[1]	NUCLEOTIDE SEQUENCE [MRNA]. Holowachuk E.W., Stoltenborg J.K., Reed R.G., Peters T. Jr.; "Bovine serum albumin: cDNA sequence and expression."; Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-214. TISSUE=Liver; Barry T., Power S., Gannon F.; "The bovine serum albumin mRNA."; Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1046/j.1365-2249.2001.01451.x; PubMed=11298124 [NCBI, ExPASy, EBI, Israel, Japan] Hilger C., Grigioni F., De Beaufort C., Michel G., Freilinger J., Hentges F.; "Differential binding of IgG and IgA antibodies to antigenic determinants of bovine serum albumin."; Clin. Exp. Immunol. 123:387-394(2001).
[4]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-214. Wu H.T., Huang M.C.; "The complete cDNA sequence of bovine serum albumin."; Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-214. STRAIN=Hereford; TISSUE=Fetal liver, and Testis; NIH - Mammalian Gene Collection (MGC) project; Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[6]	PROTEIN SEQUENCE OF 1-32. PubMed=488109 [NCBI, ExPASy, EBI, Israel, Japan] McGillivray R.T.A., Chung D.W., Davie E.W.; "Biosynthesis of bovine plasma proteins in a cell-free system. Amino-terminal sequence of preproalbumin."; Eur. J. Biochem. 98:477-485(1979).
[7]	PROTEIN SEQUENCE OF 19-28. DOI=10.1016/0006-291X(77)91648-5; PubMed=843354 [NCBI, ExPASy, EBI, Israel, Japan] Patterson J.E., Geller D.M.; "Bovine microsomal albumin: amino terminal sequence of bovine proalbumin."; Biochem. Biophys. Res. Commun. 74:1220-1226(1977).
[8]	PROTEIN SEQUENCE, AND SEQUENCE REVISION TO 118-119 AND 180. DOI=10.1016/S0006-291X(05)80083-X; PubMed=2260975 [NCBI, ExPASy, EBI, Israel, Japan] Hirayama K., Akashi S., Furuya M., Fukuhara K.; "Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and Frit-FAB LC/MS."; Biochem. Biophys. Res. Commun. 173:639-646(1990).
[9]	PROTEIN SEQUENCE OF 25-424 AND 429-607, AND VARIANT THR-214. Brown J.R.; "Structure of bovine serum albumin."; Fed. Proc. 34:591-591(1975).
[10]	SEQUENCE REVISION TO 190-195. Brown J.R.; Submitted (APR-1975) to the PIR data bank.
[11]	PROTEIN SEQUENCE OF 25-64. PubMed=2379503 [NCBI, ExPASy, EBI, Israel, Japan] Strawich E., Glimcher M.J.; "Tooth 'enamelins' identified mainly as serum proteins. Major 'enamelin' is albumin."; Eur. J. Biochem. 191:47-56(1990).
[12]	PROTEIN SEQUENCE OF 25-41. DOI=10.1016/0003-2697(88)90082-6; PubMed=3389500 [NCBI, ExPASy, EBI, Israel, Japan] Hsieh J.C., Lin F.P., Tam M.F.; "Electroblotting onto glass-fiber filter from an analytical isoelectrofocusing gel: a preparative method for isolating proteins for N-terminal microsequencing."; Anal. Biochem. 170:1-8(1988).
[13]	PROTEIN SEQUENCE OF 163-172. PubMed=2474609 [NCBI, ExPASy, EBI, Israel, Japan] Carraway R.E., Cochrane D.E., Boucher W., Mitra S.P.; "Structures of histamine-releasing peptides formed by the action of acid proteases on mammalian albumin(s)."; J. Immunol. 143:1680-1684(1989).
[14]	PROTEIN SEQUENCE OF 165-173. TISSUE=Plasma; PubMed=2437111 [NCBI, ExPASy, EBI, Israel, Japan] Carraway R.E., Mitra S.P., Cochrane D.E.; "Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s)."; J. Biol. Chem. 262:5968-5973(1987).
[15]	PROTEIN SEQUENCE OF 402-433. PubMed=7283978 [NCBI, ExPASy, EBI, Israel, Japan] Reed R.G., Putnam F.W., Peters T. Jr.; "Sequence of residues 400-403 of bovine serum albumin."; Biochem. J. 191:867-868(1980).
[16]	PROTEIN SEQUENCE OF 437-451. Vilbois F.; Submitted (AUG-1998) to UniProtKB.
[17]	DISULFIDE BONDS. Brown J.R.; "Structure of serum albumin: disulfide bridges."; Fed. Proc. 33:1389-1389(1974).

Comments

FUNCTION: Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Plasma.
ALLERGEN: Causes an allergic reaction in human.
SIMILARITY: Belongs to the ALB/AFP/VDB family.
SIMILARITY: Contains 3 albumin domains.
CAUTION: A peptide arising from positions 165 to 173 was originally (PubMed:2437111) termed neurotensin-related peptide (NRP) and was thought to regulates fat digestion, lipid absorption, and blood flow.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M73993; AAA51411.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X58989; CAA41735.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y17769; CAA76847.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF542068; AAN17824.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102742; AAI02743.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC142272; AAI42273.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A38885; ABBOS.

