ID   ALBU_BOVIN              Reviewed;         607 AA.
AC   P02769; A5PJX3; O02787; P04277; Q3SZR2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 4.
DT   02-SEP-2026, entry version 201.
DE   RecName: Full=Albumin;
DE   AltName: Full=BSA;
DE   AltName: Allergen=Bos d 6;
DE   Flags: Precursor;
GN   Name=ALB;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Holowachuk E.W., Stoltenborg J.K., Reed R.G., Peters T. Jr.;
RT   "Bovine serum albumin: cDNA sequence and expression.";
RL   Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-214.
RC   TISSUE=Liver;
RA   Barry T., Power S., Gannon F.;
RT   "The bovine serum albumin mRNA.";
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=11298124; DOI=10.1046/j.1365-2249.2001.01451.x;
RA   Hilger C., Grigioni F., De Beaufort C., Michel G., Freilinger J.,
RA   Hentges F.;
RT   "Differential binding of IgG and IgA antibodies to antigenic determinants
RT   of bovine serum albumin.";
RL   Clin. Exp. Immunol. 123:387-394(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-214.
RA   Wu H.T., Huang M.C.;
RT   "The complete cDNA sequence of bovine serum albumin.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-214.
RC   STRAIN=Hereford; TISSUE=Fetal liver, and Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 1-32 (PRECURSOR PROTEIN).
RX   PubMed=488109; DOI=10.1111/j.1432-1033.1979.tb13209.x;
RA   McGillivray R.T.A., Chung D.W., Davie E.W.;
RT   "Biosynthesis of bovine plasma proteins in a cell-free system. Amino-
RT   terminal sequence of preproalbumin.";
RL   Eur. J. Biochem. 98:477-485(1979).
RN   [7]
RP   PROTEIN SEQUENCE OF 19-28.
RX   PubMed=843354; DOI=10.1016/0006-291x(77)91648-5;
RA   Patterson J.E., Geller D.M.;
RT   "Bovine microsomal albumin: amino terminal sequence of bovine proalbumin.";
RL   Biochem. Biophys. Res. Commun. 74:1220-1226(1977).
RN   [8]
RP   PARTIAL PROTEIN SEQUENCE, AND SEQUENCE REVISION TO 118-119 AND 180.
RX   PubMed=2260975; DOI=10.1016/s0006-291x(05)80083-x;
RA   Hirayama K., Akashi S., Furuya M., Fukuhara K.;
RT   "Rapid confirmation and revision of the primary structure of bovine serum
RT   albumin by ESIMS and Frit-FAB LC/MS.";
RL   Biochem. Biophys. Res. Commun. 173:639-646(1990).
RN   [9]
RP   PROTEIN SEQUENCE OF 25-424 AND 429-607, AND VARIANT THR-214.
RA   Brown J.R.;
RT   "Structure of bovine serum albumin.";
RL   Fed. Proc. 34:591-591(1975).
RN   [10]
RP   SEQUENCE REVISION TO 190-195.
RA   Brown J.R.;
RL   Submitted (APR-1975) to the PIR data bank.
RN   [11]
RP   PROTEIN SEQUENCE OF 25-64.
RX   PubMed=2379503; DOI=10.1111/j.1432-1033.1990.tb19092.x;
RA   Strawich E., Glimcher M.J.;
RT   "Tooth 'enamelins' identified mainly as serum proteins. Major 'enamelin' is
RT   albumin.";
RL   Eur. J. Biochem. 191:47-56(1990).
RN   [12]
RP   PROTEIN SEQUENCE OF 25-41.
RX   PubMed=3389500; DOI=10.1016/0003-2697(88)90082-6;
RA   Hsieh J.C., Lin F.P., Tam M.F.;
RT   "Electroblotting onto glass-fiber filter from an analytical
RT   isoelectrofocusing gel: a preparative method for isolating proteins for N-
RT   terminal microsequencing.";
RL   Anal. Biochem. 170:1-8(1988).
RN   [13]
RP   PROTEIN SEQUENCE OF 163-172.
