TRFL_BUBBU
ID TRFL_BUBBU Reviewed; 708 AA.
AC O77698;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lactotransferrin;
DE Short=Lactoferrin;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=LTF;
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1] {ECO:0007744|PDB:1BIY}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (3.37 ANGSTROMS) OF
RP 20-708 IN COMPLEX WITH IRON AND CARBONATE, AND DISULFIDE BOND.
RC TISSUE=Mammary gland;
RX PubMed=10818344; DOI=10.1107/s0907444900005151;
RA Karthikeyan S., Yadav S., Paramasivam M., Srinivasan A., Singh T.P.;
RT "Structure of buffalo lactoferrin at 3.3 A resolution at 277 K.";
RL Acta Crystallogr. D 56:684-689(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Paramasivam M., Thattaliyath B.D., Kumar A., Srinivasan A., Singh T.P.;
RT "cDNA sequence of Buffalo lactoferrin.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GLYCOSYLATION AT ASN-252; ASN-300; ASN-495 AND ASN-564, VARIANT LYS-574,
RP DISULFIDE BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX DOI=10.1016/j.idairyj.2021.105215;
RA Gnanesh Kumar B.S., Lijina P., Akshata S.H.;
RT "N-glycoprofiling of lactoferrin with site-specificity from buffalo
RT colostrum.";
RL Int. Dairy J. 127:105215-105215(2022).
RN [4] {ECO:0007744|PDB:1CE2}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 20-708 IN COMPLEX WITH IRON AND
RP CARBONATE, AND DISULFIDE BOND.
RX PubMed=10531476; DOI=10.1107/s0907444999010951;
RA Karthikeyan S., Paramasivam M., Yadav S., Srinivasan A., Singh T.P.;
RT "Structure of buffalo lactoferrin at 2.5-A resolution using crystals grown
RT at 303 K shows different orientations of the N and C lobes.";
RL Acta Crystallogr. D 55:1805-1813(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.
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. The most effective inhibitory
CC activity is seen against E.coli and P.aeruginosa. Has anabolic,
CC differentiating and anti-apoptotic effects on osteoblasts and can also
CC inhibit osteoclastogenesis, possibly playing a role in the regulation
CC of bone growth. Interferes with the lipopolysaccharide (LPS)-stimulated
CC TLR4 signaling, but cannot directly stimulate the TLR4 signaling
CC pathway and subsequent NF-kappa-B activation (By similarity).
CC {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; AJ005203; CAA06441.1; -; mRNA.
DR PDB; 1BIY; X-ray; 3.37 A; A=20-708.
DR PDB; 1CE2; X-ray; 2.50 A; A=20-708.
DR PDBsum; 1BIY; -.
DR PDBsum; 1CE2; -.
DR AlphaFoldDB; O77698; -.
DR BMRB; O77698; -.
DR SMR; O77698; -.
DR MEROPS; S60.001; -.
DR MEROPS; S60.970; -.
DR PRIDE; O77698; -.
DR EvolutionaryTrace; O77698; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0042581; C:specific granule; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
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; IPR030684; Lactotransferrin.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF500683; Lactotransferrin; 1.
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 Repeat; Secreted; Serine protease; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P24627"
FT CHAIN 20..708
FT /note="Lactotransferrin"
FT /id="PRO_0000035728"
FT DOMAIN 25..352
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 364..693
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 278
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT BINDING 136
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344"
FT BINDING 140
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344"
FT BINDING 142
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344"
FT BINDING 143
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT BINDING 414
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT BINDING 452
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT BINDING 478
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344"
FT BINDING 482
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344"
FT BINDING 484
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344"
FT BINDING 485
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344"
FT BINDING 545
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT BINDING 614
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|Ref.3"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) (hybrid) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|Ref.3"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|Ref.3"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|Ref.3"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|Ref.3"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|Ref.3"
FT DISULFID 28..64
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 38..55
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 134..217
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 176..192
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 179..202
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 189..200
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 250..264
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 367..399
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 377..390
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 424..703
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 444..666
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 476..551
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2"
FT DISULFID 500..694
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 510..524
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 521..534
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 592..606
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT DISULFID 644..649
FT /evidence="ECO:0000269|PubMed:10531476,
FT ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY,
FT ECO:0007744|PDB:1CE2"
FT VARIANT 574
FT /note="E -> K"
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 104..118
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1BIY"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 283..297
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 335..351
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 386..395
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 415..422
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 452..459
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 487..497
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:1CE2"
FT TURN 519..523
FT /evidence="ECO:0007829|PDB:1BIY"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:1BIY"
FT HELIX 544..553
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 556..563
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 564..569
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:1BIY"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:1BIY"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 615..619
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 620..637
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:1BIY"
FT TURN 642..647
FT /evidence="ECO:0007829|PDB:1CE2"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:1BIY"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 676..680
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 682..692
FT /evidence="ECO:0007829|PDB:1CE2"
FT HELIX 698..705
FT /evidence="ECO:0007829|PDB:1CE2"
SQ SEQUENCE 708 AA; 77730 MW; 08D2600AAB2F9ACD CRC64;
MKLFVPALLS LGALGLCLAA PRKNVRWCTI SQPEWLKCHR WQWRMKKLGA PSITCVRRAF
VLECIRAITE KKADAVTLDG GMVFEAGLDP YKLRPVAAEI YGTKESPQTH YYAVAVVKKG
SNFQLDQLQG RNSCHTGLGR SAGWNIPMGI LRPYLSWTES LEPFQGAVAK FFSASCVPCV
DRQAYPNLCQ LCKGEGENQC ACSPREPYFG YSGAFKCLQD GAGDVAFVKE TTVFENLPEK
ADRDQYELLC LNNTRAPVDA FKECHLAQVP SHAVVARSVD GKEDLIWKLL SKAQEKFGKN
KSGSFQLFGS PPGQRDLLFK DCALGFLRIP SKVDSALYLG SRYLTALKNL RETAEEVQAR
RARVVWCAVG PEEQKKCQQW SQQSGQIVTC ATASTTDDCI ALVLKGEADA LSLDGGYIYT
AGKCGLVPVL AENRKSSKHS SLDCVLRPTE GYLAVAVVKK ANEGLTWNSL KGKKSCHTAV
DRTAGWNIPM GLIANQTGSC AFDEFFSQSC APGADPKSRL CALCAGDDQG LDKCVPNSKE
KYYGYTGAFR CLAEDVGDVA FVKNDTVWEN TNGESTADWA KNLNREDFRL LCLDGTRKPV
TEAQSCHLAV APNHAVVSLS ERAAHVEQVL LHQQALFGEN GKNCPDKFCL FKSETKNLLF
NDNTECLAKL GGRPTYEEYL GTEYVTAIAN LKKCSTSPLL EACAFLTR
