ID MYG_HORSE Reviewed; 154 AA. AC P68082; P02188; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 131. DE RecName: Full=Myoglobin {ECO:0000303|PubMed:4902609}; DE AltName: Full=Nitrite reductase MB {ECO:0000305|PubMed:32891753}; DE EC=1.7.-.- {ECO:0000269|PubMed:32891753}; DE AltName: Full=Pseudoperoxidase MB {ECO:0000250|UniProtKB:P02144}; DE EC=1.11.1.- {ECO:0000250|UniProtKB:P02144}; GN Name=MB; 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 PROTEIN SEQUENCE OF 2-154. RC TISSUE=Heart muscle; RX PubMed=4902609; DOI=10.1111/j.1432-1033.1969.tb00769.x; RA Dautrevaux M., Boulanger Y., Han K., Biserte G.; RT "Covalent structure of horse myoglobin."; RL Eur. J. Biochem. 11:267-277(1969). RN [2] RP PROTEIN SEQUENCE OF 2-154. RC TISSUE=Skeletal muscle; RA Romero-Herrera A.E., Lehmann H.; RT "Residue 122 of sperm whale and horse myoglobin."; RL Biochim. Biophys. Acta 336:318-323(1974). RN [3] RP PROTEIN SEQUENCE OF 2-16 AND 57-71. RX PubMed=2302197; DOI=10.1016/0006-291x(90)91922-f; RA Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J.; RT "Internal amino acid sequencing of proteins by in situ cyanogen bromide RT cleavage in polyacrylamide gels."; RL Biochem. Biophys. Res. Commun. 166:139-145(1990). RN [4] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=32891753; DOI=10.1016/j.niox.2020.08.005; RA Quesnelle K., Guimaraes D.A., Rao K., Singh A.B., Wang Y., Hogg N., RA Shiva S.; RT "Myoglobin promotes nitrite-dependent mitochondrial S-nitrosation to RT mediate cytoprotection after hypoxia/reoxygenation."; RL Nitric Oxide 104:36-43(2020). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME. RX PubMed=2359126; DOI=10.1016/s0022-2836(05)80270-0; RA Evans S.V., Brayer G.D.; RT "High-resolution study of the three-dimensional structure of horse heart RT metmyoglobin."; RL J. Mol. Biol. 213:885-897(1990). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=3346247; DOI=10.1016/s0021-9258(18)68919-7; RA Evans S.V., Brayer G.D.; RT "Horse heart metmyoglobin. A 2.8-A resolution three-dimensional structure RT determination."; RL J. Biol. Chem. 263:4263-4268(1988). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-65. RX PubMed=7654702; DOI=10.1021/bi00033a021; RA Bogumil R., Maurus R., Hildebrand D.P., Brayer G.D., Mauk A.G.; RT "Origin of the pH-dependent spectroscopic properties of pentacoordinate RT metmyoglobin variants."; RL Biochemistry 34:10483-10490(1995). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME. RX PubMed=10706294; DOI=10.1038/35002641; RA Chu K., Vojtchovsky J., McMahon B.H., Sweet R.M., Berendzen J., RA Schlichting I.; RT "Structure of a ligand-binding intermediate in wild-type carbonmonoxy RT myoglobin."; RL Nature 403:921-923(2000). RN [9] {ECO:0007744|PDB:3VAU} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-154 IN COMPLEX WITH NITRITE. RX PubMed=22430128; DOI=10.1039/c2cc31065a; RA Yi J., Richter-Addo G.B.; RT "Unveiling the three-dimensional structure of the green pigment of nitrite- RT cured meat."; RL Chem. Commun. (Camb.) 48:4172-4174(2012). CC -!- FUNCTION: Monomeric heme protein which primary function is to store CC oxygen and facilitate its diffusion within muscle tissues. Reversibly CC binds oxygen through a pentacoordinated heme iron and enables its CC timely and efficient release as needed during periods of heightened CC demand (By similarity). Depending on the oxidative conditions of CC tissues and cells, and in addition to its ability to bind oxygen, it CC also has a nitrite reductase activity whereby it regulates the CC production of bioactive nitric oxide (PubMed:32891753). Under stress CC conditions, like hypoxia and anoxia, it also protects cells against CC reactive oxygen species thanks to its pseudoperoxidase activity (By CC similarity). {ECO:0000250|UniProtKB:P02144, CC ECO:0000269|PubMed:32891753}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b- CC [protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA- CC COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, CC ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; CC Evidence={ECO:0000269|PubMed:32891753}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; CC Evidence={ECO:0000305|PubMed:32891753}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P02144}; CC -!