RX   PubMed=2474609; DOI=10.4049/jimmunol.143.5.1680;
RA   Carraway R.E., Cochrane D.E., Boucher W., Mitra S.P.;
RT   "Structures of histamine-releasing peptides formed by the action of acid
RT   proteases on mammalian albumin(s).";
RL   J. Immunol. 143:1680-1684(1989).
RN   [14]
RP   PROTEIN SEQUENCE OF 165-173.
RC   TISSUE=Plasma;
RX   PubMed=2437111; DOI=10.1016/s0021-9258(18)45523-8;
RA   Carraway R.E., Mitra S.P., Cochrane D.E.;
RT   "Structure of a biologically active neurotensin-related peptide obtained
RT   from pepsin-treated albumin(s).";
RL   J. Biol. Chem. 262:5968-5973(1987).
RN   [15]
RP   PROTEIN SEQUENCE OF 402-433.
RX   PubMed=7283978; DOI=10.1042/bj1910867;
RA   Reed R.G., Putnam F.W., Peters T. Jr.;
RT   "Sequence of residues 400-403 of bovine serum albumin.";
RL   Biochem. J. 191:867-868(1980).
RN   [16]
RP   PROTEIN SEQUENCE OF 437-451.
RA   Vilbois F.;
RL   Submitted (AUG-1998) to UniProtKB.
RN   [17]
RP   DISULFIDE BONDS.
RA   Brown J.R.;
RT   "Structure of serum albumin: disulfide bridges.";
RL   Fed. Proc. 33:1389-1389(1974).
RN   [18]
RP   FUNCTION.
RX   PubMed=6234017; DOI=10.1021/bi00305a003;
RA   Konopka K., Neilands J.B.;
RT   "Effect of serum albumin on siderophore-mediated utilization of transferrin
RT   iron.";
RL   Biochemistry 23:2122-2127(1984).
RN   [19] {ECO:0007744|PDB:2L7U}
RP   STRUCTURE BY NMR OF 148-154, AND GLYCATION AT LYS-151.
RX   PubMed=21565706; DOI=10.1016/j.str.2011.02.013;
RA   Xue J., Rai V., Singer D., Chabierski S., Xie J., Reverdatto S., Burz D.S.,
RA   Schmidt A.M., Hoffmann R., Shekhtman A.;
RT   "Advanced glycation end product recognition by the receptor for AGEs.";
RL   Structure 19:722-732(2011).
RN   [20] {ECO:0007744|PDB:4F5S}
RP   X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 25-607, DISULFIDE BONDS, AND
RP   VARIANT THR-214.
RX   PubMed=22993082; DOI=10.1107/s0907444912027047;
RA   Bujacz A.;
RT   "Structures of bovine, equine and leporine serum albumin.";
RL   Acta Crystallogr. D 68:1278-1289(2012).
RN   [21] {ECO:0007744|PDB:3V03}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 25-607 IN COMPLEX WITH CALCIUM,
RP   FUNCTION, AND DISULFIDE BONDS.
RX   PubMed=22677715; DOI=10.1016/j.molimm.2012.05.011;
RA   Majorek K.A., Porebski P.J., Dayal A., Zimmerman M.D., Jablonska K.,
RA   Stewart A.J., Chruszcz M., Minor W.;
RT   "Structural and immunologic characterization of bovine, horse, and rabbit
RT   serum albumins.";
RL   Mol. Immunol. 52:174-182(2012).
RN   [22] {ECO:0007744|PDB:4JK4}
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-607 IN COMPLEX WITH CALCIUM,
RP   AND DISULFIDE BONDS.
RX   PubMed=23769932; DOI=10.1016/j.ijbiomac.2013.06.004;
RA   Sekula B., Zielinski K., Bujacz A.;
RT   "Crystallographic studies of the complexes of bovine and equine serum
RT   albumin with 3,5-diiodosalicylic acid.";
RL   Int. J. Biol. Macromol. 60:316-324(2013).
RN   [23] {ECO:0007744|PDB:4OR0}
RP   X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 25-607, AND DISULFIDE BONDS.
