GP63_LEIME
ID GP63_LEIME Reviewed; 646 AA.
AC P43150;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Leishmanolysin C1;
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-C1;
OS Leishmania mexicana.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MNYC/BZ/62/M379;
RX PubMed=8426614; DOI=10.1016/0166-6851(93)90241-o;
RA Medina-Acosta E., Karess R.E., Russell D.G.;
RT "Structurally distinct genes for the surface protease of Leishmania
RT mexicana are developmentally regulated.";
RL Mol. Biochem. Parasitol. 57:31-46(1993).
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: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both the promastigote and the
CC amastigote forms.
CC -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR EMBL; X64394; CAA45733.1; -; mRNA.
DR PIR; S19916; S19916.
DR AlphaFoldDB; P43150; -.
DR SMR; P43150; -.
DR MEROPS; M08.001; -.
DR GlyConnect; 338; 2 N-Linked glycans.
DR VEuPathDB; TriTrypDB:LmxM.10.0460; -.
DR BRENDA; 3.4.24.36; 2951.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Signal; Transmembrane;
KW Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT PROPEP 40..102
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028670"
FT CHAIN 103..646
FT /note="Leishmanolysin C1"
FT /id="PRO_0000028671"
FT TOPO_DOM 42..606
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..646
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 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 297
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 433
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"
SQ SEQUENCE 646 AA; 69054 MW; FE448DDC78C10B0A CRC64;
MPVDSSSTHR HRCVAAPLVR LAAAGAAVTV AVGTAAAWAH AGAPQHRCIH DAMQARVLQS
VAAQRMAPSA VSAVGLPYVS VVPVENASTL DYSLSDSTSP GVVRAANWGA LRVAVSAEDL
TDPAYHCARV GQQVNNHAGD IVTCTAEDIL TDEKRDTLVK HLVPQALQLH RERLKVRQVQ
GKWKVTGMAD VICGDFKVPP EHITEGVTNT DFVLYVASVP SEESVLAWAT TCQVFPDGHP
AVGVINIPAA NIASRYDQLV TRVVTHEMAH AVGFSGTFFG AVGIVQEVPH LRRKDFNVSV
ITSSTVVAKA REQYGCNSLE YLEIEDQGGA GSAGSHIKMR NAKDELMAPA ASAGYYTALT
MAVFQDLGFY QADFSKAEEM PWGRNVGCAF LSEKCMAKNV TKWPAMFCNE SAATIRCPTD
RLRVGTCGIT AYNTSLATYW QYFTNASLGG YSPFLDYCPF VVGYRNGSCN QDASTTPDLL
AAFNVFSEAA RCIDGAFTPK NRTAADGYYT ALCANVKCDT ATRTYSVQVR GTNGYANCTP
GLRVKLSSVS DAFEKGGYVT CPPYVEVCQG NVKAAKDFAG DTDSSSSADD AADKEAMQRW
SDRMAALATA TTLLLGMVLS LMALLVVRLL LTSSPWCCCR LGGLPT
