Q60604 · SCIN_MOUSE
- ProteinScinderin
- GeneScin
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids715 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ca2+-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane (PubMed:9671468).
Severing activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2) (By similarity).
In vitro, also has barbed end capping and nucleating activities in the presence of Ca2+ (PubMed:9671468).
Required for megakaryocyte differentiation, maturation, polyploidization and apoptosis with the release of platelet-like particles (By similarity).
Plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts (PubMed:25275604, PubMed:25681458).
Regulates chondrocyte proliferation and differentiation (By similarity).
Inhibits cell proliferation and tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways (By similarity).
Severing activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2) (By similarity).
In vitro, also has barbed end capping and nucleating activities in the presence of Ca2+ (PubMed:9671468).
Required for megakaryocyte differentiation, maturation, polyploidization and apoptosis with the release of platelet-like particles (By similarity).
Plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts (PubMed:25275604, PubMed:25681458).
Regulates chondrocyte proliferation and differentiation (By similarity).
Inhibits cell proliferation and tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways (By similarity).
Isoform 2
Fails to nucleate actin polymerization, although it severs and caps actin filaments in a Ca2+-dependent manner.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 112-119 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: KGGLKYKA | ||||||
Binding site | 138-146 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: RLLHVKGRR | ||||||
Binding site | 538 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 539 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 562 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 643 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 644 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 666 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | anchoring junction | |
Cellular Component | brush border | |
Cellular Component | cell projection | |
Cellular Component | cytoplasm | |
Cellular Component | podosome | |
Cellular Component | protein-containing complex | |
Molecular Function | actin filament binding | |
Molecular Function | metal ion binding | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Biological Process | actin filament severing | |
Biological Process | actin polymerization or depolymerization | |
Biological Process | barbed-end actin filament capping | |
Biological Process | cell projection assembly | |
Biological Process | central nervous system development | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | positive regulation of actin nucleation | |
Biological Process | positive regulation of apoptotic process | |
Biological Process | positive regulation of megakaryocyte differentiation | |
Biological Process | regulation of chondrocyte differentiation | |
Biological Process | sequestering of actin monomers |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameScinderin
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ60604
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockdown in bone marrow monocytes protect mice from bone resorption in periodontal disease model.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 26 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000218745 | 1-715 | Scinderin | |||
Sequence: MAQELQHPEFARAGQQAGLQVWRVEKLELVPVPQGAYGDFYVGDAYLVLHTTKSSRGFSYRLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQSRELQGYESTDFVGYFKGGLKYKAGGVASGLNHVLTNDLTAKRLLHVKGRRVVRATEVPLSWESFNKGDCFIIDLGTEIYQWCGSSCNKYERLKASQVAIGIRDNERKGRSQLIVVEEGSEPSELMKVLGRKPELPDGDNDDDVVADISNRKMAKLYMVSDASGSMKVTLVAEENPFSMGMLLSEECFILDHGAAKQIFVWKGKNANPQERKTAMKTAEEFLQKMKYSTNTQIQVLPEGGETPIFKQFFKDWKDKDQSDGFGKVYITEKVAQIKQIPFDASKLHSSPQMAAQHNMVDDGSGGVEIWRVENSGRVQIDPSSYGEFYGGDCYIILYTYPRGQIIYTWQGANATRDELTMSAFLTVQLDRSLGGQAVQVRVSQGKEPAHLLSLFKDKPLIIYKNGTSKKEGQAPAPPTRLFQVRRNLASITRIVEVDVDANSLNSNDTFVLKLPRNNGFIWIGKGASQEEEKGAEYVADVLKCKASRIQEGKEPEEFWNSLGGRGDYQTSPLLETRAEDHPPRLYGCSNKTGRFIIEEVPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESVKSAKMYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSRW | ||||||
Modified residue | 102 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 599 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-363 | Actin-severing | ||||
Sequence: MAQELQHPEFARAGQQAGLQVWRVEKLELVPVPQGAYGDFYVGDAYLVLHTTKSSRGFSYRLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQSRELQGYESTDFVGYFKGGLKYKAGGVASGLNHVLTNDLTAKRLLHVKGRRVVRATEVPLSWESFNKGDCFIIDLGTEIYQWCGSSCNKYERLKASQVAIGIRDNERKGRSQLIVVEEGSEPSELMKVLGRKPELPDGDNDDDVVADISNRKMAKLYMVSDASGSMKVTLVAEENPFSMGMLLSEECFILDHGAAKQIFVWKGKNANPQERKTAMKTAEEFLQKMKYSTNTQIQVLPEGGETPIFKQFFKDWKDKDQSDGFGKVYITE | ||||||
Repeat | 27-76 | Gelsolin-like 1 | ||||
Sequence: LELVPVPQGAYGDFYVGDAYLVLHTTKSSRGFSYRLHFWLGKECSQDEST | ||||||
Repeat | 148-188 | Gelsolin-like 2 | ||||
Sequence: VRATEVPLSWESFNKGDCFIIDLGTEIYQWCGSSCNKYERL | ||||||
Repeat | 265-307 | Gelsolin-like 3 | ||||
Sequence: LVAEENPFSMGMLLSEECFILDHGAAKQIFVWKGKNANPQERK | ||||||
Region | 364-715 | Ca2+-dependent actin binding | ||||
Sequence: KVAQIKQIPFDASKLHSSPQMAAQHNMVDDGSGGVEIWRVENSGRVQIDPSSYGEFYGGDCYIILYTYPRGQIIYTWQGANATRDELTMSAFLTVQLDRSLGGQAVQVRVSQGKEPAHLLSLFKDKPLIIYKNGTSKKEGQAPAPPTRLFQVRRNLASITRIVEVDVDANSLNSNDTFVLKLPRNNGFIWIGKGASQEEEKGAEYVADVLKCKASRIQEGKEPEEFWNSLGGRGDYQTSPLLETRAEDHPPRLYGCSNKTGRFIIEEVPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESVKSAKMYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSRW | ||||||
Repeat | 398-451 | Gelsolin-like 4 | ||||
Sequence: VEIWRVENSGRVQIDPSSYGEFYGGDCYIILYTYPRGQIIYTWQGANATRDELT | ||||||
Repeat | 523-564 | Gelsolin-like 5 | ||||
Sequence: TRIVEVDVDANSLNSNDTFVLKLPRNNGFIWIGKGASQEEEK | ||||||
Repeat | 626-668 | Gelsolin-like 6 | ||||
Sequence: FIIEEVPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKK |
Sequence similarities
Belongs to the villin/gelsolin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q60604-1
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
- Length715
- Mass (Da)80,254
- Last updated2011-07-27 v3
- Checksum6EF9F45FBC82E249
Q60604-2
- Name2
- SynonymsD5
- Differences from canonical
- 528-627: Missing
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 44-45 | in Ref. 1; AAB61682/CAA74304 | ||||
Sequence: DA → EP | ||||||
Alternative sequence | VSP_006730 | 528-627 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U04354 EMBL· GenBank· DDBJ | AAB61682.1 EMBL· GenBank· DDBJ | mRNA | ||
Y13971 EMBL· GenBank· DDBJ | CAA74304.1 EMBL· GenBank· DDBJ | mRNA | ||
AK133484 EMBL· GenBank· DDBJ | BAE21681.1 EMBL· GenBank· DDBJ | mRNA | ||
BC063328 EMBL· GenBank· DDBJ | AAH63328.1 EMBL· GenBank· DDBJ | mRNA |