[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 101-123. DOI=10.1084/jem.167.2.724; PubMed=3346625 [NCBI, ExPASy, EBI, Israel, Japan] Button L.L., McMaster W.R.; "Molecular cloning of the major surface antigen of leishmania."; J. Exp. Med. 167:724-729(1988).
[2]	SEQUENCE REVISION. Button L.L., McMaster W.R.; J. Exp. Med. 171:589-589(1990).
[3]	GPI-ANCHOR AT ASN-577. PubMed=2145267 [NCBI, ExPASy, EBI, Israel, Japan] Schneider P., Ferguson M.A.J., McConville M.J., Mehlert A., Homans S.W., Bordier C.; "Structure of the glycosyl-phosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease."; J. Biol. Chem. 265:16955-16964(1990).
[4]	MUTAGENESIS OF TYR-254; HIS-264; GLU-265; HIS-268; ASN-300; ASN-407; ASN-534 AND ASN-577. DOI=10.1074/jbc.271.14.7903; PubMed=8626468 [NCBI, ExPASy, EBI, Israel, Japan] McGwire B.S., Chang K.-P.; "Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63). The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit."; J. Biol. Chem. 271:7903-7909(1996).
[5]	GLYCOSYLATION AT ASN-300 AND ASN-407. DOI=10.1016/S0166-6851(96)02780-6; PubMed=9041519 [NCBI, ExPASy, EBI, Israel, Japan] Funk V.A., Thomas-Oates J.E., Kielland S.L., Bates P.A., Olafson R.W.; "A unique, terminally glucosylated oligosaccharide is a common feature on Leishmania cell surfaces."; Mol. Biochem. Parasitol. 84:33-48(1997).
[6]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-300; ASN-407 AND ASN-534. DOI=10.1002/prot.340220109; PubMed=7675788 [NCBI, ExPASy, EBI, Israel, Japan] Schlagenhauf E., Etges R., Metcalf P.; "Crystallization and preliminary X-ray diffraction studies of leishmanolysin, the major surface metalloproteinase from Leishmania major."; Proteins 22:58-66(1995).
[7]	X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS). DOI=10.1016/S0969-2126(98)00104-X; PubMed=9739094 [NCBI, ExPASy, EBI, Israel, Japan] Schlagenhauf E., Etges R., Metcalf P.; "The crystal structure of the Leishmania major surface proteinase leishmanolysin."; Structure 6:1035-1046(1998).

Comments

FUNCTION: Has an integral role during the infection of macrophages in the mammalian host.
CATALYTIC ACTIVITY: Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
COFACTOR: Binds 1 zinc ion per subunit.
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
PTM: The phosphatidylinositol moiety of the GPI-anchor contains a fully saturated, unbranched 1-O-alkyl chain (mainly C24:0) and a mixture of fully saturated unbranched 2-O-acyl chains (C12:0, C14:0, C16:0, and C18:0).
SIMILARITY: Belongs to the peptidase M8 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y00647; CAA68673.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

PL0221; PL0221.

3D structure databases

PDB

1LML; X-ray; 1.86 A; A=100-577.

[ExPASy / RCSB / EBI]

PDBsum

1LML; -.

ModBase

P08148.

Protein family/group databases

MEROPS

M08.001; -.

PTM databases

GlycoSuiteDB

P08148; -.

Ontologies

GO:0031225;	Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006025; Pept_M_Zn_BS.
IPR001577; Peptidase_M8.
Graphical view of domain structure.

PANTHER

PTHR10942; Peptidase_M8; 1.

Pfam

PF01457; Peptidase_M8; 1.
Pfam graphical view of domain structure.

PRINTS

PR00782; LSHMANOLYSIN.

PROSITE

PS00142; ZINC_PROTEASE; 1.

