PERL_CAPHI
ID PERL_CAPHI Reviewed; 712 AA.
AC A0A452E9Y6; A3F9D6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Lactoperoxidase {ECO:0000303|PubMed:18191143};
DE Short=LPO {ECO:0000303|PubMed:18191143};
DE EC=1.11.1.7 {ECO:0000250|UniProtKB:P80025};
DE Flags: Precursor;
GN Name=LPO;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000312|Proteomes:UP000291000};
RN [1] {ECO:0000312|EMBL:ABN41562.1, ECO:0007744|PDB:2R5L}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 118-137, X-RAY
RP CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 118-712 IN COMPLEX WITH CALCIUM AND
RP HEME, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-315,
RP GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, AND DISULFIDE
RP BONDS.
RX PubMed=18191143; DOI=10.1016/j.jmb.2007.12.012;
RA Singh A.K., Singh N., Sharma S., Singh S.B., Kaur P., Bhushan A.,
RA Srinivasan A., Singh T.P.;
RT "Crystal structure of lactoperoxidase at 2.4 A resolution.";
RL J. Mol. Biol. 376:1060-1075(2008).
RN [2] {ECO:0000312|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=10894086; DOI=10.1016/s0024-3205(00)80003-x;
RA Benoy M.J., Essy A.K., Sreekumar B., Haridas M.;
RT "Thiocyanate mediated antifungal and antibacterial property of goat milk
RT lactoperoxidase.";
RL Life Sci. 66:2433-2439(2000).
RN [4] {ECO:0000305}
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:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 118-712 IN COMPLEX WITH CALCIUM
RP AND HEME, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, AND
RP DISULFIDE BONDS.
RA Singh A.K., Singh N., Singh S.B., Sharma S., Kaur P., Singh T.P.;
RT "Crystal structure of a ternary complex of goat lactoperoxidase with
RT cyanide and iodide ions at 2.4 A resolution.";
RL Submitted (JAN-2007) to the PDB data bank.
RN [6] {ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 118-712 IN COMPLEX WITH CALCIUM
RP AND HEME, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, AND
RP DISULFIDE BONDS.
RA Singh R.P., Pandey N., Singh A.K., Sinha M., Kaur P., Sharma S.,
RA Singh T.P.;
RT "Crystal structure of the complex of goat lactoperoxidase with Pyrazinamide
RT at 2.1 A resolution.";
RL Submitted (MAR-2011) to the PDB data bank.
RN [7] {ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 118-712 IN COMPLEX WITH CALCIUM
RP AND HEME, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, AND
RP DISULFIDE BONDS.
RA Tyagi T.K., Singh R.P., Singh A.K., Singh A., Bhushan A., Sinha M.,
RA Kaur P., Sharma S., Singh T.P.;
RT "Crystal structure of goat lactoperoxidase with 3-Amino pyrazole at 1.79
RT Angstrom resolution.";
RL Submitted (OCT-2013) to the PDB data bank.
RN [8]
RP RETRACTED PAPER.
RX PubMed=25760705; DOI=10.1107/s2053230x15001806;
RA Singh R.P., Singh A., Kushwaha G.S., Singh A.K., Kaur P., Sharma S.,
RA Singh T.P.;
RT "Mode of binding of the antithyroid drug propylthiouracil to mammalian haem
RT peroxidases.";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:304-310(2015).
RN [9] {ECO:0000305}
RP RETRACTION NOTICE OF PUBMED:25760705.
RX PubMed=26057817; DOI=10.1107/s2053230x15006962;
RA Singh R.P., Singh A., Kushwaha G.S., Singh A.K., Kaur P., Sharma S.,
RA Singh T.P.;
RT "Retraction: Mode of binding of the antithyroid drug propylthiouracil to
RT mammalian haem peroxidases.";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:804-804(2015).
RN [10] {ECO:0007744|PDB:5FF1}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 118-712 IN COMPLEX WITH CALCIUM
RP AND HEME, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, AND DISULFIDE
RP BONDS.
