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Serum albumin (BSA) (allergen Bos d 6)

 ALBU_BOVIN              Reviewed;         607 AA.
P02769; A5PJX3; O02787; P04277; Q3SZR2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 4.
30-AUG-2017, entry version 161.
RecName: Full=Serum albumin;
AltName: Full=BSA;
AltName: Allergen=Bos d 6;
Flags: Precursor;
Name=ALB;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[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;
PubMed=11298124; DOI=10.1046/j.1365-2249.2001.01451.x;
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; DOI=10.1111/j.1432-1033.1979.tb13209.x;
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.
PubMed=843354; DOI=10.1016/0006-291X(77)91648-5;
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.
PubMed=2260975; DOI=10.1016/S0006-291X(05)80083-X;
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; DOI=10.1111/j.1432-1033.1990.tb19092.x;
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.
PubMed=3389500; DOI=10.1016/0003-2697(88)90082-6;
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;
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;
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; DOI=10.1042/bj1910867;
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).
-!- 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. Major zinc transporter
in plasma, typically binds about 80% of all plasma zinc.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P02768}.
-!- ALLERGEN: Causes an allergic reaction in human.
-!- SIMILARITY: Belongs to the ALB/AFP/VDB family.
{ECO:0000255|PROSITE-ProRule:PRU00769}.
-!- CAUTION: A peptide arising from positions 165 to 173 was
originally termed neurotensin-related peptide (NRP) and was
thought to regulate fat digestion, lipid absorption, and blood
flow. {ECO:0000305|PubMed:2437111}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M73993; AAA51411.1; -; mRNA.
EMBL; X58989; CAA41735.1; -; mRNA.
EMBL; Y17769; CAA76847.1; -; mRNA.
EMBL; AF542068; AAN17824.1; -; mRNA.
EMBL; BC102742; AAI02743.1; -; mRNA.
EMBL; BC142272; AAI42273.1; -; mRNA.
PIR; A38885; ABBOS.
RefSeq; NP_851335.1; NM_180992.2.
UniGene; Bt.106669; -.
PDB; 2L7U; NMR; -; B=148-154.
PDB; 3V03; X-ray; 2.70 A; A/B=25-607.
PDB; 4F5S; X-ray; 2.47 A; A/B=25-607.
PDB; 4JK4; X-ray; 2.65 A; A/B=25-607.
PDB; 4OR0; X-ray; 2.58 A; A/B=25-607.
PDBsum; 2L7U; -.
PDBsum; 3V03; -.
PDBsum; 4F5S; -.
PDBsum; 4JK4; -.
PDBsum; 4OR0; -.
ProteinModelPortal; P02769; -.
SMR; P02769; -.
BioGrid; 158123; 5.
STRING; 9913.ENSBTAP00000022763; -.
BindingDB; P02769; -.
ChEMBL; CHEMBL3728; -.
Allergome; 165; Bos d 6.
Allergome; 3166; Bos d 6.0101.
PaxDb; P02769; -.
PeptideAtlas; P02769; -.
PRIDE; P02769; -.
GeneID; 280717; -.
KEGG; bta:280717; -.
CTD; 213; -.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
HOGENOM; HOG000293137; -.
HOVERGEN; HBG004207; -.
InParanoid; P02769; -.
KO; K16141; -.
TreeFam; TF335561; -.
PRO; PR:P02769; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; ISS:UniProtKB.
GO; GO:0051659; P:maintenance of mitochondrion location; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0006810; P:transport; IEA:InterPro.
CDD; cd00015; ALBUMIN; 3.
InterPro; IPR000264; ALB/AFP/VDB.
InterPro; IPR020858; Serum_albumin-like.
InterPro; IPR021177; Serum_albumin/AFP/Afamin.
InterPro; IPR020857; Serum_albumin_CS.
InterPro; IPR014760; Serum_albumin_N.
PANTHER; PTHR11385; PTHR11385; 1.
Pfam; PF00273; Serum_albumin; 3.
PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
PRINTS; PR00803; AFETOPROTEIN.
PRINTS; PR00802; SERUMALBUMIN.
SMART; SM00103; ALBUMIN; 3.
SUPFAM; SSF48552; SSF48552; 3.
PROSITE; PS00212; ALBUMIN_1; 3.
PROSITE; PS51438; ALBUMIN_2; 3.
1: Evidence at protein level;
3D-structure; Allergen; Cleavage on pair of basic residues;
Complete proteome; Copper; Direct protein sequencing; Disulfide bond;
Lipid-binding; Metal-binding; Methylation; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Secreted; Signal; Zinc.
SIGNAL 1 18 {ECO:0000269|PubMed:843354}.
PROPEP 19 24
/FTId=PRO_0000001057.
CHAIN 25 607 Serum albumin.
/FTId=PRO_0000001058.
DOMAIN 19 209 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 210 402 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 403 600 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
METAL 27 27 Copper. {ECO:0000250}.
METAL 91 91 Zinc. {ECO:0000250}.
METAL 123 123 Zinc. {ECO:0000250}.
METAL 270 270 Zinc. {ECO:0000250}.
METAL 272 272 Zinc. {ECO:0000250}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 107 107 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 228 228 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 443 443 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 445 445 Phosphothreonine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 557 557 N6-methyllysine.
{ECO:0000250|UniProtKB:P02768}.
MOD_RES 569 569 Phosphothreonine.
{ECO:0000250|UniProtKB:P02770}.
