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Protein

Leishmanolysin

Gene

gp63

Organism
Leishmania amazonensis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Has an integral role during the infection of macrophages in the mammalian host.

Catalytic activityi

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-.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi263 – 2631Zinc; catalyticPROSITE-ProRule annotation
Active sitei264 – 2641PROSITE-ProRule annotation
Metal bindingi267 – 2671Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi332 – 3321Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM08.001.

Names & Taxonomyi

Protein namesi
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 namesi
Name:gp63
OrganismiLeishmania amazonensis
Taxonomic identifieri5659 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737Sequence analysisAdd
BLAST
Propeptidei38 – 9962Activation peptideBy similarityPRO_0000028655Add
BLAST
Chaini100 – 574475LeishmanolysinPRO_0000028656Add
BLAST
Propeptidei575 – 59723Removed in mature formBy similarityPRO_0000028657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi124 ↔ 141By similarity
Disulfide bondi190 ↔ 229By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...)Curated
Disulfide bondi313 ↔ 383By similarity
Disulfide bondi390 ↔ 452By similarity
Disulfide bondi403 ↔ 422By similarity
Glycosylationi404 – 4041N-linked (GlcNAc...)Curated
Disulfide bondi412 ↔ 486By similarity
Disulfide bondi463 ↔ 507By similarity
Disulfide bondi512 ↔ 562By similarity
Disulfide bondi532 ↔ 555By similarity
Lipidationi574 – 5741GPI-anchor amidated asparagineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

PTM databases

UniCarbKBiQ27673.

Structurei

3D structure databases

ProteinModelPortaliQ27673.
SMRiQ27673. Positions 99-571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M8 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 1 hit.
PfamiPF01457. Peptidase_M8. 1 hit.
[Graphical view]
PRINTSiPR00782. LSHMANOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q27673-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVDSSSTHR HRCVAARLVP LAAAGAAVTV AVGTAAAWAH AGAVQHRCIH
60 70 80 90 100
DAMQARVRQS VAAQRMAPSA VSAVGLPHVT LDAGNTAAGA DPSTGTANVV
110 120 130 140 150
RAANWGALRI AVSAEDLTDP AYHCARVGQR VNNHVGDIVT CTAEDILTDE
160 170 180 190 200
KRDILVKHLV PQALQLHRER LKVQQVQGKW KVTGMTADVC RYFKVPPAHV
210 220 230 240 250
TGGVTNTDFV LYVASVPSEE SVLAWATTCQ VFADGHPAVG VINIPAANIA
260 270 280 290 300
SRYDQLVTRV VAHEMAHALG FSGTFFDRVG IVQKVPDVRG KPYFTPMINS
310 320 330 340 350
STAVAKAREQ YGCNSLEYLE MEDQGSAAPG SHIKANAQDE LMAPTASAGY
360 370 380 390 400
YTALTMAVFQ DLGFYQADFS KAEAMPWGRN AACAFLSEKC MANGITKWPA
410 420 430 440 450
MFCNESADAI RCPTSRLGVG MCDVTPYQAL PPYLQYFTDP FLAGSSAFMD
460 470 480 490 500
YCPVVVPYAD GSCAQSASEA DAAFKAFNVF SDAAACIDGA FRPKTTHGLI
510 520 530 540 550
KSYAALCANV KCDTAARTYS VQVRGSSGYA NCTPGLRFDL STVSDAFEKG
560 570 580 590
GYVTCPPYVE VCQGNAQAIK DGGNAAGRRG PRAATALVVA ALLAVAL
Length:597
Mass (Da):63,053
Last modified:November 1, 1996 - v1
Checksum:iA3ECA2264CAC0BAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46798 Genomic DNA. Translation: AAA82695.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46798 Genomic DNA. Translation: AAA82695.1.

3D structure databases

ProteinModelPortaliQ27673.
SMRiQ27673. Positions 99-571.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM08.001.

PTM databases

UniCarbKBiQ27673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR001577. Peptidase_M8.
[Graphical view]
PANTHERiPTHR10942. PTHR10942. 1 hit.
PfamiPF01457. Peptidase_M8. 1 hit.
[Graphical view]
PRINTSiPR00782. LSHMANOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MHOM/BR/73/LV78.

Entry informationi

Entry nameiGP63_LEIAM
AccessioniPrimary (citable) accession number: Q27673
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: November 1, 1996
Last modified: January 20, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.