Other

P08148; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease; Signal; Zinc; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 39`	`39`	`Potential.`
`PROPEP`	`40 100`	`61`	`Activation peptide.`	`PRO_0000028667`
`CHAIN`	`101 577`	`477`	`Leishmanolysin.`	`PRO_0000028668`
`PROPEP`	`578 602`	`25`	`Removed in mature form.`	`PRO_0000028669`
`ACT_SITE`	`265 265`
`METAL`	`264 264`		`Zinc; catalytic.`
`METAL`	`268 268`		`Zinc; catalytic.`
`METAL`	`334 334`		`Zinc; catalytic.`
`LIPID`	`577 577`		`GPI-anchor amidated asparagine.`
`CARBOHYD`	`300 300`		`N-linked (GlcNAc...).`
`CARBOHYD`	`407 407`		`N-linked (GlcNAc...).`
`CARBOHYD`	`534 534`		`N-linked (GlcNAc...).`
`DISULFID`	`125 142`
`DISULFID`	`191 230`
`DISULFID`	`314 386`
`DISULFID`	`393 455`
`DISULFID`	`406 425`
`DISULFID`	`415 489`
`DISULFID`	`466 510`
`DISULFID`	`515 565`
`DISULFID`	`535 558`
`MUTAGEN`	`254 254`		`Y->D: No significant effect on protein expression levels or catalytic activity.`
`MUTAGEN`	`264 264`		`H->F,Y: No detectable overexpression of mutant protein and hence little catalytic activity.`
`MUTAGEN`	`265 265`		`E->D: No significant effect on protein expression levels but almost abolishes catalytic activity.`
`MUTAGEN`	`268 268`		`H->N,Y: No detectable overexpression of mutant protein and hence little catalytic activity.`
`MUTAGEN`	`300 300`		`N->Q: Increases electrophoretic mobility of the protein.`
`MUTAGEN`	`407 407`		`N->Q: Increases electrophoretic mobility of the protein.`
`MUTAGEN`	`534 534`		`N->Q: Increases electrophoretic mobility of the protein.`
`MUTAGEN`	`577 577`		`N->L: Causes extracellular release of the protein.`
`STRAND`	`111 114`	`4`
`HELIX`	`116 119`	`4`
`STRAND`	`131 133`	`3`
`STRAND`	`135 137`	`3`
`STRAND`	`139 141`	`3`
`HELIX`	`144 146`	`3`
`HELIX`	`150 158`	`9`
`HELIX`	`160 169`	`10`
`STRAND`	`172 174`	`3`
`STRAND`	`177 181`	`5`
`HELIX`	`191 193`	`3`
`HELIX`	`198 202`	`5`
`STRAND`	`205 207`	`3`
`STRAND`	`209 215`	`7`
`STRAND`	`226 232`	`7`
`STRAND`	`238 244`	`7`
`HELIX`	`247 249`	`3`
`HELIX`	`256 269`	`14`
`HELIX`	`274 279`	`6`
`STRAND`	`283 287`	`5`
`HELIX`	`289 291`	`3`
`STRAND`	`296 299`	`4`
`HELIX`	`302 312`	`11`
`STRAND`	`320 322`	`3`
`TURN`	`328 332`	`5`
`STRAND`	`333 335`	`3`
`TURN`	`337 339`	`3`
`STRAND`	`346 348`	`3`
`HELIX`	`356 364`	`9`
`HELIX`	`372 374`	`3`
`TURN`	`380 383`	`4`
`HELIX`	`386 390`	`5`
`STRAND`	`393 395`	`3`
`STRAND`	`398 400`	`3`
`TURN`	`402 404`	`3`
`STRAND`	`420 425`	`6`
`HELIX`	`435 437`	`3`
`STRAND`	`440 442`	`3`
`TURN`	`450 454`	`5`
`STRAND`	`458 465`	`8`
`HELIX`	`470 472`	`3`
`TURN`	`475 477`	`3`
`HELIX`	`478 480`	`3`
`STRAND`	`487 494`	`8`
`STRAND`	`506 516`	`11`
`TURN`	`517 520`	`4`
`STRAND`	`521 525`	`5`
`STRAND`	`540 542`	`3`
`HELIX`	`543 545`	`3`
`STRAND`	`548 550`	`3`
`STRAND`	`555 557`	`3`
`HELIX`	`561 565`	`5`
`HELIX`	`569 572`	`4`

Sequence information

Length: 602 AA [This is the length of the unprocessed precursor]

Molecular weight: 63953 Da [This is the MW of the unprocessed precursor]

CRC64: 982EF3245D87C43E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVDSSSTHR RRCVAARLVR LAAAGAAVTV AVGTAAAWAH AGALQHRCVH DAMQARVRQS 

        70         80         90        100        110        120 
VADHHKAPGA VSAVGLPYVT LDAAHTAAAA DPRPGSARSV VRDVNWGALR IAVSTEDLTD 

       130        140        150        160        170        180 
PAYHCARVGQ HVKDHAGAIV TCTAEDILTN EKRDILVKHL IPQAVQLHTE RLKVQQVQGK 

       190        200        210        220        230        240 
WKVTDMVGDI CGDFKVPQAH ITEGFSNTDF VMYVASVPSE EGVLAWATTC QTFSDGHPAV 

       250        260        270        280        290        300 
GVINIPAANI ASRYDQLVTR VVTHEMAHAL GFSGPFFEDA RIVANVPNVR GKNFDVPVIN 

       310        320        330        340        350        360 
SSTAVAKARE QYGCDTLEYL EVEDQGGAGS AGSHIKMRNA QDELMAPAAA AGYYTALTMA 

       370        380        390        400        410        420 
IFQDLGFYQA DFSKAEVMPW GQNAGCAFLT NKCMEQSVTQ WPAMFCNESE DAIRCPTSRL 

       430        440        450        460        470        480 
SLGACGVTRH PGLPPYWQYF TDPSLAGVSA FMDYCPVVVP YSDGSCTQRA SEAHASLLPF 

       490        500        510        520        530        540 
NVFSDAARCI DGAFRPKATD GIVKSYAGLC ANVQCDTATR TYSVQVHGSN DYTNCTPGLR 

       550        560        570        580        590        600 
VELSTVSNAF EGGGYITCPP YVEVCQGNVQ AAKDGGNTAA GRRGPRAAAT ALLVAALLAV 


AL

P08148 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools