Q28522 · ALBU_MACMU

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).

Features

Showing features for binding site.

160050100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site19Cu cation (UniProtKB | ChEBI)
Binding site22Ca2+ 1 (UniProtKB | ChEBI)
Binding site29Ca2+ 2 (UniProtKB | ChEBI)
Binding site83Zn2+ (UniProtKB | ChEBI)
Binding site256(4Z,15Z)-bilirubin IXalpha (UniProtKB | ChEBI)
Binding site260Ca2+ 1 (UniProtKB | ChEBI)
Binding site263Zn2+ (UniProtKB | ChEBI)
Binding site265Ca2+ 1 (UniProtKB | ChEBI)
Binding site265Zn2+ (UniProtKB | ChEBI)
Binding site268Ca2+ 1 (UniProtKB | ChEBI)
Binding site271Ca2+ 2 (UniProtKB | ChEBI)
Binding site275Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentextracellular space
Cellular Componentprotein-containing complex
Molecular FunctionDNA binding
Molecular Functionenterobactin binding
Molecular Functionfatty acid binding
Molecular Functionmetal ion binding
Molecular Functionpyridoxal phosphate binding
Molecular Functiontoxic substance binding
Biological Processcellular response to calcium ion starvation
Biological Processcellular response to starvation
Biological Processnegative regulation of mitochondrial depolarization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Albumin

Gene names

    • Name
      ALB

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca

Accessions

  • Primary accession
    Q28522

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, propeptide, chain, modified residue, disulfide bond.

TypeIDPosition(s)Description
Signal1-10
PropeptidePRO_000000106911-16
ChainPRO_000000107017-600Albumin
Modified residue21Phosphoserine
Disulfide bond69↔78
Modified residue74Phosphoserine
Modified residue81Phosphoserine
Disulfide bond91↔107
Modified residue99Phosphothreonine
Disulfide bond106↔117
Disulfide bond140↔185
Disulfide bond184↔193
Disulfide bond216↔262
Modified residue221N6-succinyllysine
Disulfide bond261↔269
Disulfide bond281↔295
Modified residue289Phosphoserine
Disulfide bond294↔305
Disulfide bond332↔377
Disulfide bond376↔385
Disulfide bond408↔454
Modified residue435Phosphoserine
Modified residue436Phosphothreonine
Modified residue438Phosphothreonine
Modified residue452N6-succinyllysine
Disulfide bond453↔464
Disulfide bond477↔493
Disulfide bond492↔503
Modified residue505Phosphoserine
Disulfide bond530↔575
Modified residue535N6-succinyllysine
Modified residue550N6-methyllysine
Disulfide bond574↔583
Modified residue580N6-succinyllysine

Post-translational modification

Phosphorylated by FAM20C in the extracellular medium.

Keywords

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

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-202Albumin 1
Domain203-395Albumin 2
Domain396-593Albumin 3

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    600
  • Mass (Da)
    67,881
  • Last updated
    1996-11-01 v1
  • Checksum
    E45C871A670E740B
LLFLFSSAYSRGVFRRDTHKSEVAHRFKDLGEEHFKGLVLVAFSQYLQQCPFEEHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPPLVRPEVDVMCTAFHDNEATFLKKYLYEVARRHPYFYAPELLFFAARYKAAFAECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGDRAFKAWAVARLSQKFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYMCENQDSISSKLKECCDKPLLEKSHCLAEVENDEMPADLPSLAADYVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVMLLLRLAKAYEATLEKCCAAADPHECYAKVFDEFQPLVEEPQNLVKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGAKCCKLPEAKRMPCAEDYLSVVLNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALELDEAYVPKAFNAETFTFHADMCTLSEKEKQVKKQTALVELVKHKPKATKEQLKGVMDNFAAFVEKCCKADDKEACFAEEGPKFVAASQAALA

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M90463
EMBL· GenBank· DDBJ
AAA36906.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp