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P02769 (ALBU_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum albumin
Alternative name(s):
BSA
Allergen=Bos d 6
Gene names
Name:ALB
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serum albumin, the main protein of plasma, has a good binding capacity for 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.

Subcellular location

Secreted.

Tissue specificity

Plasma.

Post-translational modification

Phosphorylation sites are present in the extracellular medium By similarity.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Caution

A peptide arising from positions 165 to 173 was originally (Ref.14) termed neurotensin-related peptide (NRP) and was thought to regulate fat digestion, lipid absorption, and blood flow.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseAllergen
   DomainRepeat
Signal
   LigandCopper
Lipid-binding
Metal-binding
Zinc
   PTMCleavage on pair of basic residues
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to starvation

Inferred from sequence or structural similarity. Source: UniProtKB

hemolysis by symbiont of host erythrocytes

Inferred from sequence or structural similarity. Source: UniProtKB

maintenance of mitochondrion location

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

transport

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxygen binding

Inferred from electronic annotation. Source: Ensembl

pyridoxal phosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

toxic substance binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.7
Propeptide19 – 224
PRO_0000001057
Chain25 – 607583Serum albumin
PRO_0000001058

Regions

Domain19 – 209191Albumin 1
Domain210 – 402193Albumin 2
Domain403 – 600198Albumin 3

Sites

Metal binding271Copper By similarity
Metal binding911Zinc By similarity
Metal binding1231Zinc By similarity
Metal binding2701Zinc By similarity
Metal binding2721Zinc By similarity

Amino acid modifications

Modified residue821Phosphoserine By similarity
Modified residue2281N6-succinyllysine By similarity
Modified residue4421Phosphoserine By similarity
Modified residue4431Phosphothreonine By similarity
Modified residue4451Phosphothreonine By similarity
Modified residue5871N6-succinyllysine By similarity
Disulfide bond77 ↔ 86 Ref.17
Disulfide bond99 ↔ 115 Ref.17
Disulfide bond114 ↔ 125 Ref.17
Disulfide bond147 ↔ 192 Ref.17
Disulfide bond191 ↔ 200 Ref.17
Disulfide bond223 ↔ 269 Ref.17
Disulfide bond268 ↔ 276 Ref.17
Disulfide bond288 ↔ 302 Ref.17
Disulfide bond301 ↔ 312 Ref.17
Disulfide bond339 ↔ 384 Ref.17
Disulfide bond383 ↔ 392 Ref.17
Disulfide bond415 ↔ 461 Ref.17
Disulfide bond460 ↔ 471 Ref.17
Disulfide bond484 ↔ 500 Ref.17
Disulfide bond499 ↔ 510 Ref.17
Disulfide bond537 ↔ 582 Ref.17
Disulfide bond581 ↔ 590 Ref.17

Natural variations

Natural variant2141A → T. Ref.2 Ref.4 Ref.5 Ref.9

Experimental info

Sequence conflict581Missing AA sequence Ref.11
Sequence conflict1161E → A in AAI02743. Ref.5
Sequence conflict1731Y → L AA sequence Ref.14
Sequence conflict3021C → K AA sequence Ref.9
Sequence conflict304 – 3052KP → PC AA sequence Ref.9
Sequence conflict3241N → D AA sequence Ref.9
Sequence conflict394 – 3952ST → TS AA sequence Ref.9
Sequence conflict4291A → E in AAI02743. Ref.5
Sequence conflict4371K → R AA sequence Ref.16
Sequence conflict4721T → A in AAI02743. Ref.5
Sequence conflict493 – 4942SE → ES AA sequence Ref.9
Sequence conflict5791D → G in AAI02743. Ref.5

Secondary structure

............................................................................ 607
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02769 [UniParc].

Last modified February 1, 1996. Version 4.
Checksum: 39167DFE768585D4

FASTA60769,293
        10         20         30         40         50         60 
MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA FSQYLQQCPF 

        70         80         90        100        110        120 
DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK VASLRETYGD MADCCEKQEP 

       130        140        150        160        170        180 
ERNECFLSHK DDSPDLPKLK PDPNTLCDEF KADEKKFWGK YLYEIARRHP YFYAPELLYY 

       190        200        210        220        230        240 
ANKYNGVFQE CCQAEDKGAC LLPKIETMRE KVLASSARQR LRCASIQKFG ERALKAWSVA 

       250        260        270        280        290        300 
RLSQKFPKAE FVEVTKLVTD LTKVHKECCH GDLLECADDR ADLAKYICDN QDTISSKLKE 

       310        320        330        340        350        360 
CCDKPLLEKS HCIAEVEKDA IPENLPPLTA DFAEDKDVCK NYQEAKDAFL GSFLYEYSRR 

       370        380        390        400        410        420 
HPEYAVSVLL RLAKEYEATL EECCAKDDPH ACYSTVFDKL KHLVDEPQNL IKQNCDQFEK 

       430        440        450        460        470        480 
LGEYGFQNAL IVRYTRKVPQ VSTPTLVEVS RSLGKVGTRC CTKPESERMP CTEDYLSLIL 

       490        500        510        520        530        540 
NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSALTPDETY VPKAFDEKLF TFHADICTLP 

       550        560        570        580        590        600 
DTEKQIKKQT ALVELLKHKP KATEEQLKTV MENFVAFVDK CCAADDKEAC FAVEGPKLVV 