RX PubMed=27398304; DOI=10.1002/2211-5463.12051;
RA Singh R.P., Singh A., Sirohi H.V., Singh A.K., Kaur P., Sharma S.,
RA Singh T.P.;
RT "Dual binding mode of antithyroid drug methimazole to mammalian heme
RT peroxidases - structural determination of the lactoperoxidase-methimazole
RT complex at 1.97 A resolution.";
RL FEBS Open Bio 6:640-650(2016).
RN [11] {ECO:0007744|PDB:5HPW}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 118-712 IN COMPLEX WITH CALCIUM
RP AND HEME, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, AND
RP DISULFIDE BONDS.
RA Singh R.P., Singh A., Sharma P., Kaur P., Sharma S., Singh T.P.;
RT "Mode of binding of antithyroid drug, propylthiouracil to lactoperoxidase:
RT Binding studies and structure determination.";
RL Submitted (JAN-2016) to the PDB data bank.
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) (By similarity).
CC Also involved in the conversion of iodide (I(-)) into hypoiodite
CC (IO(-)) in the presence of H2O2 (By similarity). Responsible for the
CC inactivation of a wide range of micro-organisms and hence, important
CC component of defense mechanism (PubMed:10894086). Shows antibacterial
CC properties against several Gram-positive bacteria including some
CC Staphylococcus species and Gram-negative bacteria including E.coli,
CC P.aeruginosa and some Salmonella species (PubMed:10894086). Inhibits
CC the growth of several fungi including A.niger, Trichoderma species,
CC C.cassicola, P.meadii and C.salmonicolor (PubMed:10894086). Does not
CC have anti-fungal activity towards C.albicans and Pythium species
CC (PubMed:10894086). May protect the udder from infection and may promote
CC growth in newborns (PubMed:10894086). May be implicated in airway host
CC defense against infection (By similarity). May contribute to
CC maintaining an appropriate H2O2 cellular level, therefore protecting
CC cells from H2O2-caused injuries and inflammation (By similarity).
CC {ECO:0000250|UniProtKB:P22079, ECO:0000250|UniProtKB:P80025,
CC ECO:0000250|UniProtKB:Q5SW46, ECO:0000269|PubMed:10894086}.
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:0000250|UniProtKB:P80025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137;
CC Evidence={ECO:0000250|UniProtKB:P80025};
CC -!- CATALYTIC ACTIVITY:
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:0000250|UniProtKB:P80025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417;
CC Evidence={ECO:0000250|UniProtKB:P80025};
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 Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-
CC ProRule:PRU00298, ECO:0000269|PubMed:18191143,
CC ECO:0000269|PubMed:27398304};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298,
CC ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304};
CC -!- ACTIVITY REGULATION: Inhibited by small molecule methimazole (MMZ).
CC {ECO:0000269|PubMed:27398304}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18191143,
CC ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5SW46}.
CC -!- TISSUE SPECIFICITY: Mammary gland; milk. {ECO:0000269|PubMed:18191143,
CC ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068}.
CC -!- BIOTECHNOLOGY: The lactoperoxidase system is used by the dairy industry
CC for the preservation of raw milk during transportation
CC (PubMed:10894086). Freshly obtained milk is supplemented with
CC thiocyanate and hydrogen peroxide which are used by milk LPO to produce
CC antimicrobial agents (PubMed:10894086). {ECO:0000269|PubMed:10894086}.
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:0000305}.
CC -!- CAUTION: The drug propylthiouracilin was reported to bind to the distal
CC heme-pockets of LPO (PubMed:25760705). However, the paper was retracted
CC as some concerns were raised about the modeling.
CC {ECO:0000269|PubMed:25760705, ECO:0000305|PubMed:26057817}.
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DR EMBL; EF363153; ABN41562.1; -; mRNA.
DR EMBL; LWLT01000022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001272546.1; NM_001285617.1.