MOD_RES 587 587 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
DISULFID 77 86 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 99 115 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 114 125 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 147 192 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 191 200 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 223 269 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 268 276 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 288 302 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 301 312 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 339 384 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 383 392 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 415 461 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 460 471 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 484 500 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 499 510 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 537 582 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
DISULFID 581 590 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.17}.
VARIANT 214 214 A -> T. {ECO:0000269|Ref.2,
ECO:0000269|Ref.4, ECO:0000269|Ref.5,
ECO:0000269|Ref.9}.
CONFLICT 58 58 Missing (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 116 116 E -> A (in Ref. 5; AAI02743).
{ECO:0000305}.
CONFLICT 173 173 Y -> L (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 302 302 C -> K (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 304 305 KP -> PC (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 324 324 N -> D (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 394 395 ST -> TS (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 429 429 A -> E (in Ref. 5; AAI02743).
{ECO:0000305}.
CONFLICT 437 437 K -> R (in Ref. 16; AA sequence).
{ECO:0000305}.
CONFLICT 472 472 T -> A (in Ref. 5; AAI02743).
{ECO:0000305}.
CONFLICT 493 494 SE -> ES (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 579 579 D -> G (in Ref. 5; AAI02743).
{ECO:0000305}.
HELIX 30 38 {ECO:0000244|PDB:4F5S}.
HELIX 40 54 {ECO:0000244|PDB:4F5S}.
STRAND 56 58 {ECO:0000244|PDB:4F5S}.
HELIX 60 79 {ECO:0000244|PDB:4F5S}.
TURN 84 87 {ECO:0000244|PDB:4F5S}.
HELIX 90 99 {ECO:0000244|PDB:4F5S}.
HELIX 104 108 {ECO:0000244|PDB:4F5S}.
HELIX 109 116 {ECO:0000244|PDB:4F5S}.
HELIX 121 127 {ECO:0000244|PDB:4F5S}.
HELIX 143 152 {ECO:0000244|PDB:4F5S}.
HELIX 154 168 {ECO:0000244|PDB:4F5S}.
HELIX 174 191 {ECO:0000244|PDB:4F5S}.
STRAND 194 196 {ECO:0000244|PDB:4OR0}.
HELIX 197 229 {ECO:0000244|PDB:4F5S}.
HELIX 231 245 {ECO:0000244|PDB:4F5S}.
HELIX 251 269 {ECO:0000244|PDB:4F5S}.
HELIX 273 288 {ECO:0000244|PDB:4F5S}.
HELIX 291 294 {ECO:0000244|PDB:4F5S}.
HELIX 296 298 {ECO:0000244|PDB:4JK4}.
HELIX 301 303 {ECO:0000244|PDB:4F5S}.
HELIX 306 315 {ECO:0000244|PDB:4F5S}.
HELIX 329 332 {ECO:0000244|PDB:4F5S}.
HELIX 338 344 {ECO:0000244|PDB:4F5S}.
HELIX 346 360 {ECO:0000244|PDB:4F5S}.
HELIX 366 385 {ECO:0000244|PDB:4F5S}.
STRAND 386 388 {ECO:0000244|PDB:4JK4}.
HELIX 389 393 {ECO:0000244|PDB:4F5S}.
HELIX 396 403 {ECO:0000244|PDB:4F5S}.
TURN 404 407 {ECO:0000244|PDB:4F5S}.
HELIX 408 437 {ECO:0000244|PDB:4F5S}.
HELIX 443 460 {ECO:0000244|PDB:4F5S}.
STRAND 461 463 {ECO:0000244|PDB:4F5S}.
HELIX 465 489 {ECO:0000244|PDB:4F5S}.
HELIX 494 502 {ECO:0000244|PDB:4F5S}.
HELIX 507 512 {ECO:0000244|PDB:4F5S}.
STRAND 518 520 {ECO:0000244|PDB:4JK4}.
HELIX 527 530 {ECO:0000244|PDB:4F5S}.
HELIX 534 537 {ECO:0000244|PDB:4F5S}.
HELIX 541 558 {ECO:0000244|PDB:4F5S}.
HELIX 564 583 {ECO:0000244|PDB:4F5S}.
STRAND 584 586 {ECO:0000244|PDB:4OR0}.
HELIX 587 606 {ECO:0000244|PDB:4F5S}.
SEQUENCE 607 AA; 69293 MW; 39167DFE768585D4 CRC64;
MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA FSQYLQQCPF
DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK VASLRETYGD MADCCEKQEP
ERNECFLSHK DDSPDLPKLK PDPNTLCDEF KADEKKFWGK YLYEIARRHP YFYAPELLYY
ANKYNGVFQE CCQAEDKGAC LLPKIETMRE KVLASSARQR LRCASIQKFG ERALKAWSVA
RLSQKFPKAE FVEVTKLVTD LTKVHKECCH GDLLECADDR ADLAKYICDN QDTISSKLKE
CCDKPLLEKS HCIAEVEKDA IPENLPPLTA DFAEDKDVCK NYQEAKDAFL GSFLYEYSRR
HPEYAVSVLL RLAKEYEATL EECCAKDDPH ACYSTVFDKL KHLVDEPQNL IKQNCDQFEK
LGEYGFQNAL IVRYTRKVPQ VSTPTLVEVS RSLGKVGTRC CTKPESERMP CTEDYLSLIL
NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSALTPDETY VPKAFDEKLF TFHADICTLP
DTEKQIKKQT ALVELLKHKP KATEEQLKTV MENFVAFVDK CCAADDKEAC FAVEGPKLVV
STQTALA


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