Q9Y008 · SUB2_PLAFP

Function

function

Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite. May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion.

Catalytic activity

  • Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
    EC:3.4.21.62 (UniProtKB | ENZYME | Rhea)

Activity regulation

Activation may be calcium-dependent. Inhibited by the non-covalent interaction with the cleaved propeptide.

Features

Showing features for active site.

113371002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Active site750Charge relay system
Active site793Charge relay system
Active site956Charge relay system

GO annotations

AspectTerm
Cellular Componentcytoplasmic vesicle
Cellular Componentmicroneme membrane
Cellular Componentplasma membrane
Molecular Functionserine-type endopeptidase activity
Biological Processprotein processing

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Subtilisin-like protease 2
  • EC number
  • Alternative names
    • Merozoite surface sheddase
      (MESH
      )
    • PfSUB2

Gene names

    • Name
      SUB2

Organism names

Accessions

  • Primary accession
    Q9Y008

Subcellular Location

Cell membrane
; Single-pass type I membrane protein
Cytoplasmic vesicle, secretory vesicle, microneme membrane
; Single-pass type I membrane protein
Note: In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:10339607).
Immediately after schizont rupture, secreted from the micronemes to the merozoite surface where it redistributes in an actin-dependent manner to accumulate at the posterior end of newly released merozoites (By similarity).

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain683-1132Extracellular
Transmembrane1133-1153Helical
Topological domain1154-1337Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, glycosylation, chain.

Type
IDPosition(s)Description
Signal1-18
PropeptidePRO_000045075319-682Inhibition peptide
Glycosylation157N-linked (GlcNAc...) asparagine
Glycosylation335N-linked (GlcNAc...) asparagine
Glycosylation445N-linked (GlcNAc...) asparagine
Glycosylation449N-linked (GlcNAc...) asparagine
Glycosylation488N-linked (GlcNAc...) asparagine
Glycosylation546N-linked (GlcNAc...) asparagine
Glycosylation570N-linked (GlcNAc...) asparagine
Glycosylation637N-linked (GlcNAc...) asparagine
ChainPRO_5004337835683-1337Subtilisin-like protease 2
Glycosylation724N-linked (GlcNAc...) asparagine
Glycosylation816N-linked (GlcNAc...) asparagine
Glycosylation852N-linked (GlcNAc...) asparagine
Glycosylation888N-linked (GlcNAc...) asparagine
Glycosylation946N-linked (GlcNAc...) asparagine
Glycosylation1005N-linked (GlcNAc...) asparagine
Glycosylation1101N-linked (GlcNAc...) asparagine

Post-translational modification

Proteolytically cleaved at the N-terminus to generate a 74kDa intermediate which is further processed into a 72kDa form (PubMed:10339607).
The first maturation cleavage is autocatalytic, occurs in the ER and is necessary for the subsequent SUB2 trafficking to the microneme (By similarity).
The second cleavage may be mediated by PMX/plasmepsin X (By similarity).

Keywords

PTM databases

Expression

Developmental stage

Expressed during the parasite blood stage, specifically in schizonts and merozoites (at protein level).

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region85-105Disordered
Region135-163Disordered
Compositional bias143-163Basic and acidic residues
Region407-470Disordered
Compositional bias418-470Polar residues
Compositional bias495-514Basic and acidic residues
Region495-526Disordered
Domain722-1015Peptidase S8

Domain

The propeptide domain acts as an intramolecular chaperone for the folding of the catalytic domain (By similarity).
Also acts as an inhibitor of the catalytic domain thereby regulating SUB2 activity during secretion (By similarity).
The transmembrane domain is required for SUB2 progression through the secretory pathway.
The cytoplasmic domain is required for the correct redistribution at the merozoite surface and posterior capping but is dispensable for its progression through the secretory pathway.

Sequence similarities

Belongs to the peptidase S8 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,337
  • Mass (Da)
    154,394
  • Last updated
    1999-11-01 v1
  • Checksum
    42B900BE2E8FC1A4
MLNIIYVVSLILIKFIFYKECNNNNNNYLSNIELYNYKLRKRNRILNNNINDRKSFLSDLEQNYKPLFDIYELSANFEKRRKELEKKTKGEENEIEKKKENDLEKKKENDLEKEYNDVINLLELSLSSEYKELNADVSNNDNSGHEENNKHKLNKKNSSNYKNDKSLDELIKGAILKLKQNPNIKNKNMLDYDKIFKIIKEKLINKNLASNKIRGGDNEKLKEEKKQSDISTNVEVKKDIINDQLNKGIPTKKENKDDMINKESNKEDITNEGKSNSLNNLNTLNNDGNIITKVYDHYTIVTNSNDILNDISIDASDISKNSIGGINIPFNENDNSSFTHQRYIVLSNNGEKKYKIVLMTKNPKFMDMDGIYDEEEKKESLIELNQKVNKEENTNLYDGTGTLYYGKKSKKEKENTQQKGGNNPNVDINILNNNNNNNNNNNNNNNSNNNSNSMNDEEINYNNNNNNKESPSMFRRFINFLSFSGNENETEDTLIYHNKNDNSYKNKKEGTGKNNDNNDPNNNNNKKILLNVDKLVDQYLLNLKNNHTSKQELILVLKGELDLHSKNMKNVTNNAKKNLEKYFKEHFKEFDKISYDISTPINFLCIFIPTVFDMNNMDLLKQALLILHSDLHEYVENWSFSSTYHTYEADYIKEQDSVYDRSPKKKYIKASKKLYNNKYSFLNKFLNIEPLILFAKKLNSKRSNIEKEILNFLPKELRDYSTWNLSIIRVFNAWFLAGYGNKNVKVCVVDSGADINRVDLNGNLYIPEYNEKYEMTQDFYNFMVKKSYRCLGHGSHVTGIIGGVANDLGVVGVAPNITLISLRFIDGKKYGGSFHAIKALNVCILNKAPIINASWGSSHFDVNLHLTVERLKYTLNGKGSVLIAASGNKSNDNDISPLYPATFTFPHVYSVASISRNFEISPFSNYGYKSVHILAPGHHIYSTIPNNSYKIFTGTSMAAPHVCGVSALVYSVCYNQGFIPQAEEVLDILTRTSIKIISTKKRTINDSLVNAEGAVLTTLLGGLWMQMDCYFVKFNLEKGKKKHIPVVFSAYKKGVYETDIVIAIIPIDGKSKIYGEIHIPIKIVTDVNIPNFQESPRRGKNYTIDSNEAQHDEVLSYICENALYNLYEYDSHYLLASVILFFLALLSIFVGMIYMKSRKHSDKKCSKNLIKSNYIPEMDDGMEETQQLQQERRQYFRELFGENLEKNYDQHFVQDFGQDFRQDFKLGSTPDLKQYSDIDLQNKIQQPERKTVKIIINNFEDRKKETIRRLLKGLNYDGENAKKHDFTNESISNSRKNFKFSNNTEMKKNTIKSEDVKIASDDNVNKAMNQLDDMFMK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias143-163Basic and acidic residues
Compositional bias418-470Polar residues
Compositional bias495-514Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ132006
EMBL· GenBank· DDBJ
CAB43592.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp