ID   GP63_LEIMA     STANDARD;      PRT;   602 AA.
AC   P08148; P15906;
DT   01-AUG-1988 (REL. 08, CREATED)
DT   01-APR-1990 (REL. 14, LAST SEQUENCE UPDATE)
DT   01-NOV-1998 (REL. 37, 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 MAJOR.
OC   EUKARYOTA; PROTOZOA; SARCOMASTIGOPHORA; MASTIGOPHORA; KINETOPLASTIDA;
OC   TRYPANOSOMATIDAE.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 101-123.
RX   MEDLINE; 88154764.
RA   BUTTON L.L., MCMASTER W.R.;
RL   J. EXP. MED. 167:724-729(1988).
RN   [2]
RP   REVISIONS.
RA   BUTTON L.L., MCMASTER W.R.;
RL   J. EXP. MED. 171:589-589(1990).
RN   [3]
RP   GPI-ANCHOR.
RX   MEDLINE; 91009116.
RA   SCHNEIDER P., FERGUSON M.A.J., MCCONVILLE M.J., MEHLERT A.,
RA   HOMANS S.W., BORDIER C.;
RL   J. BIOL. CHEM. 265:16955-16964(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   MEDLINE; 95406217.
RA   SCHLAGENHAUF E., ETGES R., METCALF P.;
RL   PROTEINS 22:58-66(1995).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RA   SCHLAGENHAUF E., ETGES R., METCALF P.;
RL   SUBMITTED (MAR-1997) TO THE PDB DATA BANK.
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   -!- PTM: THE PHOSPHATIDYLINOSITOL MOIETY OF THE GPI-ANCHOR CONTAINS A
CC       FULLY SATURATED, UNBRANCHED 1-O-ALKYL CHAIN (MAINLY C24:0) AND A
CC       MIXTURE OF FULLY SATURATED UNBRANCHED 2-O-ACYL CHAINS (C12:0,
CC       C14:0, C16:0, AND C18:0).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M8 (ZINC METALLOPROTEASE);
CC       ALSO KNOWN AS THE LEISHMANOLYSIN SUBFAMILY.
CC   --------------------------------------------------------------------------
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DR   EMBL; Y00647; G9555; -.
DR   PIR; A27598; A27598.
DR   PIR; PL0221; PL0221.
DR   PDB; 1LML; 17-SEP-97.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
KW   HYDROLASE; METALLOPROTEASE; GLYCOPROTEIN; ZINC; ZYMOGEN; SIGNAL;
KW   CELL ADHESION; GPI-ANCHOR; 3D-STRUCTURE.
FT   SIGNAL        1     39       POTENTIAL.
FT   PROPEP       40    100       ACTIVATION PEPTIDE.
FT   CHAIN       101    577       LEISHMANOLYSIN.
FT   PROPEP      578    602       REMOVED IN MATURE FORM.
FT   METAL       264    264       ZINC (CATALYTIC).
FT   ACT_SITE    265    265
FT   METAL       268    268       ZINC (CATALYTIC).
FT   CARBOHYD    300    300       POTENTIAL.
FT   CARBOHYD    407    407       POTENTIAL.
FT   LIPID       577    577       GPI-ANCHOR.
SQ   SEQUENCE   602 AA;  63953 MW;  585DA140 CRC32;
     MSVDSSSTHR RRCVAARLVR LAAAGAAVTV AVGTAAAWAH AGALQHRCVH DAMQARVRQS
     VADHHKAPGA VSAVGLPYVT LDAAHTAAAA DPRPGSARSV VRDVNWGALR IAVSTEDLTD
     PAYHCARVGQ HVKDHAGAIV TCTAEDILTN EKRDILVKHL IPQAVQLHTE RLKVQQVQGK
     WKVTDMVGDI CGDFKVPQAH ITEGFSNTDF VMYVASVPSE EGVLAWATTC QTFSDGHPAV
     GVINIPAANI ASRYDQLVTR VVTHEMAHAL GFSGPFFEDA RIVANVPNVR GKNFDVPVIN
     SSTAVAKARE QYGCDTLEYL EVEDQGGAGS AGSHIKMRNA QDELMAPAAA AGYYTALTMA
     IFQDLGFYQA DFSKAEVMPW GQNAGCAFLT NKCMEQSVTQ WPAMFCNESE DAIRCPTSRL
     SLGACGVTRH PGLPPYWQYF TDPSLAGVSA FMDYCPVVVP YSDGSCTQRA SEAHASLLPF
     NVFSDAARCI DGAFRPKATD GIVKSYAGLC ANVQCDTATR TYSVQVHGSN DYTNCTPGLR
     VELSTVSNAF EGGGYITCPP YVEVCQGNVQ AAKDGGNTAA GRRGPRAAAT ALLVAALLAV
     AL
//