ALBU_HORSE
ID ALBU_HORSE Reviewed; 607 AA.
AC P35747;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Albumin;
DE AltName: Allergen=Equ c 3;
DE Flags: Precursor;
GN Name=ALB;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RC TISSUE=Liver;
RX PubMed=8344282; DOI=10.1111/j.1432-1033.1993.tb18024.x;
RA Ho J.X., Holowachuk E.W., Norton E.J., Twigg P.D., Carter D.C.;
RT "X-ray and primary structure of horse serum albumin (Equus caballus) at
RT 0.27-nm resolution.";
RL Eur. J. Biochem. 215:205-212(1993).
RN [2] {ECO:0007744|PDB:4F5U}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 25-607, AND DISULFIDE BONDS.
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 [3] {ECO:0007744|PDB:3V08}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 25-607, 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 [4] {ECO:0007744|PDB:4J2V}
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 25-607, 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 [5] {ECO:0007744|PDB:4OT2}
RP X-RAY CRYSTALLOGRAPHY (2.42 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).
RN [6] {ECO:0007744|PDB:5IIX}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 25-607 IN COMPLEX WITH ZINC.
RX PubMed=28567254; DOI=10.1039/c6sc02267g;
RA Handing K.B., Shabalin I.G., Kassaar O., Khazaipoul S., Blindauer C.A.,
RA Stewart A.J., Chruszcz M., Minor W.;
RT "Circulatory zinc transport is controlled by distinct interdomain sites on
RT mammalian albumins.";
RL Chem. Sci. 7:6635-6648(2016).
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 (By similarity).
CC Potentially has more than two calcium-binding sites and might
CC additionally bind calcium in a non-specific manner (By similarity). The
CC shared binding site between zinc and calcium at residue Asp-272
CC suggests a crosstalk between zinc and calcium transport in the blood
CC (By similarity). The rank order of affinity is zinc > calcium >
CC magnesium (By similarity). Binds to the bacterial siderophore
CC enterobactin and inhibits enterobactin-mediated iron uptake of E.coli
CC from ferric transferrin, and may thereby limit the utilization of iron
CC and growth of enteric bacteria such as E.coli (By similarity). Does not
CC prevent iron uptake by the bacterial siderophore aerobactin (By
CC similarity). {ECO:0000250|UniProtKB:P02768,
CC ECO:0000250|UniProtKB:P02769}.
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 -!- 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. Binds to IgE.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; X74045; CAA52194.1; -; mRNA.
DR PIR; S34053; ABHOS.
DR RefSeq; NP_001075972.1; NM_001082503.1.
DR PDB; 3V08; X-ray; 2.45 A; A=25-607.
DR PDB; 4F5T; X-ray; 2.32 A; A=25-607.
DR PDB; 4F5U; X-ray; 2.04 A; A=25-607.
DR PDB; 4J2V; X-ray; 2.12 A; A=25-607.
DR PDB; 4OT2; X-ray; 2.42 A; A=25-607.
DR PDB; 4ZBQ; X-ray; 1.92 A; A=25-607.
DR PDB; 4ZBR; X-ray; 2.19 A; A=25-607.
DR PDB; 5DBY; X-ray; 2.35 A; A=25-607.
DR PDB; 5DQF; X-ray; 2.15 A; A=28-607.
DR PDB; 5HOZ; X-ray; 2.15 A; A=25-607.
DR PDB; 5ID9; X-ray; 2.48 A; A=25-607.
DR PDB; 5IIH; X-ray; 2.40 A; A=25-607.
DR PDB; 5IIU; X-ray; 2.30 A; A=25-607.
DR PDB; 5IIX; X-ray; 2.20 A; A=25-607.
DR PDB; 5IJ5; X-ray; 2.55 A; A=25-607.
DR PDB; 5IJE; X-ray; 2.40 A; A=25-607.
DR PDB; 5V0V; X-ray; 2.45 A; A=25-607.
DR PDB; 6CI6; X-ray; 2.80 A; A=25-607.
DR PDB; 6MDQ; X-ray; 2.15 A; A=25-607.
DR PDB; 6OCI; X-ray; 2.54 A; A=25-607.
DR PDB; 6OCJ; X-ray; 2.50 A; A=25-607.
DR PDB; 6U4R; X-ray; 2.45 A; A=25-607.
DR PDB; 6U4X; X-ray; 2.25 A; A=25-607.
DR PDB; 6U5A; X-ray; 2.65 A; A=25-607.
DR PDB; 6XK0; X-ray; 2.40 A; A=25-607.
DR PDB; 7MBL; X-ray; 2.70 A; A=25-607.
DR PDBsum; 3V08; -.
DR PDBsum; 4F5T; -.
DR PDBsum; 4F5U; -.
DR PDBsum; 4J2V; -.
DR PDBsum; 4OT2; -.
