P04467 · CALB1_BOVIN
- ProteinCalbindin
- GeneCALB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids261 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Buffers cytosolic calcium. May stimulate a membrane Ca2+-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 24 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 26 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 28 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 30 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 35 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 111 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 113 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 115 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 122 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 155 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 157 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 159 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 161 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 166 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 199 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 201 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 203 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 205 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 210 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E |
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 | cytosol | |
Cellular Component | dendrite | |
Cellular Component | dendritic spine | |
Cellular Component | nucleus | |
Cellular Component | synapse | |
Cellular Component | terminal bouton | |
Molecular Function | calcium ion binding | |
Molecular Function | vitamin D binding | |
Biological Process | regulation of long-term synaptic potentiation | |
Biological Process | regulation of presynaptic cytosolic calcium ion concentration |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCalbindin
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP04467
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000073471 | 2-261 | Calbindin | |||
Sequence: AESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELQQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGVKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQDLDINNIPTYKKSIMALSDGGKLYRTDLALILSAGDN |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-7 | Interaction with RANBP9 | ||||
Sequence: AESHLQ | ||||||
Domain | 11-46 | EF-hand 1 | ||||
Sequence: ITASQFFEIWLHFDADGSGYLEGKELQNLIQELQQA | ||||||
Domain | 53-88 | EF-hand 2 | ||||
Sequence: ELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENF | ||||||
Domain | 98-133 | EF-hand 3 | ||||
Sequence: KSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEK | ||||||
Domain | 142-177 | EF-hand 4 | ||||
Sequence: KLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENF | ||||||
Domain | 186-221 | EF-hand 5 | ||||
Sequence: MCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEK | ||||||
Domain | 226-251 | EF-hand 6 | ||||
Sequence: LDINNIPTYKKSIMALSDGGKLYRTD |
Domain
This protein has four functional calcium-binding sites; potential sites II and VI have lost affinity for calcium.
Sequence similarities
Belongs to the calbindin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length261
- Mass (Da)29,964
- Last updated2007-01-23 v3
- Checksum847CD14BD7431E03
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q1LUQ4 | A0A3Q1LUQ4_BOVIN | CALB1 | 236 | ||
A0A3Q1LWK7 | A0A3Q1LWK7_BOVIN | CALB1 | 243 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 67 | in Ref. 2; AA sequence | ||||
Sequence: Q → E | ||||||
Sequence conflict | 203 | in Ref. 2; AA sequence | ||||
Sequence: N → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC116125 EMBL· GenBank· DDBJ | AAI16126.1 EMBL· GenBank· DDBJ | mRNA |