Q11002 · CANA_DROME
- ProteinCalpain-A
- GeneCalpA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids828 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Calcium-regulated non-lysosomal thiol-protease. Involved in the organization of the actin-related cytoskeleton during embryogenesis.
Miscellaneous
This protein binds calcium.
Activity regulation
Activated by millimolar concentrations of calcium, and by phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol and phosphatidic acid.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 54-55 | Cleavage; by autolysis | ||||
Sequence: KN | ||||||
Active site | 143 | |||||
Sequence: C | ||||||
Active site | 299 | |||||
Sequence: H | ||||||
Active site | 327 | |||||
Sequence: N | ||||||
Binding site | 712 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 714 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 716 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 718 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 723 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 742 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 746 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 748 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 753 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | Golgi apparatus | |
Cellular Component | neuronal cell body | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent cysteine-type endopeptidase activity | |
Biological Process | cuticle development | |
Biological Process | defense response to fungus | |
Biological Process | determination of adult lifespan | |
Biological Process | dorsal/ventral pattern formation | |
Biological Process | larval locomotory behavior | |
Biological Process | myoblast fusion | |
Biological Process | neuron remodeling | |
Biological Process | protein autoprocessing | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCalpain-A
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ11002
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000026497 | 1-828 | Calpain-A | |||
Sequence: MDDLRGFLRQAGQEFLNAAGEAAMGAAKDVVGSVINEIFIKKEADTKRVLPSIKNMRVLGEKSSSLGPYSEVQDYETILNSCLASGSLFEDPLFPASNESLQFSRRPDRHIEWLRPHEIAENPQFFVEGYSRFDVQQGELGDCWLLAATANLTQESNLFFRVIPAEQSFEENYAGIFHFRFWQYGKWVDVIIDDRLPTYNGELMYMHSTEKNEFWSALLEKAYAKLHGSYEALKGGSTCEAMEDFTGGVSEWYDLKEAPGNLFTILQKAAERNSMMGCSIEPDPNVTEAETPQGLIRGHAYSITKVCLIDIVTPNRQGKIPMIRMRNPWGNEAEWNGPWSDSSPEWRYIPEEQKAEIGLTFDRDGEFWMSFQDFLNHFDRVEICNLSPDSLTEDQQNSGKRKWEMSMYEGEWTPGVTAGGCRNFLDTFWHNPQYIITLVDPDEEDEEGQCTVIVALMQKNRRSKRNMGMECLTIGFAIYSLNDRELENRPQGLNFFRYKSSVGRSPHFINTREVCARFKLPPGHYLIVPSTFDPNEEGEFIIRVFSETQNNMEENDDHVGYGGKADTITPGFPTPKPIDPQKEGLRRLFDSIAGKDMEVDWMELKRILDHSMRDDLPKPVVFNRFSNNMAFETQAAGPGDDGAGACGLLSLICGPFLKGTPFEEQLGMNDQSNKRLIGDNPADGGPVTANAIVDETHGFSKDVCRSMVAMLDADKSGKLGFEEFETLLSEIAKWKAIFKVYDVENTGRVSGFQLREALNSAGYHLNNRVLNVLGHRYGSRDGKIAFDDFIMCAVKIKTYIDIFKERDTEKNETATFTLEEWIERTIYS | ||||||
Chain | PRO_0000026498 | 55-828 | Calpain-A catalytic subunit | |||
Sequence: NMRVLGEKSSSLGPYSEVQDYETILNSCLASGSLFEDPLFPASNESLQFSRRPDRHIEWLRPHEIAENPQFFVEGYSRFDVQQGELGDCWLLAATANLTQESNLFFRVIPAEQSFEENYAGIFHFRFWQYGKWVDVIIDDRLPTYNGELMYMHSTEKNEFWSALLEKAYAKLHGSYEALKGGSTCEAMEDFTGGVSEWYDLKEAPGNLFTILQKAAERNSMMGCSIEPDPNVTEAETPQGLIRGHAYSITKVCLIDIVTPNRQGKIPMIRMRNPWGNEAEWNGPWSDSSPEWRYIPEEQKAEIGLTFDRDGEFWMSFQDFLNHFDRVEICNLSPDSLTEDQQNSGKRKWEMSMYEGEWTPGVTAGGCRNFLDTFWHNPQYIITLVDPDEEDEEGQCTVIVALMQKNRRSKRNMGMECLTIGFAIYSLNDRELENRPQGLNFFRYKSSVGRSPHFINTREVCARFKLPPGHYLIVPSTFDPNEEGEFIIRVFSETQNNMEENDDHVGYGGKADTITPGFPTPKPIDPQKEGLRRLFDSIAGKDMEVDWMELKRILDHSMRDDLPKPVVFNRFSNNMAFETQAAGPGDDGAGACGLLSLICGPFLKGTPFEEQLGMNDQSNKRLIGDNPADGGPVTANAIVDETHGFSKDVCRSMVAMLDADKSGKLGFEEFETLLSEIAKWKAIFKVYDVENTGRVSGFQLREALNSAGYHLNNRVLNVLGHRYGSRDGKIAFDDFIMCAVKIKTYIDIFKERDTEKNETATFTLEEWIERTIYS |