RX   PubMed=24753230; DOI=10.1002/prot.24583;
RA   Bujacz A., Zielinski K., Sekula B.;
RT   "Structural studies of bovine, equine, and leporine serum albumin complexes
RT   with naproxen.";
RL   Proteins 82:2199-2208(2014).
CC   -!- FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones,
CC       bilirubin and drugs. Its main function is the regulation of the
CC       colloidal osmotic pressure of blood. Major zinc transporter in plasma,
CC       typically binds about 80% of all plasma zinc (By similarity). Major
CC       calcium and magnesium transporter in plasma, binds approximately 45% of
CC       circulating calcium and magnesium in plasma (Probable). Potentially has
CC       more than two calcium-binding sites and might additionally bind calcium
CC       in a non-specific manner (PubMed:22677715). The shared binding site
CC       between zinc and calcium at residue Asp-272 suggests a crosstalk
CC       between zinc and calcium transport in the blood (Probable). The rank
CC       order of affinity is zinc > calcium > magnesium (Probable). Binds to
CC       the bacterial siderophore enterobactin and inhibits enterobactin-
CC       mediated iron uptake of E.coli, and may thereby limit the utilization
CC       of iron and growth of enteric bacteria such as E.coli (PubMed:6234017).
CC       Does not prevent iron uptake by the bacterial siderophore aerobactin
CC       (PubMed:6234017). {ECO:0000250|UniProtKB:P02768,
CC       ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:6234017,
CC       ECO:0000305|PubMed:22677715}.
CC   -!- SUBUNIT: Interacts with FCGRT; this interaction regulates ALB
CC       homeostasis (By similarity). In plasma, occurs in a covalently-linked
CC       complex with chromophore-bound alpha-1-microglobulin; this interaction
CC       does not prevent fatty acid binding to ALB.
CC       {ECO:0000250|UniProtKB:P02768}.
CC   -!- INTERACTION:
CC       P02769; Q9BXI9-2: C1QTNF6; Xeno; NbExp=4; IntAct=EBI-2296927, EBI-27104631;
CC       P02769; P08603: CFH; Xeno; NbExp=10; IntAct=EBI-2296927, EBI-1223708;
CC       P02769; PRO_0000009136 [O00602]: FCN1; Xeno; NbExp=2; IntAct=EBI-2296927, EBI-11784425;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P02768}.
CC   -!- ALLERGEN: Can cause allergic reactions in humans.
CC   -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00769}.
CC   -!- CAUTION: A peptide arising from positions 165 to 173 was originally
CC       termed neurotensin-related peptide (NRP) and was thought to regulate
CC       fat digestion, lipid absorption, and blood flow.
CC       {ECO:0000305|PubMed:2437111}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M73993; AAA51411.1; -; mRNA.
DR   EMBL; X58989; CAA41735.1; -; mRNA.
DR   EMBL; Y17769; CAA76847.1; -; mRNA.
DR   EMBL; AF542068; AAN17824.1; -; mRNA.
DR   EMBL; BC102742; AAI02743.1; -; mRNA.
DR   EMBL; BC142272; AAI42273.1; -; mRNA.
DR   PIR; A38885; ABBOS.
DR   RefSeq; NP_851335.1; NM_180992.2.
DR   PDB; 2L7U; NMR; -; B=148-154.
DR   PDB; 3V03; X-ray; 2.70 A; A/B=25-607.
DR   PDB; 4F5S; X-ray; 2.47 A; A/B=25-607.
DR   PDB; 4JK4; X-ray; 2.65 A; A/B=25-607.
DR   PDB; 4OR0; X-ray; 2.58 A; A/B=25-607.
DR   PDB; 6QS9; X-ray; 2.80 A; A/B=1-607.
DR   PDB; 6RJV; X-ray; 3.21 A; A/B=25-607.
DR   PDB; 8KFO; X-ray; 3.60 A; A/B=1-607.
DR   PDB; 8WDD; X-ray; 3.90 A; A/B=25-607.
