TRFL_HORSE
ID TRFL_HORSE Reviewed; 695 AA.
AC O77811;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Lactotransferrin;
DE Short=Lactoferrin;
DE EC=3.4.21.-;
DE Flags: Precursor; Fragment;
GN Name=LTF;
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 (2.62 ANGSTROMS) OF
RP 7-695 IN COMPLEX WITH IRON AND CARBONATE.
RC TISSUE=Mammary gland;
RX PubMed=10366507; DOI=10.1006/jmbi.1999.2767;
RA Sharma A.K., Paramasivam M., Srinivasan A., Yadav M.P., Singh T.P.;
RT "Three-dimensional structure of mare diferric lactoferrin at 2.6-A
RT resolution.";
RL J. Mol. Biol. 289:303-317(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 7-695.
RX PubMed=10329777; DOI=10.1107/s0907444999003807;
RA Sharma A.K., Rajashankar K.R., Yadav M.P., Singh T.P.;
RT "Structure of mare apolactoferrin: the N and C lobes are in the closed
RT form.";
RL Acta Crystallogr. D 55:1152-1157(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 7-695 IN COMPLEX WITH IRON.
RX PubMed=10531474; DOI=10.1107/s0907444999009439;
RA Sharma A.K., Singh T.P.;
RT "Structure of oxalate-substituted diferric mare lactoferrin at 2.7 A
RT resolution.";
RL Acta Crystallogr. D 55:1792-1798(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 7-695 IN COMPLEX WITH CARBONATE.
RX PubMed=10531475; DOI=10.1107/s0907444999009865;
RA Sharma A.K., Singh T.P.;
RT "Lactoferrin-metal interactions: first crystal structure of a complex of
RT lactoferrin with a lanthanide ion (Sm3+) at 3.4 A resolution.";
RL Acta Crystallogr. D 55:1799-1804(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH IRON.
RX PubMed=11599026; DOI=10.1002/prot.1143;
RA Sharma A.K., Kumar S., Sharma V., Nagpal A., Singh N., Tamboli I., Mani I.,
RA Raman G., Singh T.P.;
RT "Lactoferrin-melanin interaction and its possible implications in melanin
RT polymerization: crystal structure of the complex formed between mare
RT lactoferrin and melanin monomers at 2.7-A resolution.";
RL Proteins 45:229-236(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 7-695.
RX PubMed=11807246; DOI=10.1107/s090744490101993x;
RA Kumar P., Khan J.A., Yadav S., Singh T.P.;
RT "Crystal structure of equine apolactoferrin at 303 K providing further
RT evidence of closed conformations of N and C lobes.";
RL Acta Crystallogr. D 58:225-232(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS) OF 7-695 IN COMPLEX WITH GLUCOSE AND
RP IRON.
RA Mir R., Kaur A., Singh A.K., Singh N., Kaur P., Sharma S., Singh T.P.;
RT "Crystal structure of the complex of Lactoferrin with 6-
RT (Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolution.";
RL Submitted (APR-2008) to the PDB data bank.
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.
CC -!- FUNCTION: Lactotransferrin is a major iron-binding and multifunctional
CC protein found in exocrine fluids such as breast milk and mucosal
CC secretions. Has antimicrobial activity. Antimicrobial properties may
CC include bacteriostasis, which is related to its ability to sequester
CC free iron and thus inhibit microbial growth, as well as direct
CC bactericidal properties leading to the release of lipopolysaccharides
CC from the bacterial outer membrane. May have anabolic, differentiating
CC and anti-apoptotic effects on osteoblasts and may also inhibit
CC osteoclastogenesis, possibly playing a role in the regulation of bone
CC growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4
CC signaling (By similarity). Can bind glucose. {ECO:0000250}.
CC -!- FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a
CC serine protease of the peptidase S60 family that cuts arginine rich
CC regions. This function contributes to the antimicrobial activity. Shows
CC a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-,
CC and of Z-Phe-Arg-|-aminomethylcoumarin sites. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}.
CC Note=Secreted into most exocrine fluids by various endothelial cells.
CC Stored in the secondary granules of neutrophils (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; AJ010930; CAA09407.1; -; mRNA.
DR PDB; 1B1X; X-ray; 2.62 A; A=7-695.
DR PDB; 1B7U; X-ray; 3.80 A; A=7-695.
DR PDB; 1B7Z; X-ray; 2.70 A; A=7-695.
DR PDB; 1F9B; X-ray; 2.70 A; A=1-695.
DR PDB; 1I6B; X-ray; 3.20 A; A=7-695.
DR PDB; 1QJM; X-ray; 3.40 A; A=7-695.
DR PDB; 3CR9; X-ray; 3.49 A; A=7-695.
DR PDBsum; 1B1X; -.
DR PDBsum; 1B7U; -.
DR PDBsum; 1B7Z; -.
DR PDBsum; 1F9B; -.
DR PDBsum; 1I6B; -.
DR PDBsum; 1QJM; -.
