Q8R1S4 · MTSS1_MOUSE
- ProteinProtein MTSS 1
- GeneMtss1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids759 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Inhibits the nucleation of actin filaments in vitro.
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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Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameProtein MTSS 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8R1S4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 746 | Loss of actin-binding. | ||||
Sequence: K → A | ||||||
Mutagenesis | 747 | Loss of actin-binding. | ||||
Sequence: K → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000096640 | 1-759 | Protein MTSS 1 | |||
Sequence: MEAVIEKECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKNKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLPSSSEQVILDLKGSDYSWSYQTPPSSPSTTMSRKSSVCSSLNSVNSSDSRSSGSHSHSPSSHYRYRSSNLAQQAPVRLSSVSSHDSGFISQDAFQSKSPSPMPPEAANQLSNGFSHCSLSSESHAGPVGAGPFPHCLPASRLLPRVTSVHLPDYAHYYTIGPGMFPSSQIPSWKDWAKPGPYDQPLVNTLQRRKEKREPDSNGGGPTTTGGPPAGAEEAQRPRSMTVSAATRPGEEMAACEELTLALSRGLQLDVQRSSRDSLQCSSGYSTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRFS | ||||||
Modified residue | 262 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 265 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 266 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 275 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 326 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 429 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 607 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 648 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 651 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Strongly expressed in the developing neurons and skeletal and cardiac muscles in embryos. Strongly expressed also in liver, outer layers of the kidney, and in the Purkinje cells of the brain.
Interaction
Subunit
Binds to actin.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8R1S4 | Mtss1 Q8R1S4 | 2 | EBI-15622277, EBI-15622277 | |
BINARY | Q8R1S4 | Pard3 Q99NH2-1 | 2 | EBI-15622277, EBI-15946047 | |
BINARY | Q8R1S4 | Prkci Q62074 | 4 | EBI-15622277, EBI-82016 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-254 | IMD | ||||
Sequence: MEAVIEKECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKNKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLPSSSEQVILDLKGS | ||||||
Coiled coil | 108-157 | |||||
Sequence: LQEQMEEWKKVANQLDKDHAKEYKKARQEIKNKSSDTLKLQKKAKKVDAQ | ||||||
Region | 259-309 | Disordered | ||||
Sequence: SYQTPPSSPSTTMSRKSSVCSSLNSVNSSDSRSSGSHSHSPSSHYRYRSSN | ||||||
Region | 331-354 | Disordered | ||||
Sequence: QDAFQSKSPSPMPPEAANQLSNGF | ||||||
Region | 431-472 | Disordered | ||||
Sequence: QRRKEKREPDSNGGGPTTTGGPPAGAEEAQRPRSMTVSAATR | ||||||
Region | 569-759 | Disordered | ||||
Sequence: KRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRFS | ||||||
Compositional bias | 618-638 | Pro residues | ||||
Sequence: PVIPVKTPTVPDLPGVLPSPP | ||||||
Compositional bias | 655-673 | Polar residues | ||||
Sequence: GEGPQGVSNIPSSLWSGQA | ||||||
Compositional bias | 689-705 | Basic and acidic residues | ||||
Sequence: EHRQAIPESEAEDQERD | ||||||
Domain | 731-748 | WH2 | ||||
Sequence: QGEDMLNAIRRGVKLKKT |
Domain
The WH2 motif at the C-terminus binds to actin monomers.
Sequence similarities
Belongs to the MTSS family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8R1S4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsLong
- Length759
- Mass (Da)82,408
- Last updated2002-06-01 v1
- Checksum3E9008065FF78439
Q8R1S4-2
- Name2
- SynonymsShort
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BPM9 | A0A2I3BPM9_MOUSE | Mtss1 | 204 | ||
A0A2I3BQ67 | A0A2I3BQ67_MOUSE | Mtss1 | 242 | ||
A0A2I3BQ92 | A0A2I3BQ92_MOUSE | Mtss1 | 162 | ||
G3X9H7 | G3X9H7_MOUSE | Mtss1 | 759 |
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 139 | in Ref. 3; BAC27008 | ||||
Sequence: N → K | ||||||
Alternative sequence | VSP_050527 | 483 | in isoform 2 | |||
Sequence: L → P | ||||||
Alternative sequence | VSP_050528 | 487 | in isoform 2 | |||
Sequence: L → P | ||||||
Compositional bias | 618-638 | Pro residues | ||||
Sequence: PVIPVKTPTVPDLPGVLPSPP | ||||||
Alternative sequence | VSP_050529 | 646-681 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 655-673 | Polar residues | ||||
Sequence: GEGPQGVSNIPSSLWSGQA | ||||||
Compositional bias | 689-705 | Basic and acidic residues | ||||
Sequence: EHRQAIPESEAEDQERD | ||||||
Sequence conflict | 758 | in Ref. 3; BAC27008 | ||||
Sequence: F → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY214918 EMBL· GenBank· DDBJ | AAO52743.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003483 EMBL· GenBank· DDBJ | AAH03483.1 EMBL· GenBank· DDBJ | mRNA | ||
BC024131 EMBL· GenBank· DDBJ | AAH24131.1 EMBL· GenBank· DDBJ | mRNA | ||
BC042632 EMBL· GenBank· DDBJ | AAH42632.1 EMBL· GenBank· DDBJ | mRNA | ||
AK030533 EMBL· GenBank· DDBJ | BAC27008.1 EMBL· GenBank· DDBJ | mRNA |