DR PDBsum; 4ZBQ; -.
DR PDBsum; 4ZBR; -.
DR PDBsum; 5DBY; -.
DR PDBsum; 5DQF; -.
DR PDBsum; 5HOZ; -.
DR PDBsum; 5ID9; -.
DR PDBsum; 5IIH; -.
DR PDBsum; 5IIU; -.
DR PDBsum; 5IIX; -.
DR PDBsum; 5IJ5; -.
DR PDBsum; 5IJE; -.
DR PDBsum; 5V0V; -.
DR PDBsum; 6CI6; -.
DR PDBsum; 6MDQ; -.
DR PDBsum; 6OCI; -.
DR PDBsum; 6OCJ; -.
DR PDBsum; 6U4R; -.
DR PDBsum; 6U4X; -.
DR PDBsum; 6U5A; -.
DR PDBsum; 6XK0; -.
DR PDBsum; 7MBL; -.
DR AlphaFoldDB; P35747; -.
DR SMR; P35747; -.
DR STRING; 9796.ENSECAP00000041304; -.
DR ChEMBL; CHEMBL3751645; -.
DR Allergome; 3302; Equ c 3.0101.
DR Allergome; 335; Equ c 3.
DR PaxDb; P35747; -.
DR PeptideAtlas; P35747; -.
DR PRIDE; P35747; -.
DR GeneID; 100034206; -.
DR KEGG; ecb:100034206; -.
DR CTD; 213; -.
DR InParanoid; P35747; -.
DR OrthoDB; 906547at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; ISS: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:0008270; F:zinc ion binding; IBA:GO_Central.
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; 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; Disulfide bond; Lipid-binding; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT /id="PRO_0000001065"
FT CHAIN 25..607
FT /note="Albumin"
FT /id="PRO_0000001066"
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:0000250|UniProtKB:P02769"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28567254,
FT ECO:0007744|PDB:5IIH"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28567254,
FT ECO:0007744|PDB:5IIH"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28567254,
FT ECO:0007744|PDB:5IIH"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
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 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 DISULFID 77..86
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 99..115
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 114..125
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 147..192
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 191..200
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 223..269
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 268..276
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 288..302
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 301..312
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 339..384
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 383..392
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 415..461
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 460..471
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 484..500
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 499..510
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 537..582
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT DISULFID 581..590
FT /evidence="ECO:0000269|PubMed:22677715,
FT ECO:0000269|PubMed:22993082, ECO:0000269|PubMed:23769932,
FT ECO:0000269|PubMed:24753230, ECO:0007744|PDB:3V08,
FT ECO:0007744|PDB:4F5T, ECO:0007744|PDB:4F5U,
FT ECO:0007744|PDB:4J2V, ECO:0007744|PDB:4OT2"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4F5T"
FT HELIX 30..54
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4J2V"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT TURN 99..103
FT /evidence="ECO:0007829|PDB:6U4X"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 197..229
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7MBL"
FT HELIX 251..269
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 346..359
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 366..384
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 389..393
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 401..421
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 423..437
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 443..460
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 468..489
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 494..501
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 507..513
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:4F5U"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 534..538
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 541..558
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 564..582
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:4ZBQ"
FT HELIX 587..605
FT /evidence="ECO:0007829|PDB:4ZBQ"
SQ SEQUENCE 607 AA; 68599 MW; 256F6E830A1B90C5 CRC64;
MKWVTFVSLL FLFSSAYSRG VLRRDTHKSE IAHRFNDLGE KHFKGLVLVA FSQYLQQCPF
EDHVKLVNEV TEFAKKCAAD ESAENCDKSL HTLFGDKLCT VATLRATYGE LADCCEKQEP
ERNECFLTHK DDHPNLPKLK PEPDAQCAAF QEDPDKFLGK YLYEVARRHP YFYGPELLFH
AEEYKADFTE CCPADDKLAC LIPKLDALKE RILLSSAKER LKCSSFQNFG ERAVKAWSVA
RLSQKFPKAD FAEVSKIVTD LTKVHKECCH GDLLECADDR ADLAKYICEH QDSISGKLKA
CCDKPLLQKS HCIAEVKEDD LPSDLPALAA DFAEDKEICK HYKDAKDVFL GTFLYEYSRR
HPDYSVSLLL RIAKTYEATL EKCCAEADPP ACYRTVFDQF TPLVEEPKSL VKKNCDLFEE
VGEYDFQNAL IVRYTKKAPQ VSTPTLVEIG RTLGKVGSRC CKLPESERLP CSENHLALAL
NRLCVLHEKT PVSEKITKCC TDSLAERRPC FSALELDEGY VPKEFKAETF TFHADICTLP
EDEKQIKKQS ALAELVKHKP KATKEQLKTV LGNFSAFVAK CCGREDKEAC FAEEGPKLVA
SSQLALA
