GP63_CRIFA
ID GP63_CRIFA Reviewed; 653 AA.
AC Q06031;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Leishmanolysin homolog;
DE EC=3.4.24.36;
DE AltName: Full=Cell surface protease;
DE AltName: Full=Major surface glycoprotein;
DE AltName: Full=Protein gp63;
DE Flags: Precursor;
GN Name=gp63;
OS Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11745;
RX PubMed=8426615; DOI=10.1016/0166-6851(93)90242-p;
RA Inverso J.A., Medina-Acosta E., O'Connor J., Russell D.G., Cross G.A.M.;
RT "Crithidia fasciculata contains a transcribed leishmanial surface
RT proteinase (gp63) gene homologue.";
RL Mol. Biochem. Parasitol. 57:47-54(1993).
RN [2]
RP SEQUENCE REVISION TO LEU-122.
RA Inverso J.A., Medina-Acosta E., O'Connor J., Russell D.G., Cross G.A.M.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an integral role during the infection of macrophages in
CC the mammalian host. {ECO:0000250}.
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; M94364; AAA30319.1; -; Genomic_DNA.
DR EMBL; M94365; AAA30320.2; -; Genomic_DNA.
DR PIR; A60961; A60961.
DR AlphaFoldDB; Q06031; -.
DR SMR; Q06031; -.
DR MEROPS; M08.001; -.
DR VEuPathDB; TriTrypDB:CFAC1_040011900; -.
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..44
FT /evidence="ECO:0000255"
FT PROPEP 45..113
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT /id="PRO_0000028652"
FT CHAIN 114..628
FT /note="Leishmanolysin homolog"
FT /id="PRO_0000028653"
FT PROPEP 629..653
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028654"
FT REGION 590..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 628
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
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 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 138..155
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 203..242
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 326..398
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 405..468
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 418..437
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 427..502
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 479..524
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 529..579
FT /evidence="ECO:0000250|UniProtKB:P08148"
FT DISULFID 549..572
FT /evidence="ECO:0000250|UniProtKB:P08148"
SQ SEQUENCE 653 AA; 69171 MW; 263A1DA7568034B6 CRC64;
MHAPPTATRR SGPRRTHGIM ARLVRLAAGV LVVTLVIGAL TALSADDAKT HPHKVCIHDE
LQQSLLDSVA QQGLAPQRVS RVGLPYVASA TAAPAAQVGG VDFALAGDSA PDVTRSAEWG
ELRITVSAEE LTDPAYHCAT VGQVISNHID DYVTCTADDI MTAEKLDILM NYLIPEALQM
HKDRLQVQQV QGTWKVARMT SYCGRFKVPE EHFTTGLSNT DFVLYVASVP TSPGVLAWAN
TCQVFSNDQP AVGVINIPAA TITERYDHLM VHAVTHEIAH SLGFSNAFFT NTGIGQFVTG
VRGNPDTVPV INSPTVVAKA REHYGCDDVT YVELEDAGGS GTMGSHWKIR NAQDELMAGI
SGVAYYTSLT LSAFEDLGYY KANYSNAETM KWGKDVGCAF LTGKCVVDNV TQFPSMYCDK
DENVYRCHTA RLNLGSCEVT DYTFDLPDYL QYFTVPSVGG SADYYDYCPY IVRSPIGSCT
QAASSASPFV SAFNTFSMAS RCIDGTFTPK STGGATVTAH LGMCTNVACN TADKTYSIQV
YGNGAYIPCT PGATISLDTV SDAFEAGGNI TCPPYLEVCQ SNVKGAMDYE SMTNSGSGSS
RPAPVEPSGS GSGSSAATTA PSPTRDGSAA ADRIAPRTAA VALLALAVAA ACV
