANWGALRI AVSAEDLTDP
AYHCARVGQR VNNHVGDIVT CTAEDILTDE KRDILVKHLV PQALQLHRER LKVQQVQGKW
KVTGMTADVC RYFKVPPAHV TGGVTNTDFV LYVASVPSEE SVLAWATTCQ VFADGHPAVG
VINIPAANIA SRYDQLVTRV VAHEMAHALG FSGTFFDRVG IVQKVPDVRG KPYFTPMINS
STAVAKAREQ YGCNSLEYLE MEDQGSAAPG SHIKANAQDE LMAPTASAGY YTALTMAVFQ
DLGFYQADFS KAEAMPWGRN AACAFLSEKC MANGITKWPA MFCNESADAI RCPTSRLGVG
MCDVTPYQAL PPYLQYFTDP FLAGSSAFMD YCPVVVPYAD GSCAQSASEA DAAFKAFNVF
SDAAACIDGA FRPKTTHGLI KSYAALCANV KCDTAARTYS VQVRGSSGYA NCTPGLRFDL
STVSDAFEKG GYVTCPPYVE VCQGNAQAIK DGGNAAGRRG PRAATALVVA ALLAVAL
