TRFE_CHICK
ID TRFE_CHICK Reviewed; 705 AA.
AC P02789;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ovotransferrin;
DE AltName: Full=Allergen Gal d III;
DE AltName: Full=Conalbumin;
DE AltName: Full=Serum transferrin;
DE AltName: Allergen=Gal d 3;
DE Flags: Precursor;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7060577; DOI=10.1111/j.1432-1033.1982.tb05879.x;
RA Jeltsch J.-M., Chambon P.;
RT "The complete nucleotide sequence of the chicken ovotransferrin mRNA.";
RL Eur. J. Biochem. 122:291-295(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3658709; DOI=10.1093/nar/15.18.7643;
RA Jeltsch J.-M., Hen R., Maroteaux L., Garnier J.-M., Chambon P.;
RT "Sequence of the chicken ovotransferrin gene.";
RL Nucleic Acids Res. 15:7643-7645(1987).
RN [3]
RP PROTEIN SEQUENCE OF 1-19 (PRECURSOR PROTEIN).
RC TISSUE=Egg white, and Serum;
RX PubMed=649604; DOI=10.1016/s0021-9258(17)34753-1;
RA Thibodeau S.N., Lee D.C., Palmiter R.D.;
RT "Identical precursors for serum transferrin and egg white conalbumin.";
RL J. Biol. Chem. 253:3771-3774(1978).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=6895872; DOI=10.1111/j.1432-1033.1982.tb05880.x;
RA Williams J., Elleman T.C., Kingston I.B., Wilkins A.G., Kuhn K.A.;
RT "The primary structure of hen ovotransferrin.";
RL Eur. J. Biochem. 122:297-303(1982).
RN [5]
RP PROTEIN SEQUENCE OF 140-155; 288-310; 405-434; 442-458; 479-494; 493-517;
RP 539-549; 578-594 AND 657-666, TISSUE SPECIFICITY, INDUCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Egg white {ECO:0000303|PubMed:25436390};
RX PubMed=25436390; DOI=10.1021/jf504469t;
RA Kim J., Choi Y.H.;
RT "Differential abundance of egg white proteins in laying hens treated with
RT corticosterone.";
RL J. Agric. Food Chem. 62:12346-12359(2014).
RN [6]
RP PROTEIN SEQUENCE OF 480-582.
RX PubMed=1172663; DOI=10.1042/bj1470463;
RA Kingston I.B., Williams J.;
RT "The amino acid sequence of a carbohydrate-containing fragment of hen
RT ovotransferrin.";
RL Biochem. J. 147:463-472(1975).
RN [7]
RP DISULFIDE BONDS.
RX PubMed=4907959; DOI=10.1042/bj1160515;
RA Elleman T.C., Williams J.;
RT "The amino acid sequences of cysteic acid-containing peptides from
RT performic acid-oxidized ovotransferrin.";
RL Biochem. J. 116:515-532(1970).
RN [8]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=574451; DOI=10.1111/j.1432-1033.1979.tb04203.x;
RA Dorland L., Haverkamp J., Vliegenthart J.F.G., Spik G., Fournet B.,
RA Montreuil J.;
RT "Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and
RT methylation analysis of the single glycan chain of chicken
RT ovotransferrin.";
RL Eur. J. Biochem. 100:569-574(1979).
RN [9]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=7881176; DOI=10.1093/glycob/4.5.617;
RA Jacquinot P.-M., Leger D., Wieruszeski J.-M., Coddeville B., Montreuil J.,
RA Spik G.;
RT "Change in glycosylation of chicken transferrin glycans biosynthesized
RT during embryogenesis and primary culture of embryo hepatocytes.";
RL Glycobiology 4:617-624(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-351.
RX PubMed=8218271; DOI=10.1021/bi00096a004;
RA Dewan J.C., Mikami B., Hirose M., Sacchettini J.C.;
RT "Structural evidence for a pH-sensitive dilysine trigger in the hen
RT ovotransferrin N-lobe: implications for transferrin iron release.";
RL Biochemistry 32:11963-11968(1993).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND METAL- AND CARBONATE-BINDING
RP SITES.
RX PubMed=7490743; DOI=10.1006/jmbi.1995.0611;
RA Kurokawa H., Mikami B., Hirose M.;
RT "Crystal structure of diferric hen ovotransferrin at 2.4-A resolution.";
RL J. Mol. Biol. 254:196-207(1995).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=10497206; DOI=10.1074/jbc.274.40.28445;
RA Kurokawa H., Dewan J.C., Mikami B., Sacchettini J.C., Hirose M.;
RT "Crystal structure of hen apo-ovotransferrin. Both lobes adopt an open
RT conformation upon loss of iron.";
RL J. Biol. Chem. 274:28445-28452(1999).
