ID   GP63_LEIDO     STANDARD;      PRT;   590 AA.
AC   P23223;
DT   01-NOV-1991 (REL. 20, CREATED)
DT   01-NOV-1991 (REL. 20, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   LEISHMANOLYSIN PRECURSOR (EC 3.4.24.36) (CELL SURFACE PROTEASE)
DE   (MAJOR SURFACE GLYCOPROTEIN) (GP63 PROTEIN) (PROMASTIGOTE SURFACE
DE   ENDOPEPTIDASE).
GN   GP63.
OS   LEISHMANIA DONOVANI.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; KINETOPLASTIDA;
OC   TRYPANOSOMATIDAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=LV9;
RX   MEDLINE; 92107220.
RA   WEBB J.R., BUTTON L.L., MCMASTER R.W.;
RL   MOL. BIOCHEM. PARASITOL. 48:173-184(1991).
CC   -!- FUNCTION: HAS AN INTEGRAL ROLE DURING THE INFECTION OF MACROPHAGES
CC       IN THE MAMMALIAN HOST.
CC   -!- CATALYTIC ACTIVITY: PREFERENCE FOR HYDROPHOBIC RESIDUES AT P1 AND
CC       P1' AND BASIC RESIDUES AT P2 AND P3'. A MODEL NONAPEPTIDE IS
CC       CLEAVED AT -ALA-TYR-|-LEU-LYS-LYS-.
CC   -!- COFACTOR: BINDS AND REQUIRES A ZINC ATOM, WHICH IS ESSENTIAL FOR
CC       PROTEOLYTIC ACTIVITY.
CC   -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M8 (ZINC METALLOPROTEASE);
CC       ALSO KNOWN AS THE LEISHMANOLYSIN SUBFAMILY.
DR   EMBL; M60048; G159335; -.
DR   PIR; A45621; A45621.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
KW   HYDROLASE; METALLOPROTEASE; GLYCOPROTEIN; ZINC; ZYMOGEN; SIGNAL;
KW   CELL ADHESION; GPI-ANCHOR.
FT   SIGNAL        1     39       POTENTIAL.
FT   PROPEP       40     87       ACTIVATION PEPTIDE.
FT   CHAIN        88    565       LEISHMANOLYSIN.
FT   PROPEP      566    590       REMOVED IN MATURE FORM (BY SIMILARITY).
FT   METAL       251    251       ZINC (CATALYTIC) (BY SIMILARITY).
FT   ACT_SITE    252    252       BY SIMILARITY.
FT   METAL       255    255       ZINC (CATALYTIC) (BY SIMILARITY).
FT   CARBOHYD    287    287       POTENTIAL.
FT   LIPID       565    565       GPI-ANCHOR (BY SIMILARITY).
SQ   SEQUENCE   590 AA;  62950 MW;  49322942 CRC32;
     MSVDSSSTHR HRSVAARLVR LAAAGAAVIA AVGTAAAWAH AGAVQHRCIH DAMQARVRQS
     VARHHTAPGA VSAVGLSYVT LGAAPTVVRA ANWGALRIAV STEDLTDSAY HCARVGQRIS
     TRDGRFAICT AEDILTDEKR DILVKYLIPQ ALQLHTERLK VRQVQDKWKV TGMGNEICGH
     FKVPPAHITD GLSNTDFVMY VASVPSEGDV LAWATTCQVF SDGHPAVGVI NIPAANIASR
     YDQLVTRVVT HEMAHALGFS VVFFRDARIL ESISNVRHKD FDVPVINSST AVAKAREQYG
     CGTLEYLEME DQGGAGSAGS HIKMRNAQDE LMAPASDAGY YSALTMAIFQ DLGFYQADFS
     KAEEMPWGRN AGCAFLSEKC MEDGITKWPA MFCNENEVTM RCHTGRLSLG VCGLSSSDIP
     LPPYWQYFTD PLLAGISAFM DYCPVVVPFG DGSCAQRASE AGAPFKGFNV FSDAARCIDG
     AFRPKTTETV TNSYAGLCAN VRCDTATRTY SVQVHGGSGY ANCTPGLRVE LSTVSSAFEE
     GGYITCPPYV EVCQGNVQAA KDGGNAAAGR RGPRAAATAL LVAALLAVAL
//