Q99317 · MSA2_PLAFC

Function

function

May play a role in the merozoite attachment to the erythrocyte.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Cellular Componentside of membrane
Biological Processcell adhesion

Names & Taxonomy

Protein names

  • Recommended name
    Merozoite surface protein 2
  • Alternative names
    • Merozoite surface antigen 2
      (MSA-2
      )

Gene names

    • Name
      MSP2
    • Synonyms
      MSA2

Organism names

Accessions

  • Primary accession
    Q99317

Subcellular Location

Cell membrane
; Lipid-anchor, GPI-anchor
Note: During host erythrocyte invasion by merozoites, carried into invaded erythrocytes where it is rapidly degraded.

Keywords

Phenotypes & Variants

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000002459021-236Merozoite surface protein 2
Glycosylation22N-linked (GlcNAc...) asparagine
Glycosylation36N-linked (GlcNAc...) asparagine
Glycosylation139N-linked (GlcNAc...) asparagine
Glycosylation211N-linked (GlcNAc...) asparagine
Disulfide bond219↔227
Glycosylation235N-linked (GlcNAc...) asparagine
Lipidation236GPI-anchor amidated asparagine
Glycosylation236N-linked (GlcNAc...) asparagine
PropeptidePRO_0000024591237-262Removed in mature form

Keywords

PTM databases

Expression

Keywords

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias44-64Polar residues
Region44-188Polymorphic region
Region44-223Disordered
Compositional bias81-116Polar residues
Compositional bias125-217Polar residues

Domain

The N-terminal region appears to be involved in lipid binding.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    262
  • Mass (Da)
    27,375
  • Last updated
    1996-10-01 v1
  • Checksum
    72E0B2A315E9D154
MKVIKTLSIINFFIFVTFNIKNESKYSNTFINNAYNMSIRRSMAESKPPTGTGGSGSAGSGAGASAGNGANPGADAERSPSTPATPATPATTTTTTTTNDAEASTSTSSENPNHKNAETNPKGKGEVQKPNQANKETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLNNSSNIASINKFVVLISATLVLSFAIFI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias44-64Polar residues
Compositional bias81-116Polar residues
Compositional bias125-217Polar residues

Polymorphism

The sequence varies across Plasmodium strains (PubMed:2090943).
All variants share conserved N- and C-terminal regions; however, they belong to two allelic families, represented by 3D7 strain and FC27 strain sequences respectively, distinguished by tandem repeats and dimorphic flanking sequences within the central region of the protein (PubMed:2090943).

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M60186
EMBL· GenBank· DDBJ
AAA29687.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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