PERL_BUBBU
ID PERL_BUBBU Reviewed; 712 AA.
AC A5JUY8; F2X043;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Lactoperoxidase {ECO:0000303|PubMed:19339248};
DE Short=LPO {ECO:0000303|PubMed:12071645, ECO:0000303|PubMed:19339248};
DE Short=WBLP {ECO:0000303|PubMed:12071645};
DE EC=1.11.1.7 {ECO:0000269|PubMed:12071645, ECO:0000269|PubMed:19339248};
DE Flags: Precursor;
GN Name=LPO {ECO:0000312|EMBL:ADZ95997.1};
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:0000305, ECO:0000312|EMBL:ABQ45486.1, ECO:0000312|PDB:2GJM}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland {ECO:0000312|EMBL:ABQ45486.1};
RA Kushwaha G.S., Baskar Singh S., Sheikh I.A., Ethayathulla A.S., Sharma S.,
RA Srinivasan A., Singh T.P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABQ45486.1, ECO:0000312|PDB:2GJM}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pradeep M.A., Kaushik J.K., Mohanty A.K.;
RT "Cloning and sequencing of Bubalus bubalis lactoperoxidase gene.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12071645; DOI=10.1081/pb-120004127;
RA Ozdemir H., Hacibeyoglu H.I., Uslu H.;
RT "Purification of lactoperoxidase from creek-water buffalo milk and
RT investigation of kinetic and antibacterial properties.";
RL Prep. Biochem. Biotechnol. 32:143-155(2002).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND GLYCOSYLATION AT ASN-106; ASN-212; ASN-322 AND ASN-449.
RX PubMed=30296068; DOI=10.1021/acs.jafc.8b03243;
RA B S G.K., Mohan Reddy P., Kottekad S.;
RT "Comparative Site-Specific N-Glycosylation Analysis of Lactoperoxidase from
RT Buffalo and Goat Milk Using RP-UHPLC-MS/MS Reveals a Distinct Glycan
RT Pattern.";
RL J. Agric. Food Chem. 66:11492-11499(2018).
RN [5] {ECO:0000305, ECO:0000312|EMBL:ABQ45486.1, ECO:0000312|PDB:2GJM}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 130-712 IN COMPLEX WITH
RP THIOCYANATE; CALCIUM AND HEME, CALCIUM-BINDING SITES, GLYCOSYLATION AT
RP ASN-212; ASN-322; ASN-358 AND ASN-449, AND DISULFIDE BONDS.
RA Sheikh I.A., Ethayathulla A.S., Singh A.K., Singh N., Sharma S.,
RA Singh T.P.;
RT "Crystal structure of Buffalo lactoperoxidase at 2.75A resolution.";
RL Submitted (MAR-2006) to the PDB data bank.
RN [6] {ECO:0000305, ECO:0000312|EMBL:ABQ45486.1, ECO:0000312|PDB:2GJM}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 118-712 IN COMPLEX WITH CALCIUM
RP AND HEME, CALCIUM-BINDING SITES, PHOSPHORYLATION AT SER-315, GLYCOSYLATION
RP AT ASN-212; ASN-322; ASN-358 AND ASN-449, AND DISULFIDE BONDS.
RA Sheikh I.A., Jain R., Singh N., Sharma S., Bhushan A., Kaur P.,
RA Srinivasan A., Singh T.P.;
RT "Crystal structure of the complex of buffalo Lactoperoxidase with fluoride
RT ion at 3.5A resolution.";
RL Submitted (JUL-2007) to the PDB data bank.
RN [7] {ECO:0000305, ECO:0000312|PDB:3ERH}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 118-712 IN COMPLEXES WITH
RP THIOCYANATE; CYANIDE; CALCIUM AND HEME, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CALCIUM-BINDING SITES,
RP PHOSPHORYLATION AT SER-315, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND
RP ASN-449, AND DISULFIDE BONDS.
RX PubMed=19339248; DOI=10.1074/jbc.m807644200;
RA Sheikh I.A., Singh A.K., Singh N., Sinha M., Singh S.B., Bhushan A.,
RA Kaur P., Srinivasan A., Sharma S., Singh T.P.;
RT "Structural evidence of substrate specificity in mammalian peroxidases:
RT structure of the thiocyanate complex with lactoperoxidase and its
RT interactions at 2.4 A resolution.";
RL J. Biol. Chem. 284:14849-14856(2009).