DR   PDB; 9QQD; EM; 3.10 A; A=28-605.
DR   AlphaFoldDB; P02769; -.
DR   BMRB; P02769; -.
DR   EMDB; EMD-10794; -.
DR   EMDB; EMD-53298; -.
DR   MDRepo; P02769; -.
DR   SASBDB; P02769; -.
DR   SMR; P02769; -.
DR   BioGRID; 158123; 5.
DR   FunCoup; P02769; 275.
DR   IntAct; P02769; 15.
DR   STRING; 9913.ENSBTAP00000022763; -.
DR   BindingDB; P02769; -.
DR   ChEMBL; CHEMBL3728; -.
DR   DrugCentral; P02769; -.
DR   Allergome; 165; Bos d 6.
DR   Allergome; 3166; Bos d 6.0101.
DR   CarbonylDB; P02769; -.
DR   GlyCosmos; P02769; 1 site, No reported glycans.
DR   GlyGen; P02769; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 9913-ENSBTAP00000022763; -.
DR   PeptideAtlas; P02769; -.
DR   PRIDE; P02769; -.
DR   ABCD; P02769; 3 sequenced antibodies.
DR   GeneID; 280717; -.
DR   KEGG; bta:280717; -.
DR   CTD; 213; -.
DR   eggNOG; ENOG502R7EA; Eukaryota.
DR   HOGENOM; CLU_030161_0_0_1; -.
DR   InParanoid; P02769; -.
DR   OrthoDB; 9875082at2759; -.
DR   SABIO-RK; P02769; -.
DR   EvolutionaryTrace; P02769; -.
DR   PRO; PR:P02769; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:1903981; F:enterobactin binding; IDA:UniProtKB.
DR   GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
DR   GO; GO:0072732; P:cellular response to calcium ion starvation; ISS:UniProtKB.
DR   GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR   GO; GO:0051902; P:negative regulation of mitochondrial depolarization; ISS:UniProtKB.
DR   GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
DR   CDD; cd00015; ALBUMIN; 3.
DR   FunFam; 1.10.246.10:FF:000001; Serum albumin; 2.
DR   FunFam; 1.10.246.10:FF:000002; Serum albumin; 2.
DR   FunFam; 1.10.246.10:FF:000003; Serum albumin; 1.
DR   Gene3D; 1.10.246.10; -; 6.
DR   InterPro; IPR000264; ALB/AFP/VDB.
DR   InterPro; IPR020858; Serum_albumin-like.
DR   InterPro; IPR021177; Serum_albumin/AFP/Afamin.
DR   InterPro; IPR020857; Serum_albumin_CS.
DR   InterPro; IPR014760; Serum_albumin_N.
DR   PANTHER; PTHR11385:SF15; ALBUMIN; 1.
DR   PANTHER; PTHR11385; SERUM ALBUMIN-RELATED; 1.
DR   Pfam; PF00273; Serum_albumin; 3.
DR   PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
DR   PRINTS; PR00803; AFETOPROTEIN.
DR   PRINTS; PR00802; SERUMALBUMIN.
DR   SMART; SM00103; ALBUMIN; 3.
DR   SUPFAM; SSF48552; Serum albumin-like; 3.
DR   PROSITE; PS00212; ALBUMIN_1; 3.