STQTALA 

« Hide

References

« Hide 'large scale' references
[1]"Bovine serum albumin: cDNA sequence and expression."
Holowachuk E.W., Stoltenborg J.K., Reed R.G., Peters T. Jr.
Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The bovine serum albumin mRNA."
Barry T., Power S., Gannon F.
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-214.
Tissue: Liver.
[3]"Differential binding of IgG and IgA antibodies to antigenic determinants of bovine serum albumin."
Hilger C., Grigioni F., De Beaufort C., Michel G., Freilinger J., Hentges F.
Clin. Exp. Immunol. 123:387-394(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"The complete cDNA sequence of bovine serum albumin."
Wu H.T., Huang M.C.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-214.
[5]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-214.
Strain: Hereford.
Tissue: Fetal liver and Testis.
[6]"Biosynthesis of bovine plasma proteins in a cell-free system. Amino-terminal sequence of preproalbumin."
McGillivray R.T.A., Chung D.W., Davie E.W.
Eur. J. Biochem. 98:477-485(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-32.
[7]"Bovine microsomal albumin: amino terminal sequence of bovine proalbumin."
Patterson J.E., Geller D.M.
Biochem. Biophys. Res. Commun. 74:1220-1226(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-28.
[8]"Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and Frit-FAB LC/MS."
Hirayama K., Akashi S., Furuya M., Fukuhara K.
Biochem. Biophys. Res. Commun. 173:639-646(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, SEQUENCE REVISION TO 118-119 AND 180.
[9]"Structure of bovine serum albumin."
Brown J.R.
Fed. Proc. 34:591-591(1975)
Cited for: PROTEIN SEQUENCE OF 25-424 AND 429-607, VARIANT THR-214.
[10]Brown J.R.
Submitted (APR-1975) to the PIR data bank
Cited for: SEQUENCE REVISION TO 190-195.
[11]"Tooth 'enamelins' identified mainly as serum proteins. Major 'enamelin' is albumin."
Strawich E., Glimcher M.J.
Eur. J. Biochem. 191:47-56(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-64.
[12]"Electroblotting onto glass-fiber filter from an analytical isoelectrofocusing gel: a preparative method for isolating proteins for N-terminal microsequencing."
Hsieh J.C., Lin F.P., Tam M.F.
Anal. Biochem. 170:1-8(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-41.
[13]"Structures of histamine-releasing peptides formed by the action of acid proteases on mammalian albumin(s)."
Carraway R.E., Cochrane D.E., Boucher W., Mitra S.P.
J. Immunol. 143:1680-1684(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 163-172.
[14]"Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s)."
Carraway R.E., Mitra S.P., Cochrane D.E.
J. Biol. Chem. 262:5968-5973(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 165-173.
Tissue: Plasma.
[15]"Sequence of residues 400-403 of bovine serum albumin."
Reed R.G., Putnam F.W., Peters T. Jr.
Biochem. J. 191:867-868(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 402-433.
[16]Vilbois F.
Submitted (AUG-1998) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 437-451.
[17]"Structure of serum albumin: disulfide bridges."
Brown J.R.
Fed. Proc. 33:1389-1389(1974)
Cited for: DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73993 mRNA. Translation: AAA51411.1.
X58989 mRNA. Translation: CAA41735.1.
Y17769 mRNA. Translation: CAA76847.1.
AF542068 mRNA. Translation: AAN17824.1.
BC102742 mRNA. Translation: AAI02743.1.
BC142272 mRNA. Translation: AAI42273.1.
PIRABBOS. A38885.
RefSeqNP_851335.1. NM_180992.2.
UniGeneBt.106669.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L7UNMR-B148-154[»]
3V03X-ray2.70A/B25-607[»]
4F5SX-ray2.47A/B25-607[»]
4JK4X-ray2.65A/B25-607[»]
ProteinModelPortalP02769.
SMRP02769. Positions 29-584.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid158123. 5 interactions.
STRING9913.ENSBTAP00000022763.

Chemistry

BindingDBP02769.
ChEMBLCHEMBL3728.

Protein family/group databases

Allergome165. Bos d 6.
3166. Bos d 6.0101.

Proteomic databases

PaxDbP02769.
PRIDEP02769.
ProMEXP02769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000022763; ENSBTAP00000022763; ENSBTAG00000017121.
GeneID280717.
KEGGbta:280717.

Organism-specific databases

CTD213.

Phylogenomic databases

eggNOGNOG45992.
GeneTreeENSGT00390000000113.
HOGENOMHOG000293137.
HOVERGENHBG004207.
InParanoidP02769.
KOK16141.
OrthoDBEOG7S4X5C.
TreeFamTF335561.

Enzyme and pathway databases

ReactomeREACT_227097. Immune System.

Family and domain databases

InterProIPR000264. ALB/AFP/VDB.
IPR001703. Alpha-fetoprotein.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSPR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMSSF48552. SSF48552. 3 hits.
PROSITEPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804896.

Entry information

Entry nameALBU_BOVIN
AccessionPrimary (citable) accession number: P02769
Secondary accession number(s): A5PJX3 expand/collapse secondary AC list , O02787, P04277, Q3SZR2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Allergens

Nomenclature of allergens and list of entries