NP_851335.1; -.

3D structure databases

HSSP

P02768; 1HK1. [HSSP ENTRY / PDB]

SMR

P02769; 27-607.

ModBase

P02769.

Ontologies

GO:0043234;	Cellular component: protein complex (inferred from sequence or structural similarity from UniProtKB).
GO:0003677;	Molecular function: DNA binding (inferred from sequence or structural similarity from UniProtKB).
GO:0008144;	Molecular function: drug binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005504;	Molecular function: fatty acid binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from sequence or structural similarity from UniProtKB).
GO:0030170;	Molecular function: pyridoxal phosphate binding (inferred from sequence or structural similarity from UniProtKB).
GO:0015643;	Molecular function: toxin binding (inferred from sequence or structural similarity from UniProtKB).
GO:0009267;	Biological process: cellular response to starvation (inferred from sequence or structural similarity from UniProtKB).
GO:0019836;	Biological process: hemolysis by symbiont of host red blood cells (inferred from sequence or structural similarity from UniProtKB).
GO:0051659;	Biological process: maintenance of mitochondrion location (inferred from sequence or structural similarity from UniProtKB).
GO:0043066;	Biological process: negative regulation of apoptosis (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001703; Alphafetoprot.
IPR000264; Serum_albumin.
IPR014760; Serum_albumin_N.
Graphical view of domain structure.

Pfam

PF00273; Serum_albumin; 3.
Pfam graphical view of domain structure.

PRINTS

PR00803; AFETOPROTEIN.
PR00802; SERUMALBUMIN.

ProDom

PD002486; Serum_albumin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00103; ALBUMIN; 3.
SMART graphical view of domain structure.

PROSITE

PS00212; ALBUMIN; 3.

BLOCKS

P02769.

Genome annotation databases

Ensembl

ENSBTAG00000017121; Bos taurus. [Contig view]

GeneID

280717; -.

KEGG

bta:280717; -.

Phylogenomic databases

HOVERGEN

P02769; -.

Other

ProtoNet

P02769.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allergen; Cleavage on pair of basic residues; Copper; Direct protein sequencing; Lipid-binding; Metal-binding; Phosphoprotein; Polymorphism; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`PROPEP`	`19 24`	`6`		`PRO_0000001057`
`CHAIN`	`25 607`	`583`	`Serum albumin.`	`PRO_0000001058`
`DOMAIN`	`25 204`	`180`	`Albumin 1.`
`DOMAIN`	`211 396`	`186`	`Albumin 2.`
`DOMAIN`	`403 594`	`192`	`Albumin 3.`
`METAL`	`27 27`		`Copper (By similarity).`
`MOD_RES`	`82 82`		`Phosphoserine (By similarity).`
`DISULFID`	`77 86`
`DISULFID`	`99 115`
`DISULFID`	`114 125`
`DISULFID`	`147 192`
`DISULFID`	`191 200`
`DISULFID`	`223 269`
`DISULFID`	`268 276`
`DISULFID`	`288 302`
`DISULFID`	`301 312`
`DISULFID`	`339 384`
`DISULFID`	`383 392`
`DISULFID`	`415 461`
`DISULFID`	`460 471`
`DISULFID`	`484 500`
`DISULFID`	`499 510`
`DISULFID`	`537 582`
`DISULFID`	`581 590`
`VARIANT`	`214 214`	`1`	`A -> T.`
`CONFLICT`	`58 58`		`Missing (in Ref. 11; AA sequence).`
`CONFLICT`	`116 116`		`E -> A (in Ref. 5; AAI02743).`
`CONFLICT`	`173 173`		`Y -> L (in Ref. 14; AA sequence).`
`CONFLICT`	`302 302`		`C -> K (in Ref. 9; AA sequence).`
`CONFLICT`	`304 305`		`KP -> PC (in Ref. 9; AA sequence).`
`CONFLICT`	`324 324`		`N -> D (in Ref. 9; AA sequence).`
`CONFLICT`	`394 395`		`ST -> TS (in Ref. 9; AA sequence).`
`CONFLICT`	`429 429`		`A -> E (in Ref. 5; AAI02743).`
`CONFLICT`	`437 437`		`K -> R (in Ref. 16; AA sequence).`
`CONFLICT`	`472 472`		`T -> A (in Ref. 5; AAI02743).`
`CONFLICT`	`493 494`		`SE -> ES (in Ref. 9; AA sequence).`
`CONFLICT`	`579 579`		`D -> G (in Ref. 5; AAI02743).`

Sequence information

Length: 607 AA [This is the length of the unprocessed precursor]

Molecular weight: 69293 Da [This is the MW of the unprocessed precursor]

CRC64: 39167DFE768585D4 [This is a checksum on the sequence]

        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

P02769 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools