GP63_LEIGU
ID GP63_LEIGU Reviewed; 621 AA.
AC Q00689;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 guyanensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania guyanensis species complex.
OX NCBI_TaxID=5670;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1625703; DOI=10.1016/0166-6851(92)90045-l;
RA Steinkraus H.B., Langer P.J.;
RT "The protein sequence predicted from a Leishmania guyanensis gp63 major
RT surface glycoprotein gene is divergent as compared with other Leishmania
RT species.";
RL Mol. Biochem. Parasitol. 52:141-144(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; M85203; AAA29240.1; -; mRNA.
DR AlphaFoldDB; Q00689; -.
DR SMR; Q00689; -.
DR MEROPS; M08.001; -.
DR BRENDA; 3.4.24.36; 15260.
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..37
FT /evidence="ECO:0000255"
FT PROPEP 38..98
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028664"
FT CHAIN 99..579
FT /note="Leishmanolysin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028665"
FT PROPEP 580..621
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028666"
FT ACT_SITE 263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 579
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 123..140
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 189..228
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 312..384
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 391..454
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 404..423
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 413..488
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 465..508
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 513..563
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 533..556
FT /evidence="ECO:0000250|UniProtKB:P08148"
SQ SEQUENCE 621 AA; 66930 MW; D49AA95C1221BC6D CRC64;
MSRDRSSTHR RRSVAARLIG FAAAGLVMAV GAAAVWAQAA GHHCIHDRLQ ARVLQSVAQQ
RSVPAAFSAL GLPYVSTGTI SSAHTVDWAL ADSTSPSVAR AADWGTLRIA VSTADLTDPG
YHCTRVGQRV NNHNGEIVTC TAEDVLTEEK RDILVSYLIP QALQLHAERL KVRQVQGSWK
VTGMTGSICG DFSVPTAHLT AGVTNADFVL YVASVPSEPG VLAWATTCQV FSDDHPAVGV
INIPAANIVS RYDQGATRVV THEVAHALGF SSTFFKSAGI VKSVTNLRGK PFAAPVINSS
TVVAKAREQY GCPTLEYLEV EDQGGSGSAG SHIKMRNAKD ELMAPASAAG YYTALTMAVF
EDLGFYKADF TKAEVMPWGR NASCDFLTKK CMENNITQWP EMFCNTTERR YRCPTDRLRL
GTCGIRTYST PMPPYFEYFN DTFLAGYSAF LDYCPFTLGY SNGACNQDPS TAPALLKEFS
VFSDASRCLD GAFQPTTARE VLMYNALCAN VMCDTAARTY SVQVRGSSGY VACTPGQRVE
LATLSAAFVN GSYITCPPYV EVCQANIKGV IDFEGDAADT AAMRRWRERM TALATVTAAL
LGIVLAAMAI LVVWLLLITI P
