Reviewed, UniProtKB/Swiss-Prot Q27673 (GP63_LEIAM)

Names and origin

Protein names

Recommended name:
    Leishmanolysin
    EC=3.4.24.36
Alternative name(s):
    Cell surface protease
    Major surface glycoprotein
    Protein gp63
    Promastigote surface endopeptidase
    Major surface protease

Gene names

Name:

gp63

Organism

Leishmania amazonensis

Taxonomic identifier

5659 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmania

Protein attributes

Sequence length	597 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 By similarity.
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 Non-traceable author statement. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
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 protein binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 37	37	Potential
	Propeptide	38 – 99	62	Activation peptide By similarity		PRO_0000028655
	Chain	100 – 574	475	Leishmanolysin		PRO_0000028656
	Propeptide	575 – 597	23	Removed in mature form By similarity		PRO_0000028657
Sites
	Active site	264	1	By similarity
	Metal binding	263	1	Zinc; catalytic By similarity
	Metal binding	267	1	Zinc; catalytic By similarity
	Metal binding	332	1	Zinc; catalytic By similarity
Amino acid modifications
	Lipidation	574	1	GPI-anchor amidated asparagine By similarity
	Glycosylation	299	1	N-linked (GlcNAc...) Probable
	Glycosylation	404	1	N-linked (GlcNAc...) Probable
	Disulfide bond	124 ↔ 141		By similarity
	Disulfide bond	190 ↔ 229		By similarity
	Disulfide bond	313 ↔ 383		By similarity
	Disulfide bond	390 ↔ 452		By similarity
	Disulfide bond	403 ↔ 422		By similarity
	Disulfide bond	412 ↔ 486		By similarity
	Disulfide bond	463 ↔ 507		By similarity
	Disulfide bond	512 ↔ 562		By similarity
	Disulfide bond	532 ↔ 555		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q27673-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A3ECA2264CAC0BAD	FASTA	597	63,053
	10 20 30 40 50 60 MSVDSSSTHR HRCVAARLVP LAAAGAAVTV AVGTAAAWAH AGAVQHRCIH DAMQARVRQS 70 80 90 100 110 120 VAAQRMAPSA VSAVGLPHVT LDAGNTAAGA DPSTGTANVV RAANWGALRI AVSAEDLTDP 130 140 150 160 170 180 AYHCARVGQR VNNHVGDIVT CTAEDILTDE KRDILVKHLV PQALQLHRER LKVQQVQGKW 190 200 210 220 230 240 KVTGMTADVC RYFKVPPAHV TGGVTNTDFV LYVASVPSEE SVLAWATTCQ VFADGHPAVG 250 260 270 280 290 300 VINIPAANIA SRYDQLVTRV VAHEMAHALG FSGTFFDRVG IVQKVPDVRG KPYFTPMINS 310 320 330 340 350 360 STAVAKAREQ YGCNSLEYLE MEDQGSAAPG SHIKANAQDE LMAPTASAGY YTALTMAVFQ 370 380 390 400 410 420 DLGFYQADFS KAEAMPWGRN AACAFLSEKC MANGITKWPA MFCNESADAI RCPTSRLGVG 430 440 450 460 470 480 MCDVTPYQAL PPYLQYFTDP FLAGSSAFMD YCPVVVPYAD GSCAQSASEA DAAFKAFNVF 490 500 510 520 530 540 SDAAACIDGA FRPKTTHGLI KSYAALCANV KCDTAARTYS VQVRGSSGYA NCTPGLRFDL 550 560 570 580 590 STVSDAFEKG GYVTCPPYVE VCQGNAQAIK DGGNAAGRRG PRAATALVVA ALLAVAL

References

[1]

"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." McGwire B.S., Chang K.-P. J. Biol. Chem. 271:7903-7909(1996) [PubMed: 8626468] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MHOM/BR/73/LV78.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L46798 Genomic DNA. Translation: AAA82695.1.
3D structure databases
HSSP	HSSP built from PDB template 1LML based on UniProtKB P08148.
SMR	Q27673. Positions 99-571.
ModBase	Search...
Protein family/group databases
MEROPS	M08.001.
Enzyme and pathway databases
BRENDA	3.4.24.36. 267701.
Family and domain databases
InterPro	IPR006025. Pept_M_Zn_BS. 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_LEIAM

Accession

Primary (citable) accession number: Q27673

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)