DR   PROSITE; PS51438; ALBUMIN_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Calcium; Cleavage on pair of basic residues;
KW   Copper; Direct protein sequencing; Disulfide bond; Glycation; Glycoprotein;
KW   Lipid-binding; Metal-binding; Methylation; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:843354"
FT   PROPEP          19..24
FT                   /id="PRO_0000001057"
FT   CHAIN           25..607
FT                   /note="Albumin"
FT                   /id="PRO_0000001058"
FT   DOMAIN          19..209
FT                   /note="Albumin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          210..402
FT                   /note="Albumin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          403..600
FT                   /note="Albumin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   BINDING         27
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P02770"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:22677715,
FT                   ECO:0007744|PDB:3V03"
FT   BINDING         37
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22677715,
FT                   ECO:0000269|PubMed:23769932, ECO:0007744|PDB:3V03,
FT                   ECO:0007744|PDB:4JK4"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   BINDING         267
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:22677715,
FT                   ECO:0000269|PubMed:23769932, ECO:0007744|PDB:3V03,
FT                   ECO:0007744|PDB:4JK4"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   BINDING         272
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:22677715,
FT                   ECO:0007744|PDB:3V03"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   BINDING         275
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:22677715,
FT                   ECO:0000269|PubMed:23769932, ECO:0007744|PDB:3V03,
FT                   ECO:0007744|PDB:4JK4"
FT   BINDING         278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22677715,
FT                   ECO:0000269|PubMed:23769932, ECO:0007744|PDB:3V03,
FT                   ECO:0007744|PDB:4JK4"
FT   BINDING         282
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:22677715,
FT                   ECO:0000269|PubMed:23769932, ECO:0007744|PDB:3V03,
FT                   ECO:0007744|PDB:4JK4"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         107
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         228
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P07724"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07724"
FT   MOD_RES         442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         443
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         445
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         557
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02768"
FT   MOD_RES         569
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02770"
FT   MOD_RES         587
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P07724"
FT   CARBOHYD        151
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:21565706"
FT   DISULFID        77..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        99..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        114..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        147..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        191..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        223..269
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        268..276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        288..302
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        301..312
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        339..384
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        383..392
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        415..461
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        460..471
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        484..500
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        499..510
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        537..582
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   DISULFID        581..590
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT                   ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:22993082,
FT                   ECO:0000269|PubMed:23769932, ECO:0000269|Ref.17,
FT                   ECO:0007744|PDB:3V03, ECO:0007744|PDB:4F5S,
FT                   ECO:0007744|PDB:4JK4, ECO:0007744|PDB:4OR0"
FT   VARIANT         214
FT                   /note="A -> T"
FT                   /evidence="ECO:0000269|PubMed:22993082, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.4, ECO:0000269|Ref.5, ECO:0000269|Ref.9"
FT   CONFLICT        58
FT                   /note="Missing (in Ref. 11; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="E -> A (in Ref. 5; AAI02743)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="Y -> L (in Ref. 14; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="C -> K (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304..305
FT                   /note="KP -> PC (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="N -> D (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        394..395
FT                   /note="ST -> TS (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        429
FT                   /note="A -> E (in Ref. 5; AAI02743)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="K -> R (in Ref. 16; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        472
FT                   /note="T -> A (in Ref. 5; AAI02743)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        493..494
FT                   /note="SE -> ES (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        579
FT                   /note="D -> G (in Ref. 5; AAI02743)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..38
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           40..54
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           60..79
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   TURN            84..87
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           90..99
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           104..108
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           109..116
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           121..127
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           136..139
FT                   /evidence="ECO:0007829|PDB:3V03"
FT   HELIX           143..152
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           154..168
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:9QQD"
FT   HELIX           174..191
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:4OR0"
FT   HELIX           197..229
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           231..245
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:9QQD"
FT   HELIX           251..269
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           273..288
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           291..294
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:4JK4"
FT   HELIX           301..303
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           306..315
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           316..322
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           329..332
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           338..344
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           346..360
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           366..385
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   STRAND          386..388
FT                   /evidence="ECO:0007829|PDB:4JK4"
FT   HELIX           389..393
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           396..403
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   TURN            404..407
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           408..437
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           443..460
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   STRAND          461..463
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           465..489
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           494..502
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           507..512
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   STRAND          518..520
FT                   /evidence="ECO:0007829|PDB:4JK4"
FT   HELIX           521..525
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           527..530
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           534..537
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           541..558
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   HELIX           564..583
FT                   /evidence="ECO:0007829|PDB:4F5S"
FT   STRAND          584..586
FT                   /evidence="ECO:0007829|PDB:4OR0"
FT   HELIX           587..606
FT                   /evidence="ECO:0007829|PDB:4F5S"
SQ   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
//