CC -!- FUNCTION: Transferrins are iron binding transport proteins which can
CC bind two Fe(3+) ions in association with the binding of an anion,
CC usually bicarbonate. Responsible for the transport of iron from sites
CC of absorption and heme degradation to those of storage and utilization.
CC There are two forms of hen transferrin, ovotransferrin, found in the
CC ovoducts and, serum transferrin, secreted by the liver. Serum
CC transferrin may also have a role in stimulating cell proliferation and
CC is regulated by iron levels. Ovotransferrin has a bacteriostatic
CC function and, is not controlled by iron levels.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in the magnum of the oviduct (at protein
CC level). {ECO:0000269|PubMed:25436390}.
CC -!- INDUCTION: Up-regulated by dietary stress. Increased expression at day
CC 14 in the magnum of the oviduct in the corticosterone-fed laying hens
CC (at protein level). {ECO:0000269|PubMed:25436390}.
CC -!- PTM: Different forms of hen transferrin are distinguished by their
CC carbohydrate composition. Ovotransferrin and embryo serum transferrin
CC but not adult serum transferrin, have bisecting N-acetylglucosamine.
CC Transferrin secreted by embryo hepatocytes in primary culture is marked
CC by the presence of (alpha1-6) fucosylation of the core N-
CC acetylglucosamine. Serum transferrins also differ in the number of
CC attached neuraminic acid residues. In both embryo forms, sialylation
CC occurs on the Man (alpha 1-3)-linked antennae.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; X02009; CAA26040.1; -; mRNA.
DR EMBL; Y00407; CAA68468.1; -; Genomic_DNA.
DR PIR; A26845; TFCHE.
DR RefSeq; NP_990635.1; NM_205304.1.
DR PDB; 1AIV; X-ray; 3.00 A; A=20-705.
DR PDB; 1D9K; X-ray; 3.20 A; P/Q=153-165.
DR PDB; 1IEJ; X-ray; 1.65 A; A=20-351.
DR PDB; 1IQ7; X-ray; 2.30 A; A=361-705.
DR PDB; 1JL4; X-ray; 4.30 A; C=153-165.
DR PDB; 1N04; X-ray; 2.80 A; A=20-705.
DR PDB; 1NFT; X-ray; 2.10 A; A=23-351.
DR PDB; 1NNT; X-ray; 2.30 A; A=24-351.
DR PDB; 1OVT; X-ray; 2.40 A; A=20-705.
DR PDB; 1RYX; X-ray; 3.50 A; A=20-705.
DR PDB; 1TFA; X-ray; 1.90 A; A=23-351.
DR PDB; 2D3I; X-ray; 2.15 A; A=20-705.
DR PDBsum; 1AIV; -.
DR PDBsum; 1D9K; -.
DR PDBsum; 1IEJ; -.
DR PDBsum; 1IQ7; -.
DR PDBsum; 1JL4; -.
DR PDBsum; 1N04; -.
DR PDBsum; 1NFT; -.
DR PDBsum; 1NNT; -.
DR PDBsum; 1OVT; -.
DR PDBsum; 1RYX; -.
DR PDBsum; 1TFA; -.
DR PDBsum; 2D3I; -.
DR AlphaFoldDB; P02789; -.
DR SASBDB; P02789; -.
DR SMR; P02789; -.
DR BioGRID; 676501; 1.
DR IntAct; P02789; 2.
DR MINT; P02789; -.
DR STRING; 9031.ENSGALP00000010405; -.
DR Allergome; 3293; Gal d 3.0101.
DR Allergome; 361; Gal d 3.
DR MEROPS; S60.970; -.
DR GlyConnect; 482; 7 N-Linked glycans.
DR iPTMnet; P02789; -.
DR PRIDE; P02789; -.
DR GeneID; 396241; -.
DR KEGG; gga:396241; -.
DR CTD; 7018; -.
DR VEuPathDB; HostDB:geneid_396241; -.
DR eggNOG; ENOG502QT0C; Eukaryota.
DR OrthoDB; 232859at2759; -.
DR PhylomeDB; P02789; -.
DR EvolutionaryTrace; P02789; -.
DR PRO; PR:P02789; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:1990377; C:organomineral extracellular matrix; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IDA:AgBase.
DR GO; GO:0005506; F:iron ion binding; IDA:AgBase.
DR GO; GO:0006953; P:acute-phase response; IEP:AgBase.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0019730; P:antimicrobial humoral response; TAS:AgBase.
