Q8ILT5 · SEY1_PLAF7
- ProteinProtein SEY1 homolog
- GeneSEY1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids937 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Probable GTP-binding protein involved in generating and maintaining the structure of the tubular endoplasmic reticulum network.
Features
Showing features for binding site.
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 | endoplasmic reticulum membrane | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein SEY1 homolog
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8ILT5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-848 | Cytoplasmic | ||||
Sequence: MEKGVEKTQIIDYDGNVIEDLKEWMIDNKLNDLGFSYNVIAVLGSQSSGKSTLLNNLFKTSFDVMNTKQGHSQTTKGLWLSYDKFDDETNNSSSFFKLKKKNKPTLILDVEGTDSKERGDNRLTFEHRSALFCLALADCVIVNLWYHSLGNFTASNYGLLKTVMEVNLELFQQEKNSPKTILLFTVRDWFEEFAPIEVVRNKILDEYINKIWKEMKKPKEAEKLNINNFFIIEVVGLSHGIIKKEDFLKDVNNLRDKWINNLRPSKYSRNIPSDGFAQYCNNIWNTIVKQSQLDIPSQKEMLSTFRCQEIKNNVINNINKEIKEKSIESHNKVIENFKEWAEKNIIQKCLDDYFKDASRYKENICLRTSQELLDYLFTQLQAIVDNNLQYIQRTLCTKFFNELSNMYKICTIEKNTFSFSRDSNLKTVKDNNKNTSHEDIKRDLLNNNQDKCVHLWSNFLYNADKLEYFTFCNFYENYEKSNIEIKTNMKNDDNLKNDDNLKNDAHNNITTHQFNYKPTLSVLSTSIYKDSNRIRNIQCGILLNKTRQTIKNSFKNMDTYLLTTKNTEEYWNNTVQLVLKLQDNINTHLTKCFINLKGTNHNNLNIYNDDMMYNNDDMVFNNNDDDDNNNNNNNNNYYYYNKNDDANLSKDENYNNKFSFSLTNEKGIFQNINNNNEGSDEICYTNALKKIDLIKNKQVYKSTINEDINNKLQNKKYIHELKNYYLDEIMDVLKNKLDEISENLATIIIQRFESVFNYDEYEQPRQWRDISMAELKKIFLKSKNYAFLIIDILQKNIKVELIDDYLPNNFIKDEIIEKGKIKAKRRIQEICRDAQYIQETGSKMSLKN | ||||||
Transmembrane | 849-869 | Helical | ||||
Sequence: VPVVFWIILLLFGWNEILFFI | ||||||
Topological domain | 870-872 | Lumenal | ||||
Sequence: RMF | ||||||
Transmembrane | 873-893 | Helical | ||||
Sequence: FKLNVILPLFFAAAFIVSTFV | ||||||
Topological domain | 894-937 | Cytoplasmic | ||||
Sequence: YNGNTQALSYINKIIFYMAKNSYNFFKHIQAISNPPPKNVQKQE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000384955 | 1-937 | UniProt | Protein SEY1 homolog | |||
Sequence: MEKGVEKTQIIDYDGNVIEDLKEWMIDNKLNDLGFSYNVIAVLGSQSSGKSTLLNNLFKTSFDVMNTKQGHSQTTKGLWLSYDKFDDETNNSSSFFKLKKKNKPTLILDVEGTDSKERGDNRLTFEHRSALFCLALADCVIVNLWYHSLGNFTASNYGLLKTVMEVNLELFQQEKNSPKTILLFTVRDWFEEFAPIEVVRNKILDEYINKIWKEMKKPKEAEKLNINNFFIIEVVGLSHGIIKKEDFLKDVNNLRDKWINNLRPSKYSRNIPSDGFAQYCNNIWNTIVKQSQLDIPSQKEMLSTFRCQEIKNNVINNINKEIKEKSIESHNKVIENFKEWAEKNIIQKCLDDYFKDASRYKENICLRTSQELLDYLFTQLQAIVDNNLQYIQRTLCTKFFNELSNMYKICTIEKNTFSFSRDSNLKTVKDNNKNTSHEDIKRDLLNNNQDKCVHLWSNFLYNADKLEYFTFCNFYENYEKSNIEIKTNMKNDDNLKNDDNLKNDAHNNITTHQFNYKPTLSVLSTSIYKDSNRIRNIQCGILLNKTRQTIKNSFKNMDTYLLTTKNTEEYWNNTVQLVLKLQDNINTHLTKCFINLKGTNHNNLNIYNDDMMYNNDDMVFNNNDDDDNNNNNNNNNYYYYNKNDDANLSKDENYNNKFSFSLTNEKGIFQNINNNNEGSDEICYTNALKKIDLIKNKQVYKSTINEDINNKLQNKKYIHELKNYYLDEIMDVLKNKLDEISENLATIIIQRFESVFNYDEYEQPRQWRDISMAELKKIFLKSKNYAFLIIDILQKNIKVELIDDYLPNNFIKDEIIEKGKIKAKRRIQEICRDAQYIQETGSKMSLKNVPVVFWIILLLFGWNEILFFIRMFFKLNVILPLFFAAAFIVSTFVYNGNTQALSYINKIIFYMAKNSYNFFKHIQAISNPPPKNVQKQE | |||||||
Modified residue (large scale data) | 61 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 105 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 115 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 420 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 423 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 435 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 436 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 559 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 590 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 649 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 659 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 661 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 663 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 679 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 754 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-280 | GB1/RHD3-type G | ||||
Sequence: GFSYNVIAVLGSQSSGKSTLLNNLFKTSFDVMNTKQGHSQTTKGLWLSYDKFDDETNNSSSFFKLKKKNKPTLILDVEGTDSKERGDNRLTFEHRSALFCLALADCVIVNLWYHSLGNFTASNYGLLKTVMEVNLELFQQEKNSPKTILLFTVRDWFEEFAPIEVVRNKILDEYINKIWKEMKKPKEAEKLNINNFFIIEVVGLSHGIIKKEDFLKDVNNLRDKWINNLRPSKYSRNIPSDGFAQYC | ||||||
Coiled coil | 319-339 | |||||
Sequence: NKEIKEKSIESHNKVIENFKE | ||||||
Coiled coil | 725-750 | |||||
Sequence: YLDEIMDVLKNKLDEISENLATIIIQ |
Sequence similarities
Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length937
- Mass (Da)110,609
- Last updated2009-09-22 v2
- Checksum0105532D574D6D20
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN999946 EMBL· GenBank· DDBJ | CZT99872.1 EMBL· GenBank· DDBJ | Genomic DNA |