Q99319 · MSA2_PLAFH
- ProteinMerozoite surface protein 2
- GeneMSP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids281 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
May play a role in the merozoite attachment to the erythrocyte.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Biological Process | cell adhesion |
Names & Taxonomy
Protein names
- Recommended nameMerozoite surface protein 2
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ99319
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor, GPI-anchor
Note: During host erythrocyte invasion by merozoites, carried into invaded erythrocytes where it is rapidly degraded.
Keywords
- Cellular component
Phenotypes & Variants
Keywords
- Disease
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MKVIKTLSIINFFIFVTFNI | ||||||
Chain | PRO_0000024596 | 21-255 | Merozoite surface protein 2 | |||
Sequence: KNESKYSNTFINNAYNMSIRRSMEESNPPTGASGRAGAGASGRAGAGASGRAGAGAGAVASAGSGDGAVASAGNGANPGADAKRSTSTPATTTTTTTTNDAEASTSTSSENPNHNNAKTNPKGKEVQEPNKANTETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLNN | ||||||
Glycosylation | 22 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 36 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 158 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 230 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 238↔246 | |||||
Sequence: CTDGNKENC | ||||||
Glycosylation | 254 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 255 | GPI-anchor amidated asparagine | ||||
Sequence: N | ||||||
Glycosylation | 255 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Propeptide | PRO_0000024597 | 256-281 | Removed in mature form | |||
Sequence: SSNIASINKFVVLISATLVLSFAIFI |
Keywords
- PTM
PTM databases
Expression
Keywords
- Developmental stage
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 42-242 | Disordered | ||||
Sequence: SMEESNPPTGASGRAGAGASGRAGAGASGRAGAGAGAVASAGSGDGAVASAGNGANPGADAKRSTSTPATTTTTTTTNDAEASTSTSSENPNHNNAKTNPKGKEVQEPNKANTETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGN | ||||||
Region | 44-207 | Polymorphic region | ||||
Sequence: EESNPPTGASGRAGAGASGRAGAGASGRAGAGAGAVASAGSGDGAVASAGNGANPGADAKRSTSTPATTTTTTTTNDAEASTSTSSENPNHNNAKTNPKGKEVQEPNKANTETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQS | ||||||
Repeat | 51-58 | 1 | ||||
Sequence: GASGRAGA | ||||||
Region | 51-74 | 3 X 8 AA tandem repeats of G-A-S-G-R-A-G-A | ||||
Sequence: GASGRAGAGASGRAGAGASGRAGA | ||||||
Repeat | 59-66 | 2 | ||||
Sequence: GASGRAGA | ||||||
Repeat | 67-74 | 3 | ||||
Sequence: GASGRAGA | ||||||
Compositional bias | 100-143 | Polar residues | ||||
Sequence: ADAKRSTSTPATTTTTTTTNDAEASTSTSSENPNHNNAKTNPKG | ||||||
Compositional bias | 150-236 | Polar residues | ||||
Sequence: NKANTETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQK |
Domain
The N-terminal region appears to be involved in lipid binding.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length281
- Mass (Da)28,892
- Last updated1996-10-01 v1
- Checksum50598AA42D64CCBC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 100-143 | Polar residues | ||||
Sequence: ADAKRSTSTPATTTTTTTTNDAEASTSTSSENPNHNNAKTNPKG | ||||||
Compositional bias | 150-236 | Polar residues | ||||
Sequence: NKANTETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQK |
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).
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).