CC -!- FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion
CC of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid
CC (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (Probable). Also
CC involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in
CC the presence of H2O2 (By similarity). Responsible for the inactivation
CC of a wide range of micro-organisms and hence, important component of
CC defense mechanism (PubMed:12071645). Shows antibacterial properties
CC against E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus,
CC S.epidermidis and S.dysenteriae (PubMed:12071645). May protect the
CC udder from infection and may promote growth in newborns (By
CC similarity). May be implicated in airway host defense against infection
CC (By similarity). May contribute to maintaining an appropriate H2O2
CC cellular level, therefore protecting cells from H2O2-caused injuries
CC and inflammation (By similarity). {ECO:0000250|UniProtKB:A0A452E9Y6,
CC ECO:0000250|UniProtKB:P22079, ECO:0000250|UniProtKB:P80025,
CC ECO:0000250|UniProtKB:Q5SW46, ECO:0000269|PubMed:12071645,
CC ECO:0000305|PubMed:12071645, ECO:0000305|PubMed:19339248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC Evidence={ECO:0000269|PubMed:12071645, ECO:0000305|PubMed:19339248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137;
CC Evidence={ECO:0000305|PubMed:12071645, ECO:0000305|PubMed:19339248};
CC -!- CATALYTIC ACTIVITY: [Lactoperoxidase]:
CC Reaction=H(+) + H2O2 + thiocyanate = H2O + hypothiocyanous acid;
CC Xref=Rhea:RHEA:69416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18022, ChEBI:CHEBI:133907;
CC Evidence={ECO:0000305|PubMed:19339248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417;
CC Evidence={ECO:0000305|PubMed:19339248};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + iodide = H2O + hypoiodite; Xref=Rhea:RHEA:69420,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382,
CC ChEBI:CHEBI:29232; Evidence={ECO:0000250|UniProtKB:P80025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69421;
CC Evidence={ECO:0000250|UniProtKB:P80025};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298,
CC ECO:0000269|PubMed:19339248};
CC Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-
CC ProRule:PRU00298, ECO:0000269|PubMed:19339248};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298,
CC ECO:0000269|PubMed:19339248};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298,
CC ECO:0000269|PubMed:19339248};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.82 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
CC (at pH 6.0 and 60 degrees Celsius) {ECO:0000269|PubMed:12071645};
CC KM=0.77 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
CC (at pH 6.0 and 25 degrees Celsius) {ECO:0000269|PubMed:12071645};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:12071645};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:12071645};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12071645,
CC ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5SW46}.
CC -!- TISSUE SPECIFICITY: Mammary gland; milk. {ECO:0000269|PubMed:12071645,
CC ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068}.
CC -!- MISCELLANEOUS: Thiocyanate (SCN(-)) and hypothiocyanite (OSCN(-)) are
CC bound in the distal heme cavity. The iodide ion (I(-)) occupies a
CC position which is stabilized by the interactions with heme moiety, His-
CC 226, Arg-372 and Glu-375. Hydrogen peroxide is held between the heme
CC iron and His-226. {ECO:0000250|UniProtKB:P80025}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
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DR EMBL; EF580919; ABQ45486.1; -; mRNA.
DR EMBL; HQ285238; ADZ95997.1; -; mRNA.
DR RefSeq; NP_001277812.1; NM_001290883.1.
DR PDB; 2GJM; X-ray; 2.75 A; A=130-712.
DR PDB; 2O86; X-ray; 2.80 A; A=118-712.
DR PDB; 2Z5Z; X-ray; 3.50 A; A=118-712.
DR PDB; 3ERH; X-ray; 2.40 A; A=118-712.
DR PDB; 3FAQ; X-ray; 2.70 A; A=118-712.
DR PDB; 3FNL; X-ray; 2.48 A; A=118-712.
DR PDB; 4Y55; X-ray; 2.10 A; A=118-712.
DR PDBsum; 2GJM; -.
DR PDBsum; 2O86; -.
DR PDBsum; 2Z5Z; -.
DR PDBsum; 3ERH; -.
DR PDBsum; 3FAQ; -.
