P23223 (GP63_LEIDO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leishmanolysin
EC=3.4.24.36

Alternative name(s):
Cell surface protease
Major surface glycoprotein
Major surface protease
Promastigote surface endopeptidase
Protein gp63

Gene names

Name:

gp63

Organism

Leishmania donovani

Taxonomic identifier

5661 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmania

Protein attributes

Sequence length	590 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (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 By similarity.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Sequence similarities	Belongs to the peptidase M8 family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein Zymogen
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 39	39	Potential
	Propeptide	40 – 87	48	Activation peptide		PRO_0000028661
	Chain	88 – 565	478	Leishmanolysin		PRO_0000028662
	Propeptide	566 – 590	25	Removed in mature form By similarity		PRO_0000028663
Sites
	Active site	252	1	By similarity
	Metal binding	251	1	Zinc; catalytic By similarity
	Metal binding	255	1	Zinc; catalytic By similarity
	Metal binding	321	1	Zinc; catalytic By similarity
Amino acid modifications
	Lipidation	565	1	GPI-anchor amidated asparagine By similarity
	Glycosylation	287	1	N-linked (GlcNAc...) Potential
	Disulfide bond	112 ↔ 129		By similarity
	Disulfide bond	178 ↔ 217		By similarity
	Disulfide bond	301 ↔ 373		By similarity
	Disulfide bond	380 ↔ 443		By similarity
	Disulfide bond	393 ↔ 412		By similarity
	Disulfide bond	402 ↔ 477		By similarity
	Disulfide bond	454 ↔ 498		By similarity
	Disulfide bond	503 ↔ 553		By similarity
	Disulfide bond	523 ↔ 546		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23223 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 0FB315D299659F58	FASTA	590	62,950
	10 20 30 40 50 60 MSVDSSSTHR HRSVAARLVR LAAAGAAVIA AVGTAAAWAH AGAVQHRCIH DAMQARVRQS 70 80 90 100 110 120 VARHHTAPGA VSAVGLSYVT LGAAPTVVRA ANWGALRIAV STEDLTDSAY HCARVGQRIS 130 140 150 160 170 180 TRDGRFAICT AEDILTDEKR DILVKYLIPQ ALQLHTERLK VRQVQDKWKV TGMGNEICGH 190 200 210 220 230 240 FKVPPAHITD GLSNTDFVMY VASVPSEGDV LAWATTCQVF SDGHPAVGVI NIPAANIASR 250 260 270 280 290 300 YDQLVTRVVT HEMAHALGFS VVFFRDARIL ESISNVRHKD FDVPVINSST AVAKAREQYG 310 320 330 340 350 360 CGTLEYLEME DQGGAGSAGS HIKMRNAQDE LMAPASDAGY YSALTMAIFQ DLGFYQADFS 370 380 390 400 410 420 KAEEMPWGRN AGCAFLSEKC MEDGITKWPA MFCNENEVTM RCHTGRLSLG VCGLSSSDIP 430 440 450 460 470 480 LPPYWQYFTD PLLAGISAFM DYCPVVVPFG DGSCAQRASE AGAPFKGFNV FSDAARCIDG 490 500 510 520 530 540 AFRPKTTETV TNSYAGLCAN VRCDTATRTY SVQVHGGSGY ANCTPGLRVE LSTVSSAFEE 550 560 570 580 590 GGYITCPPYV EVCQGNVQAA KDGGNAAAGR RGPRAAATAL LVAALLAVAL

References

[1]	"Heterogeneity of the genes encoding the major surface glycoprotein of Leishmania donovani." Webb J.R., Button L.L., McMaster R.W. Mol. Biochem. Parasitol. 48:173-184(1991) [PubMed: 1762629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MHOM/ET/67/HU3 / LV9.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60048 Genomic DNA. Translation: AAA29244.1.
PIR	A45621.
3D structure databases
ProteinModelPortal	P23223.
SMR	P23223. Positions 87-562.
ModBase	Search...
Protein family/group databases
MEROPS	M08.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001577. Peptidase_M8. [Graphical view]
PANTHER	PTHR10942. Peptidase_M8. 1 hit.
Pfam	PF01457. Peptidase_M8. 1 hit. [Graphical view]
PRINTS	PR00782. LSHMANOLYSIN.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GP63_LEIDO

Accession

Primary (citable) accession number: P23223

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)