ALBU_BOVIN
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 03-AUG-2022, entry version 188.
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;
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). Interacts with TASOR (By similarity). In
CC plasma, occurs in a covalently-linked complex with chromophore-bound
CC alpha-1-microglobulin; this interaction does not prevent fatty acid
CC binding to ALB. {ECO:0000250|UniProtKB:P02768,
CC ECO:0000250|UniProtKB:P07724}.
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; P02741: CRP; Xeno; NbExp=2; IntAct=EBI-2296927, EBI-1395983;
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}.
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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 PDBsum; 2L7U; -.
DR PDBsum; 3V03; -.
DR PDBsum; 4F5S; -.
DR PDBsum; 4JK4; -.
DR PDBsum; 4OR0; -.
DR PDBsum; 6QS9; -.
DR PDBsum; 6RJV; -.
DR AlphaFoldDB; P02769; -.
DR BMRB; P02769; -.
DR SASBDB; P02769; -.
DR SMR; P02769; -.
DR BioGRID; 158123; 5.
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 PaxDb; P02769; -.
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; 906547at2759; -.
DR TreeFam; TF335561; -.
DR SABIO-RK; P02769; -.
DR PRO; PR:P02769; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0051659; P:maintenance of mitochondrion location; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR CDD; cd00015; ALBUMIN; 3.
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; PTHR11385; 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; SSF48552; 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 143..152
FT /evidence="ECO:0007829|PDB:4F5S"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:4F5S"
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 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 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 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