DR PDBsum; 3FNL; -.
DR PDBsum; 4Y55; -.
DR AlphaFoldDB; A5JUY8; -.
DR SMR; A5JUY8; -.
DR iPTMnet; A5JUY8; -.
DR PRIDE; A5JUY8; -.
DR GeneID; 102405711; -.
DR KEGG; bbub:102405711; -.
DR CTD; 4025; -.
DR EvolutionaryTrace; A5JUY8; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0036393; F:thiocyanate peroxidase activity; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR029587; LPO.
DR PANTHER; PTHR11475:SF67; PTHR11475:SF67; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Calcium; Cytoplasm;
KW Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Nitration; Oxidoreductase; Peroxidase; Phosphoprotein; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..100
FT /evidence="ECO:0000250|UniProtKB:P80025"
FT /id="PRO_0000424888"
FT CHAIN 101..712
FT /note="Lactoperoxidase"
FT /evidence="ECO:0000250|UniProtKB:P80025"
FT /id="PRO_0000424889"
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 225
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT BINDING 375
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT BINDING 468
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:19339248"
FT SITE 372
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P05164,
FT ECO:0000255|PROSITE-ProRule:PRU00298"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19339248, ECO:0000269|Ref.6"
FT MOD_RES 482
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11678"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:30296068"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:30296068"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT DISULFID 123..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT DISULFID 132..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT DISULFID 246..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT DISULFID 250..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT DISULFID 354..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT DISULFID 573..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT DISULFID 671..696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT CONFLICT 206
FT /note="E -> D (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="G -> R (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="R -> H (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="H -> Q (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="N -> D (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="I -> V (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="T -> V (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="F -> M (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="T -> A (in Ref. 2; ADZ95997)"
FT /evidence="ECO:0000305"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3FAQ"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:4Y55"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:3ERH"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3ERH"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4Y55"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3FAQ"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:3ERH"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:4Y55"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:4Y55"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 377..400
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 406..427
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:3ERH"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:2GJM"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:4Y55"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:3ERH"
FT HELIX 510..518
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:3ERH"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3FNL"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 550..560
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 566..572
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 581..587
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 591..601
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 609..615
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 626..641
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 655..661
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 666..673
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 678..685
FT /evidence="ECO:0007829|PDB:3FNL"
FT TURN 689..692
FT /evidence="ECO:0007829|PDB:4Y55"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:3FNL"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:4Y55"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:4Y55"
SQ SEQUENCE 712 AA; 80698 MW; 426BF93704E7309B CRC64;
MWVCLQLPVF LASVTLFEVA ASDTIAQAAS TTTISDAVSK VKIQVNKAFL DSRTRLKTTL
SSEAPTTQQL SEYFKHAKGQ TRTAIRNGQV WEESFKRLRR DTTLTNVTDP SLDLTALSWE
VGCGAPVPLV KCDENSPYRT ITGDCNNRRS PALGAANRAL ARWLPAEYED GLALPFGWTQ
RKTRNGFRVP LAREVSNKIV GYLDEEGVLD QNRSLLFMQW GQIVDHDLDF APETELGSNE
HSKTQCEEYC IQGDNCFPIM FPKNDPKLKT QGKCMPFFRA GFVCPTPPYQ SLAREQINAV
TSFLDASLVY GSEPSLASRL RNLSSPLGLM AVNQEAWDHG LAYLPFNNKK PSPCEFINTT
ARVPCFLAGD FRASEQILLA TAHTLLLREH NRLARELKKL NPHWNGEKLY QEARKILGAF
IQIITFRDYL PIVLGSEMQK WIPPYQGYNN SVDPRISNVF TFAFRFGHME VPSTVSRLDE
NYQPWGPEAE LPLHTLFFNT WRIIKDGGID PLTRGLLAKK SKLMNQDKMV TSELRNKLFQ
PTHKIHGFDL AAINLQRCRD HGMPGYNSWR GFCGLSQPKT LKGLQTVLKN KILAKKLMDL
YKTPDNIDIW IGGNAEPMVE RGRVGPLLAC LLGRQFQQIR DGDRFWWENP GVFTEKQRDS
LQKFSFSRLI CDNTHITKVP LHAFQANNYP HDFVDCSTVD KLDLSPWASR EN