DR RefSeq; XP_017919048.1; XM_018063559.1.
DR RefSeq; XP_017919049.1; XM_018063560.1.
DR RefSeq; XP_017919050.1; XM_018063561.1.
DR RefSeq; XP_017919051.1; XM_018063562.1.
DR PDB; 2E9E; X-ray; 3.25 A; A/B=118-712.
DR PDB; 2EFB; X-ray; 2.94 A; A/B=118-712.
DR PDB; 2EHA; X-ray; 3.30 A; A/B=118-712.
DR PDB; 2OJV; X-ray; 2.40 A; A=118-712.
DR PDB; 2R5L; X-ray; 2.40 A; A=118-712.
DR PDB; 3N8F; X-ray; 3.25 A; A/B=118-712.
DR PDB; 3NAK; X-ray; 3.30 A; A/B=118-712.
DR PDB; 3NIU; X-ray; 2.94 A; A/B=118-712.
DR PDB; 3QF1; X-ray; 2.60 A; A=118-712.
DR PDB; 3R55; X-ray; 2.10 A; A=118-712.
DR PDB; 3RKE; X-ray; 2.30 A; A=118-712.
DR PDB; 3SXV; X-ray; 2.10 A; A=118-712.
DR PDB; 4MSF; X-ray; 1.98 A; A=118-712.
DR PDB; 4OEK; X-ray; 2.47 A; A=118-712.
DR PDB; 4QJQ; X-ray; 2.10 A; A=118-712.
DR PDB; 5FF1; X-ray; 1.97 A; A/B=118-712.
DR PDB; 5HPW; X-ray; 2.50 A; A/B/C/D=118-712.
DR PDB; 6LF7; X-ray; 1.79 A; A=118-712.
DR PDB; 7WCS; X-ray; 1.98 A; A=118-712.
DR PDBsum; 2E9E; -.
DR PDBsum; 2EFB; -.
DR PDBsum; 2EHA; -.
DR PDBsum; 2OJV; -.
DR PDBsum; 2R5L; -.
DR PDBsum; 3N8F; -.
DR PDBsum; 3NAK; -.
DR PDBsum; 3NIU; -.
DR PDBsum; 3QF1; -.
DR PDBsum; 3R55; -.
DR PDBsum; 3RKE; -.
DR PDBsum; 3SXV; -.
DR PDBsum; 4MSF; -.
DR PDBsum; 4OEK; -.
DR PDBsum; 4QJQ; -.
DR PDBsum; 5FF1; -.
DR PDBsum; 5HPW; -.
DR PDBsum; 6LF7; -.
DR PDBsum; 7WCS; -.
DR AlphaFoldDB; A0A452E9Y6; -.
DR SMR; A0A452E9Y6; -.
DR STRING; 9925.ENSCHIP00000008975; -.
DR PeroxiBase; 5320; ChiLPO01.
DR iPTMnet; A0A452E9Y6; -.
DR Ensembl; ENSCHIT00000016739; ENSCHIP00000008975; ENSCHIG00000011979.
DR GeneID; 100860761; -.
DR KEGG; chx:100860761; -.
DR CTD; 4025; -.
DR GeneTree; ENSGT00940000160488; -.
DR OMA; QNKMMTR; -.
DR OrthoDB; 276568at2759; -.
DR Proteomes; UP000291000; Chromosome 19.