Post-translational modification
Undergoes calcium-dependent autolytic cleavage between Lys-54 and Asn-55, which is necessary for activation of the protein.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Localized to the anterior and posterior embryonic poles just after fertilization. Becomes distributed around the polar buds and just below the pole cells of the posterior pole during cleavage cycles. During these nuclear divisions anterior localization disappears. Localized to actin caps that underlie the plasma membrane, immediately above each nucleus at cleavage cycles 8 and 9. Localized to a small set of nerve, midgut and blood cells in adults.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-14 | EF-hand 1 | ||||
Sequence: MDDLRGFLRQAGQE | ||||||
Domain | 88-387 | Calpain catalytic | ||||
Sequence: LFEDPLFPASNESLQFSRRPDRHIEWLRPHEIAENPQFFVEGYSRFDVQQGELGDCWLLAATANLTQESNLFFRVIPAEQSFEENYAGIFHFRFWQYGKWVDVIIDDRLPTYNGELMYMHSTEKNEFWSALLEKAYAKLHGSYEALKGGSTCEAMEDFTGGVSEWYDLKEAPGNLFTILQKAAERNSMMGCSIEPDPNVTEAETPQGLIRGHAYSITKVCLIDIVTPNRQGKIPMIRMRNPWGNEAEWNGPWSDSSPEWRYIPEEQKAEIGLTFDRDGEFWMSFQDFLNHFDRVEICNLS | ||||||
Region | 388-557 | Domain III | ||||
Sequence: PDSLTEDQQNSGKRKWEMSMYEGEWTPGVTAGGCRNFLDTFWHNPQYIITLVDPDEEDEEGQCTVIVALMQKNRRSKRNMGMECLTIGFAIYSLNDRELENRPQGLNFFRYKSSVGRSPHFINTREVCARFKLPPGHYLIVPSTFDPNEEGEFIIRVFSETQNNMEENDD | ||||||
Region | 558-577 | Linker | ||||
Sequence: HVGYGGKADTITPGFPTPKP | ||||||
Region | 578-828 | Domain IV | ||||
Sequence: IDPQKEGLRRLFDSIAGKDMEVDWMELKRILDHSMRDDLPKPVVFNRFSNNMAFETQAAGPGDDGAGACGLLSLICGPFLKGTPFEEQLGMNDQSNKRLIGDNPADGGPVTANAIVDETHGFSKDVCRSMVAMLDADKSGKLGFEEFETLLSEIAKWKAIFKVYDVENTGRVSGFQLREALNSAGYHLNNRVLNVLGHRYGSRDGKIAFDDFIMCAVKIKTYIDIFKERDTEKNETATFTLEEWIERTIYS | ||||||
Domain | 579-614 | EF-hand 2 | ||||
Sequence: DPQKEGLRRLFDSIAGKDMEVDWMELKRILDHSMRD | ||||||
Domain | 699-734 | EF-hand 3 | ||||
Sequence: FSKDVCRSMVAMLDADKSGKLGFEEFETLLSEIAKW | ||||||
Domain | 729-764 | EF-hand 4 | ||||
Sequence: SEIAKWKAIFKVYDVENTGRVSGFQLREALNSAGYH | ||||||
Domain | 764-799 | EF-hand 5 | ||||
Sequence: HLNNRVLNVLGHRYGSRDGKIAFDDFIMCAVKIKTY |
Sequence similarities
Belongs to the peptidase C2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q11002-1
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.
- NameB
- Length828
- Mass (Da)93,963
- Last updated2001-10-18 v2
- Checksum09576D1268BD569C
Q11002-2
- NameA
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0B4LG26 | A0A0B4LG26_DROME | CalpA | 843 | ||
A8DYJ3 | A8DYJ3_DROME | CalpA | 828 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 35 | in Ref. 2; CAA86993/CAA86994 | ||||
Sequence: I → Y | ||||||
Sequence conflict | 306 | in Ref. 2; CAA86994 | ||||
Sequence: V → I | ||||||
Sequence conflict | 397 | in Ref. 1; CAA55298/CAA55297 | ||||
Sequence: N → H | ||||||
Alternative sequence | VSP_005244 | 554-565 | in isoform A | |||
Sequence: ENDDHVGYGGKA → CVQVDNDNEFVY | ||||||
Sequence conflict | 554-565 | In isoform Q11002-2; in Ref. 2; CAA86994 | ||||
Sequence: CVQVDNDNEFVY → RTSRQ | ||||||
Alternative sequence | VSP_005245 | 566-828 | in isoform A | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X78555 EMBL· GenBank· DDBJ | CAA55298.1 EMBL· GenBank· DDBJ | mRNA | ||
X78555 EMBL· GenBank· DDBJ | CAA55297.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
Z46891 EMBL· GenBank· DDBJ | CAA86993.1 EMBL· GenBank· DDBJ | mRNA | ||
Z46892 EMBL· GenBank· DDBJ | CAA86994.1 EMBL· GenBank· DDBJ | mRNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF57563.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF57564.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY051678 EMBL· GenBank· DDBJ | AAK93102.1 EMBL· GenBank· DDBJ | mRNA |