Q28522 · ALBU_MACMU
- ProteinAlbumin
- GeneALB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids600 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Binds water, Ca2+, Na+, K+, fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity).
Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity).
Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity).
The shared binding site between zinc and calcium at residue Asp-265 suggests a crosstalk between zinc and calcium transport in the blood (By similarity).
The rank order of affinity is zinc > calcium > magnesium (By similarity).
Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity).
Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity).
Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity).
Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity).
The shared binding site between zinc and calcium at residue Asp-265 suggests a crosstalk between zinc and calcium transport in the blood (By similarity).
The rank order of affinity is zinc > calcium > magnesium (By similarity).
Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity).
Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 19 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 22 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 29 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 83 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 256 | (4Z,15Z)-bilirubin IXalpha (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 260 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 263 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 265 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 265 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 268 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 271 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 275 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
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 | cytoplasm | |
Cellular Component | extracellular space | |
Cellular Component | protein-containing complex | |
Molecular Function | DNA binding | |
Molecular Function | enterobactin binding | |
Molecular Function | fatty acid binding | |
Molecular Function | metal ion binding | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | toxic substance binding | |
Biological Process | cellular response to calcium ion starvation | |
Biological Process | cellular response to starvation | |
Biological Process | negative regulation of mitochondrial depolarization |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAlbumin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionQ28522
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-10 | |||||
Sequence: LLFLFSSAYS | ||||||
Propeptide | PRO_0000001069 | 11-16 | ||||
Sequence: RGVFRR | ||||||
Chain | PRO_0000001070 | 17-600 | Albumin | |||
Sequence: DTHKSEVAHRFKDLGEEHFKGLVLVAFSQYLQQCPFEEHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPPLVRPEVDVMCTAFHDNEATFLKKYLYEVARRHPYFYAPELLFFAARYKAAFAECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGDRAFKAWAVARLSQKFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYMCENQDSISSKLKECCDKPLLEKSHCLAEVENDEMPADLPSLAADYVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVMLLLRLAKAYEATLEKCCAAADPHECYAKVFDEFQPLVEEPQNLVKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGAKCCKLPEAKRMPCAEDYLSVVLNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALELDEAYVPKAFNAETFTFHADMCTLSEKEKQVKKQTALVELVKHKPKATKEQLKGVMDNFAAFVEKCCKADDKEACFAEEGPKFVAASQAALA | ||||||
Modified residue | 21 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 69↔78 | |||||
Sequence: CVADESAENC | ||||||
Modified residue | 74 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 81 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 91↔107 | |||||
Sequence: CTVATLRETYGEMADCC | ||||||
Modified residue | 99 | Phosphothreonine | ||||
Sequence: T | ||||||
Disulfide bond | 106↔117 | |||||
Sequence: CCAKQEPERNEC | ||||||
Disulfide bond | 140↔185 | |||||
Sequence: CTAFHDNEATFLKKYLYEVARRHPYFYAPELLFFAARYKAAFAECC | ||||||
Disulfide bond | 184↔193 | |||||
Sequence: CCQAADKAAC | ||||||
Disulfide bond | 216↔262 | |||||
Sequence: CASLQKFGDRAFKAWAVARLSQKFPKAEFAEVSKLVTDLTKVHTECC | ||||||
Modified residue | 221 | N6-succinyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 261↔269 | |||||
Sequence: CCHGDLLEC | ||||||
Disulfide bond | 281↔295 | |||||
Sequence: CENQDSISSKLKECC | ||||||
Modified residue | 289 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 294↔305 | |||||
Sequence: CCDKPLLEKSHC | ||||||
Disulfide bond | 332↔377 | |||||
Sequence: CKNYAEAKDVFLGMFLYEYARRHPDYSVMLLLRLAKAYEATLEKCC | ||||||
Disulfide bond | 376↔385 | |||||
Sequence: CCAAADPHEC | ||||||
Disulfide bond | 408↔454 | |||||
Sequence: CELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGAKCC | ||||||
Modified residue | 435 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 436 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 438 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 452 | N6-succinyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 453↔464 | |||||
Sequence: CCKLPEAKRMPC | ||||||
Disulfide bond | 477↔493 | |||||
Sequence: CVLHEKTPVSEKVTKCC | ||||||
Disulfide bond | 492↔503 | |||||
Sequence: CCTESLVNRRPC | ||||||
Modified residue | 505 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 530↔575 | |||||
Sequence: CTLSEKEKQVKKQTALVELVKHKPKATKEQLKGVMDNFAAFVEKCC | ||||||
Modified residue | 535 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 550 | N6-methyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 574↔583 | |||||
Sequence: CCKADDKEAC | ||||||
Modified residue | 580 | N6-succinyllysine | ||||
Sequence: K |
Post-translational modification
Phosphorylated by FAM20C in the extracellular medium.
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Plasma.
Interaction
Subunit
Interacts with FCGRT; this interaction regulates ALB homeostasis (By similarity).
Interacts with TASOR (By similarity).
In plasma, occurs in a covalently-linked complex with chromophore-bound alpha-1-microglobulin; this interaction does not prevent fatty acid binding to ALB
Interacts with TASOR (By similarity).
In plasma, occurs in a covalently-linked complex with chromophore-bound alpha-1-microglobulin; this interaction does not prevent fatty acid binding to ALB
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-202 | Albumin 1 | ||||
Sequence: RGVFRRDTHKSEVAHRFKDLGEEHFKGLVLVAFSQYLQQCPFEEHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPPLVRPEVDVMCTAFHDNEATFLKKYLYEVARRHPYFYAPELLFFAARYKAAFAECCQAADKAACLLPKLDELR | ||||||
Domain | 203-395 | Albumin 2 | ||||
Sequence: DEGKASSAKQRLKCASLQKFGDRAFKAWAVARLSQKFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYMCENQDSISSKLKECCDKPLLEKSHCLAEVENDEMPADLPSLAADYVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVMLLLRLAKAYEATLEKCCAAADPHECYAKVFDEFQP | ||||||
Domain | 396-593 | Albumin 3 | ||||
Sequence: LVEEPQNLVKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGAKCCKLPEAKRMPCAEDYLSVVLNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALELDEAYVPKAFNAETFTFHADMCTLSEKEKQVKKQTALVELVKHKPKATKEQLKGVMDNFAAFVEKCCKADDKEACFAEEGPKFVA |
Sequence similarities
Belongs to the ALB/AFP/VDB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length600
- Mass (Da)67,881
- Last updated1996-11-01 v1
- ChecksumE45C871A670E740B
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M90463 EMBL· GenBank· DDBJ | AAA36906.1 EMBL· GenBank· DDBJ | mRNA |