P02769 (ALBU_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serum albumin

Alternative name(s):
BSA
Allergen=Bos d 6

Gene names

Name:

ALB

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	607 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Coding sequence diversity	Polymorphism
Disease	Allergen
Domain	Repeat Signal
Ligand	Copper Lipid-binding Metal-binding Zinc
PTM	Cleavage on pair of basic residues Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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_component	cytoplasm Inferred from electronic annotation. Source: Compara extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara protein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA 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: Compara pyridoxal phosphate binding Inferred from sequence or structural similarity. Source: UniProtKB toxin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.7

Propeptide

19 – 22

4

PRO_0000001057

Chain

25 – 607

583

Serum albumin

PRO_0000001058

Regions

Domain

19 – 209

191

Albumin 1

Domain

210 – 402

193

Albumin 2

Domain

403 – 600

198

Albumin 3

Sites

Metal binding

27

1

Copper By similarity

Metal binding

91

1

Zinc By similarity

Metal binding

123

1

Zinc By similarity

Metal binding

270

1

Zinc By similarity

Metal binding

272

1

Zinc By similarity

Amino acid modifications

Modified residue

82

1

Phosphoserine By similarity

Modified residue

442

1

Phosphoserine By similarity

Modified residue

443

1

Phosphothreonine By similarity

Modified residue

445

1

Phosphothreonine By similarity

Disulfide bond

77 ↔ 86

Ref.17

Disulfide bond

99 ↔ 115

Ref.17

Disulfide bond

114 ↔ 125

Ref.17

Disulfide bond

147 ↔ 192

Ref.17

Disulfide bond

191 ↔ 200

Ref.17

Disulfide bond

223 ↔ 269

Ref.17

Disulfide bond

268 ↔ 276

Ref.17

Disulfide bond

288 ↔ 302

Ref.17

Disulfide bond

301 ↔ 312

Ref.17

Disulfide bond

339 ↔ 384

Ref.17

Disulfide bond

383 ↔ 392

Ref.17

Disulfide bond

415 ↔ 461

Ref.17

Disulfide bond

460 ↔ 471

Ref.17

Disulfide bond

484 ↔ 500

Ref.17

Disulfide bond

499 ↔ 510

Ref.17

Disulfide bond

537 ↔ 582

Ref.17

Disulfide bond

581 ↔ 590

Ref.17

Natural variations

Natural variant

214

1

A → T. Ref.2 Ref.4 Ref.5 Ref.9

Experimental info

Sequence conflict

58

1

Missing AA sequence Ref.11

Sequence conflict

116

1

E → A in AAI02743. Ref.5

Sequence conflict

173

1

Y → L AA sequence Ref.14

Sequence conflict

302

1

C → K AA sequence Ref.9

Sequence conflict

304 – 305

2

KP → PC AA sequence Ref.9

Sequence conflict

324

1

N → D AA sequence Ref.9

Sequence conflict

394 – 395

2

ST → TS AA sequence Ref.9

Sequence conflict

429

1

A → E in AAI02743. Ref.5

Sequence conflict

437

1

K → R AA sequence Ref.16

Sequence conflict

472

1

T → A in AAI02743. Ref.5

Sequence conflict

493 – 494

2

SE → ES AA sequence Ref.9

Sequence conflict

579

1

D → G in AAI02743. Ref.5

Secondary structure

1

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607

Helix Strand Turn

Details...

Helix

30 – 38

9

Helix

40 – 54

15

Beta strand

56 – 58

3

Helix

60 – 79

20

Turn

84 – 87

4

Helix

90 – 99

10

Helix

104 – 108

5

Helix

109 – 116

8

Helix

121 – 127

7

Helix

143 – 152

10

Helix

154 – 168

15

Helix

174 – 191

18

Beta strand

194 – 196

3

Helix

197 – 229

33

Helix

231 – 245

15

Helix

251 – 269

19

Helix

273 – 288

16

Helix

291 – 294

4

Helix

301 – 303

3

Helix

306 – 315

10

Helix

329 – 332

4

Helix

338 – 344

7

Helix

346 – 360

15

Helix

366 – 385

20

Helix

389 – 393

5

Helix

396 – 403

8

Turn

404 – 407

4

Helix

408 – 437

30

Helix

443 – 460

18

Beta strand

461 – 463

3

Helix

465 – 489

25

Helix

494 – 502

9

Helix

507 – 512

6

Helix

527 – 530

4

Helix

534 – 537

4

Helix

541 – 558

18

Helix

564 – 583

20

Helix

587 – 606

20

Sequences

	Sequence		Length	Mass (Da)
	P02769 [UniParc]. Last modified February 1, 1996. Version 4. Checksum: 39167DFE768585D4	FASTA	607	69,293
	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

References

	« Hide 'large scale' referencesShow '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.

IPI

IPI01028455.

PIR

ABBOS. A38885.

RefSeq

NP_851335.1. NM_180992.2.

UniGene

Bt.106669.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L7U	NMR	-	B	148-154	[»]
3V03	X-ray	2.70	A/B	25-607	[»]
4F5S	X-ray	2.47	A/B	25-607	[»]

ProteinModelPortal

P02769.

SMR

P02769. Positions 29-584.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000022763.

Protein family/group databases

Allergome

165. Bos d 6.
3166. Bos d 6.0101.

Proteomic databases

PaxDb

P02769.

PRIDE

P02769.

ProMEX

P02769.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000022763; ENSBTAP00000022763; ENSBTAG00000017121.

GeneID

280717.

KEGG

bta:280717.

Organism-specific databases

CTD

213.

Phylogenomic databases

eggNOG

NOG45992.

GeneTree

ENSGT00390000000113.

HOGENOM

HOG000293137.

HOVERGEN

HBG004207.

InParanoid

P02769.

KO

K16141.

OrthoDB

EOG4Z0B55.

Enzyme and pathway databases

Reactome

REACT_109781. Immune System.

Family and domain databases

InterPro

IPR000264. ALB/AFP/VDB.
IPR001703. Alpha-fetoprotein.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]

Pfam

PF00273. Serum_albumin. 3 hits.
[Graphical view]

PIRSF

PIRSF002520. Serum_albumin_subgroup. 1 hit.

PRINTS

PR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.

SMART

SM00103. ALBUMIN. 3 hits.
[Graphical view]

SUPFAM

SSF48552. Serum_albumin. 3 hits.

PROSITE

PS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02769.

ChEMBL

CHEMBL3728.

NextBio

20804896.

Entry information

Entry name

ALBU_BOVIN

Accession

Primary (citable) accession number: P02769
Secondary accession number(s): A5PJX3 , O02787, P04277, Q3SZR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 127 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program