DR Bgee; ENSCHIG00000011979; Expressed in rumen and 5 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0036393; F:thiocyanate peroxidase activity; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0046265; P:thiocyanate catabolic process; IDA:UniProtKB.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Nitration; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..117
FT /evidence="ECO:0000269|PubMed:18191143"
FT /id="PRO_0000447715"
FT CHAIN 118..712
FT /note="Lactoperoxidase"
FT /evidence="ECO:0000269|PubMed:18191143"
FT /id="PRO_5002652894"
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="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:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT BINDING 375
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
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:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT SITE 372
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18191143"
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:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:30296068"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:30296068"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE,
FT ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF,
FT ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ,
FT ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW,
FT ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE,
FT ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF,
FT ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ,
FT ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW,
FT ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E,
FT ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA,
FT ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L,
FT ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK,
FT ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1,
FT ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE,
FT ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF,
FT ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ,
FT ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW,
FT ECO:0007744|PDB:6LF7, ECO:0007744|PDB:7WCS"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304,
FT ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT DISULFID 123..284
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT DISULFID 132..145
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT DISULFID 246..256
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT DISULFID 250..274
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT DISULFID 354..365
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT DISULFID 573..630
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT DISULFID 671..696
FT /evidence="ECO:0000269|PubMed:18191143,
FT ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB,
FT ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV,
FT ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F,
FT ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU,
FT ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55,
FT ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV,
FT ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK,
FT ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1,
FT ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7,
FT ECO:0007744|PDB:7WCS"
FT CONFLICT 113
FT /note="D -> E (in Ref. 1; ABN41562)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..135
FT /note="KCDEN -> TCDEQ (in Ref. 1; ABN41562)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..255
FT /note="IQGDN -> VQGDE (in Ref. 1; ABN41562)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="K -> N (in Ref. 1; ABN41562)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="I -> V (in Ref. 1; ABN41562)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="I -> V (in Ref. 1; ABN41562)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="V -> I (in Ref. 1; ABN41562)"
FT /evidence="ECO:0000305"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:4OEK"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2OJV"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6LF7"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3R55"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:6LF7"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5FF1"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2EFB"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2OJV"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2OJV"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:5FF1"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:3RKE"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:6LF7"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6LF7"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 377..400
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 406..427
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:3QF1"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:6LF7"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 509..518
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:3R55"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:2EHA"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 550..560
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 566..572
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 581..588
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 591..601
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 609..615
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 626..641
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 655..661
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 666..673
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:6LF7"
FT TURN 689..692
FT /evidence="ECO:0007829|PDB:6LF7"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:6LF7"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:6LF7"
SQ SEQUENCE 712 AA; 80366 MW; 00D61198D3B757C7 CRC64;
MLVCLHLQVF LASVALFEVA ASDTIAQAAS TTTISDAVSK VKTQVNKAFL DSRTRLKTAL
SSEAPTTRQL SEYFKHAKGR TRTAIRNGQV WEESLKRLRR DTTLTNVTDP SLDLTALSWE
VGCGAPVPLV KCDENSPYRT ITGDCNNRRS PALGAANRAL ARWLPAEYED GLAVPFGWTQ
RKTRNGFRVP LAREVSNKIV GYLDEEGVLD QNRSLLFMQW GQIVDHDLDF APETELGSSE
HSKVQCEEYC IQGDNCFPIM FPKNDPKLKT QGKCMPFFRA GFVCPTPPYQ SLARDQINAV
TSFLDASLVY GSEPSLASRL RNLSSPLGLM AVNQEAWDHG LAYPPFNNVK PSPCEFINTT
AHVPCFQAGD SRASEQILLA TVHTLLLREH NRLARELKRL NPHWDGEMLY QEARKILGAF
IQIITFRDYL PIVLGSEMQK WIPPYQGYNN SVDPRISNVF TFAFRFGHME VPSTVSRLDE
NYQPWGPEAE LPLHTLFFNT WRIIKDGGID PLVRGLLAKK SKLMNQNKMV TSELRNKLFQ
PTHKIHGFDL AAINLQRCRD HGMPGYNSWR GFCGLSQPKT LKGLQAVLKN KILAKKLLDL
YKTPDNIDIW IGGNAEPMVE RGRVGPLLAC LLGRQFQQIR DGDRFWWENP GVFTEKQRDS
LQKVSFSRLI CDNTHVTKVP LHAFQANNYP HDFVDCSAVD KLDLSPWASR EN
