Q5NVH5 · ALBU_PONAB
- ProteinAlbumin
- GeneALB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids609 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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-273 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-273 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 | 27 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 30 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 37 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 91 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 264 | (4Z,15Z)-bilirubin IXalpha (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 268 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 271 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 273 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 273 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 276 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 279 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 283 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | blood microparticle | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | protein-containing complex | |
Molecular Function | DNA binding | |
Molecular Function | enterobactin binding | |
Molecular Function | exogenous protein binding | |
Molecular Function | fatty acid binding | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxygen binding | |
Molecular Function | protein-folding chaperone binding | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | toxic substance binding | |
Biological Process | cellular response to calcium ion starvation | |
Biological Process | negative regulation of mitochondrial depolarization |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAlbumin
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo
Accessions
- Primary accessionQ5NVH5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKWVTFISLLFLFSSAYS | ||||||
Propeptide | PRO_0000280759 | 19-24 | ||||
Sequence: RGVFRR | ||||||
Chain | PRO_0000280760 | 25-609 | Albumin | |||
Sequence: DAHKSEVAHRFKDLGEEKFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAVRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCLAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNELLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEPKRMPCAEDYLSVVLNQLCVLHEKTPVSERVTKCCTESLVNRRPCFSALEVDETYVPKEFNADTFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKTVMEDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL | ||||||
Modified residue | 29 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 77↔86 | |||||
Sequence: CVADESAENC | ||||||
Modified residue | 82 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 89 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 99↔115 | |||||
Sequence: CTVATLRETYGEMADCC | ||||||
Modified residue | 107 | Phosphothreonine | ||||
Sequence: T | ||||||
Disulfide bond | 114↔125 | |||||
Sequence: CCAKQEPERNEC | ||||||
Disulfide bond | 148↔193 | |||||
Sequence: CTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAVRYKAAFTECC | ||||||
Disulfide bond | 192↔201 | |||||
Sequence: CCQAADKAAC | ||||||
Disulfide bond | 224↔270 | |||||
Sequence: CASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECC | ||||||
Modified residue | 229 | N6-succinyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 269↔277 | |||||
Sequence: CCHGDLLEC | ||||||
Disulfide bond | 289↔303 | |||||
Sequence: CENQDSISSKLKECC | ||||||
Modified residue | 297 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 302↔313 | |||||
Sequence: CCEKPLLEKSHC | ||||||
Disulfide bond | 340↔385 | |||||
Sequence: CKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCC | ||||||
Disulfide bond | 384↔393 | |||||
Sequence: CCAAADPHEC | ||||||
Disulfide bond | 416↔462 | |||||
Sequence: CELFEQLGEYKFQNELLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCC | ||||||
Modified residue | 443 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 444 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 446 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 460 | N6-succinyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 461↔472 | |||||
Sequence: CCKHPEPKRMPC | ||||||
Disulfide bond | 485↔501 | |||||
Sequence: CVLHEKTPVSERVTKCC | ||||||
Disulfide bond | 500↔511 | |||||
Sequence: CCTESLVNRRPC | ||||||
Modified residue | 513 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 538↔583 | |||||
Sequence: CTLSEKERQIKKQTALVELVKHKPKATKEQLKTVMEDFAAFVEKCC | ||||||
Modified residue | 543 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 558 | N6-methyllysine | ||||
Sequence: K | ||||||
Modified residue | 570 | Phosphothreonine | ||||
Sequence: T | ||||||
Disulfide bond | 582↔591 | |||||
Sequence: CCKADDKETC | ||||||
Modified residue | 588 | N6-succinyllysine | ||||
Sequence: K |
Post-translational modification
Phosphorylated by FAM20C in the extracellular medium.
Keywords
- PTM
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 | 19-210 | Albumin 1 | ||||
Sequence: RGVFRRDAHKSEVAHRFKDLGEEKFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAVRYKAAFTECCQAADKAACLLPKLDELR | ||||||
Domain | 211-403 | Albumin 2 | ||||
Sequence: DEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCLAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKP | ||||||
Domain | 404-601 | Albumin 3 | ||||
Sequence: LVEEPQNLIKQNCELFEQLGEYKFQNELLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEPKRMPCAEDYLSVVLNQLCVLHEKTPVSERVTKCCTESLVNRRPCFSALEVDETYVPKEFNADTFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKTVMEDFAAFVEKCCKADDKETCFAEEGKKLVA |
Sequence similarities
Belongs to the ALB/AFP/VDB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length609
- Mass (Da)69,480
- Last updated2011-06-28 v2
- ChecksumCD8FBA3459C42B1F
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2J8UTW0 | A0A2J8UTW0_PONAB | ALB | 396 | ||
A0A2J8UTW2 | A0A2J8UTW2_PONAB | ALB | 459 | ||
A0A2J8UTW3 | A0A2J8UTW3_PONAB | ALB | 417 | ||
A0A2J8UTX5 | A0A2J8UTX5_PONAB | ALB | 604 | ||
A0A2J8UTX6 | A0A2J8UTX6_PONAB | ALB | 494 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 42 | in Ref. 1; CAI29688 | ||||
Sequence: K → N | ||||||
Sequence conflict | 183 | in Ref. 1; CAI29688 | ||||
Sequence: V → K | ||||||
Sequence conflict | 314 | in Ref. 1; CAI29688 | ||||
Sequence: L → I | ||||||
Sequence conflict | 430 | in Ref. 1; CAI29688 | ||||
Sequence: E → A | ||||||
Sequence conflict | 467 | in Ref. 1; CAI29688 | ||||
Sequence: P → A | ||||||
Sequence conflict | 495 | in Ref. 1; CAI29688 | ||||
Sequence: E → D | ||||||
Sequence conflict | 529 | in Ref. 1; CAI29688 | ||||
Sequence: D → E | ||||||
Sequence conflict | 570 | in Ref. 1; CAI29688 | ||||
Sequence: T → A | ||||||
Sequence conflict | 573 | in Ref. 1; CAI29688 | ||||
Sequence: E → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR524764 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
CR545545 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
CR545546 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
CR765111 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
CR926060 EMBL· GenBank· DDBJ | CAI29688.1 EMBL· GenBank· DDBJ | mRNA |