DR PDBsum; 3CR9; -.
DR AlphaFoldDB; O77811; -.
DR SMR; O77811; -.
DR IntAct; O77811; 1.
DR STRING; 9796.ENSECAP00000033689; -.
DR MEROPS; S60.001; -.
DR PaxDb; O77811; -.
DR PRIDE; O77811; -.
DR InParanoid; O77811; -.
DR EvolutionaryTrace; O77811; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0042581; C:specific granule; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019731; P:antibacterial humoral response; ISS:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; ISS:UniProtKB.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; ISS:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:2001205; P:negative regulation of osteoclast development; ISS:UniProtKB.
DR GO; GO:1900229; P:negative regulation of single-species biofilm formation in or on host organism; ISS:UniProtKB.
DR GO; GO:2000308; P:negative regulation of tumor necrosis factor (ligand) superfamily member 11 production; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; ISS:UniProtKB.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
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; Disulfide bond; Glycoprotein; Hydrolase; Immunity;
KW Ion transport; Iron; Iron transport; Metal-binding; Osteogenesis; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Transport.
FT SIGNAL <1..6
FT CHAIN 7..695
FT /note="Lactotransferrin"
FT /id="PRO_0000035731"
FT DOMAIN 12..339
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 351..680
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 66
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474,
FT ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"
FT BINDING 98
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474,
FT ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"
FT BINDING 123
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"
FT BINDING 127
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"
FT BINDING 129
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"
FT BINDING 130
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"
FT BINDING 198
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474,
FT ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"
FT BINDING 259
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474,
FT ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"
FT BINDING 401
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474,
FT ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"
FT BINDING 436
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 439
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474,
FT ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"
FT BINDING 465
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"
FT BINDING 469
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"
FT BINDING 471
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"
FT BINDING 472
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"
FT BINDING 532
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474,
FT ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"
FT BINDING 600
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|Ref.7"
FT BINDING 601
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474,
FT ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"
FT BINDING 666
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|Ref.7"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 15..51
FT DISULFID 25..42
FT DISULFID 121..204
FT DISULFID 163..179
FT DISULFID 166..189
FT DISULFID 176..187
FT DISULFID 237..251
FT DISULFID 354..386
FT DISULFID 364..377
FT DISULFID 411..690
FT DISULFID 431..653
FT DISULFID 463..538
FT DISULFID 487..681
FT DISULFID 497..511
FT DISULFID 508..521
FT DISULFID 579..593
FT DISULFID 631..636
FT NON_TER 1
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 183..187
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1I6B"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:1F9B"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3CR9"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 373..382
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 402..410
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 414..422
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:1I6B"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 439..448
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 470..473
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 474..484
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:1I6B"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:1I6B"
FT HELIX 531..540
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 551..555
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 556..560
FT /evidence="ECO:0007829|PDB:1I6B"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 574..578
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:1I6B"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 587..592
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:1B1X"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 610..624
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:1B1X"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:1I6B"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 663..667
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 669..679
FT /evidence="ECO:0007829|PDB:1B1X"
FT HELIX 685..693
FT /evidence="ECO:0007829|PDB:1B1X"
SQ SEQUENCE 695 AA; 75991 MW; 07BB84D50E1B165D CRC64;
LGLCLAAPRK SVRWCTISPA EAAKCAKFQR NMKKVRGPSV SCIRKTSSFE CIQAIAANKA
DAVTLDGGLV YEAGLHPYKL RPVAAEVYQT RGKPQTRYYA VAVVKKGSGF QLNQLQGVKS
CHTGLGRSAG WNIPIGTLRP YLNWTGPPEP LQKAVANFFS ASCVPCADGK QYPNLCRLCA
GTEADKCACS SQEPYFGYSG AFKCLENGAG DVAFVKDSTV FENLPDEADR DKYELLCPDN
TRKPVDAFKE CHLARVPSHA VVARSVDGRE DLIWRLLHRA QEEFGRNKSS AFQLFKSTPE
NKDLLFKDSA LGFVRIPSQI DSGLYLGANY LTATQNLRET AAEVAARRER VVWCAVGPEE
ERKCKQWSDV SNRKVACASA STTEECIALV LKGEADALNL DGGFIYVAGK CGLVPVLAEN
QKSQNSNAPD CVHRPPEGYL AVAVVRKSDA DLTWNSLSGK KSCHTGVGRT AAWNIPMGLL
FNQTGSCKFD KFFSQSCAPG ADPQSSLCAL CVGNNENENK CMPNSEERYY GYTGAFRCLA
EKAGDVAFVK DVTVLQNTDG KNSEPWAKDL KQEDFELLCL DGTRKPVAEA ESCHLARAPN
HAVVSQSDRA QHLKKVLFLQ QDQFGGNGPD CPGKFCLFKS ETKNLLFNDN TECLAELQGK
TTYEQYLGSE YVTSITNLRR CSSSPLLEAC AFLRA