DR GO; GO:0006881; P:extracellular sequestering of iron ion; NAS:AgBase.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; TAS:AgBase.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:AgBase.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:649604"
FT CHAIN 20..705
FT /note="Ovotransferrin"
FT /id="PRO_0000035719"
FT DOMAIN 26..352
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 364..689
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT REGION 352..360
FT /note="Connecting region"
FT BINDING 79
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT BINDING 111
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT BINDING 136
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 140
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 142
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 143
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 210
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT BINDING 269
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT BINDING 414
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT BINDING 450
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT BINDING 475
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT BINDING 479
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT BINDING 481
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT BINDING 482
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT BINDING 543
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT BINDING 611
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6895872"
FT DISULFID 29..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 39..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959"
FT DISULFID 134..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 179..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 190..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 247..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 367..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 377..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959"
FT DISULFID 424..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959"
FT DISULFID 440..662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 473..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 497..690
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959, ECO:0000269|PubMed:6895872"
FT DISULFID 507..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959"
FT DISULFID 518..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959"
FT DISULFID 589..603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:4907959"
FT VARIANT 83
FT /note="A -> V"
FT VARIANT 100
FT /note="V -> I"
FT VARIANT 154
FT /note="R -> W"
FT VARIANT 239..240
FT /note="QK -> LN"
FT VARIANT 686
FT /note="S -> N"
FT CONFLICT 132
FT /note="T -> N (in Ref. 1; CAA26040)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="L -> F (in Ref. 1; CAA26040)"
FT /evidence="ECO:0000305"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:1IEJ"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1IEJ"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1AIV"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:1IEJ"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 104..118
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1AIV"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1IEJ"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1RYX"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1IEJ"
FT TURN 197..201
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1RYX"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1AIV"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1AIV"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1IEJ"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1N04"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1OVT"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:1NFT"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:1IEJ"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:1IEJ"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1OVT"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:1N04"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 370..383
FT /evidence="ECO:0007829|PDB:2D3I"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 396..405
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:1AIV"
FT STRAND 450..460
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:1OVT"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:2D3I"
FT TURN 480..483
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 484..494
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1IQ7"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:1RYX"
FT HELIX 542..552
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:1N04"
FT TURN 575..579
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:1OVT"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 597..602
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 620..634
FT /evidence="ECO:0007829|PDB:2D3I"
FT TURN 639..643
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:2D3I"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:1IQ7"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 672..676
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 678..687
FT /evidence="ECO:0007829|PDB:2D3I"
FT TURN 688..690
FT /evidence="ECO:0007829|PDB:2D3I"
FT HELIX 694..703
FT /evidence="ECO:0007829|PDB:2D3I"
SQ SEQUENCE 705 AA; 77777 MW; 864201A93146FA84 CRC64;
MKLILCTVLS LGIAAVCFAA PPKSVIRWCT ISSPEEKKCN NLRDLTQQER ISLTCVQKAT
YLDCIKAIAN NEADAISLDG GQAFEAGLAP YKLKPIAAEV YEHTEGSTTS YYAVAVVKKG
TEFTVNDLQG KTSCHTGLGR SAGWNIPIGT LLHRGAIEWE GIESGSVEQA VAKFFSASCV
PGATIEQKLC RQCKGDPKTK CARNAPYSGY SGAFHCLKDG KGDVAFVKHT TVNENAPDQK
DEYELLCLDG SRQPVDNYKT CNWARVAAHA VVARDDNKVE DIWSFLSKAQ SDFGVDTKSD
FHLFGPPGKK DPVLKDLLFK DSAIMLKRVP SLMDSQLYLG FEYYSAIQSM RKDQLTPSPR
ENRIQWCAVG KDEKSKCDRW SVVSNGDVEC TVVDETKDCI IKIMKGEADA VALDGGLVYT
AGVCGLVPVM AERYDDESQC SKTDERPASY FAVAVARKDS NVNWNNLKGK KSCHTAVGRT
AGWVIPMGLI HNRTGTCNFD EYFSEGCAPG SPPNSRLCQL CQGSGGIPPE KCVASSHEKY
FGYTGALRCL VEKGDVAFIQ HSTVEENTGG KNKADWAKNL QMDDFELLCT DGRRANVMDY
RECNLAEVPT HAVVVRPEKA NKIRDLLERQ EKRFGVNGSE KSKFMMFESQ NKDLLFKDLT
KCLFKVREGT TYKEFLGDKF YTVISSLKTC NPSDILQMCS FLEGK