- SUBUNIT: Monomeric. {ECO:0000250|UniProtKB:P02185}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm CC {ECO:0000250|UniProtKB:P02144}. CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE- CC ProRule:PRU00238}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; A91098; MYHO. DR RefSeq; NP_001157488.1; NM_001164016.1. DR PDB; 1AZI; X-ray; 2.00 A; A=2-154. DR PDB; 1BJE; X-ray; 1.80 A; A=2-154. DR PDB; 1DWR; X-ray; 1.45 A; A=2-154. DR PDB; 1DWS; X-ray; 1.45 A; A=2-154. DR PDB; 1DWT; X-ray; 1.40 A; A=2-154. DR PDB; 1GJN; X-ray; 1.35 A; A=2-154. DR PDB; 1HRM; X-ray; 1.70 A; A=2-154. DR PDB; 1HSY; X-ray; 1.90 A; A=2-154. DR PDB; 1NPF; X-ray; 1.90 A; A=2-154. DR PDB; 1NPG; X-ray; 1.70 A; A=2-154. DR PDB; 1NZ2; X-ray; 1.90 A; A=2-154. DR PDB; 1NZ3; X-ray; 1.60 A; A=2-154. DR PDB; 1NZ4; X-ray; 1.80 A; A=2-154. DR PDB; 1NZ5; X-ray; 1.70 A; A=2-154. DR PDB; 1RSE; X-ray; 1.70 A; A=2-154. DR PDB; 1WLA; X-ray; 1.70 A; A=2-154. DR PDB; 1XCH; X-ray; 1.70 A; A=2-154. DR PDB; 1YMA; X-ray; 2.00 A; A=2-154. DR PDB; 1YMB; X-ray; 1.90 A; A=2-154. DR PDB; 1YMC; X-ray; 2.00 A; A=2-154. DR PDB; 2FRF; X-ray; 1.20 A; A=2-154. DR PDB; 2FRI; X-ray; 1.60 A; X=2-154. DR PDB; 2FRJ; X-ray; 1.30 A; X=2-154. DR PDB; 2FRK; X-ray; 1.30 A; X=2-154. DR PDB; 2IN4; X-ray; 2.15 A; A=2-154. DR PDB; 2NSR; X-ray; 1.90 A; A=2-154. DR PDB; 2NSS; X-ray; 2.00 A; A=2-154. DR PDB; 2O58; X-ray; 1.65 A; X=2-154. DR PDB; 2O5B; X-ray; 2.00 A; X=2-154. DR PDB; 2O5L; X-ray; 1.70 A; X=2-154. DR PDB; 2O5M; X-ray; 1.65 A; X=2-154. DR PDB; 2O5O; X-ray; 1.60 A; X=2-154. DR PDB; 2O5Q; X-ray; 1.90 A; X=2-154. DR PDB; 2O5S; X-ray; 1.60 A; X=2-154. DR PDB; 2O5T; X-ray; 1.60 A; X=2-154. DR PDB; 2V1E; X-ray; 1.30 A; A=2-154. DR PDB; 2V1F; X-ray; 1.20 A; A=2-154. DR PDB; 2V1G; X-ray; 1.35 A; A=2-154. DR PDB; 2V1H; X-ray; 1.30 A; A=2-154. DR PDB; 2V1I; X-ray; 1.20 A; A=2-154. DR PDB; 2V1J; X-ray; 1.40 A; A=2-154. DR PDB; 2V1K; X-ray; 1.25 A; A=2-154. DR PDB; 2VLX; X-ray; 1.30 A; A=2-154. DR PDB; 2VLY; X-ray; 1.60 A; A=2-154. DR PDB; 2VLZ; X-ray; 1.50 A; A=2-154. DR PDB; 2VM0; X-ray; 1.60 A; A=2-154. DR PDB; 3BA2; X-ray; 1.80 A; A=2-154. DR PDB; 3HC9; X-ray; 2.00 A; A=2-154. DR PDB; 3HEN; X-ray; 1.90 A; A=2-154. DR PDB; 3HEO; X-ray; 2.00 A; A=2-154. DR PDB; 3HEP; X-ray; 1.95 A; A=2-154. DR PDB; 3LR7; X-ray; 1.60 A; A=2-154. DR PDB; 3LR9; X-ray; 1.55 A; A=2-154. DR PDB; 3RJ6; X-ray; 1.23 A; A/B=2-154. DR PDB; 3RJN; X-ray; 1.90 A; B=2-154. DR PDB; 3V2V; X-ray; 1.65 A; A=2-154. DR PDB; 3V2Z; X-ray; 1.65 A; A=2-154. DR PDB; 3VAU; X-ray; 1.70 A; A=2-154. DR PDB; 3VM9; X-ray; 1.05 A; A/B=2-154. DR PDB; 3WFT; X-ray; 1.30 A; A=2-154. DR PDB; 3WFU; X-ray; 1.35 A; A=2-154. DR PDB; 3WI8; X-ray; 2.20 A; A=2-154. DR PDB; 3WYO; X-ray; 2.00 A; A/B/C/D=2-154. DR PDB; 4DC7; X-ray; 1.50 A; A=2-153. DR PDB; 4DC8; X-ray; 1.50 A; A=2-153. DR PDB; 4NS2; X-ray; 1.18 A; A=1-154. DR PDB; 4TWU; X-ray; 1.08 A; A=1-154. DR PDB; 4TWV; X-ray; 1.06 A; A=1-154. DR PDB; 5AZQ; X-ray; 1.40 A; A=2-154. DR PDB; 5AZR; X-ray; 1.20 A; A=2-154. DR PDB; 5CMV; X-ray; 1.80 A; A=2-153. DR PDB; 5CN4; X-ray; 1.80 A; A=2-153. DR PDB; 5CN5; X-ray; 1.80 A; A=2-153. DR PDB; 5CN6; X-ray; 1.80 A; A=2-153. DR PDB; 5CN7; X-ray; 1.80 A; A=2-153. DR PDB; 5CN8; X-ray; 1.80 A; A=2-153. DR PDB; 5CN9; X-ray; 1.80 A; A=2-153. DR PDB; 5CNB; X-ray; 1.80 A; A=2-153. DR PDB; 5CNC; X-ray; 1.80 A; A=2-153. DR PDB; 5CND; X-ray; 1.80 A; A=2-153. DR PDB; 5CNE; X-ray; 1.80 A; A=2-153. DR PDB; 5CNF; X-ray; 1.80 A; A=2-153. DR PDB; 5CNG; X-ray; 1.80 A; A=2-153. DR PDB; 5D5R; X-ray; 1.60 A; A=2-153. DR PDB; 5YCG; X-ray; 2.40 A; A=1-154. DR PDB; 5YL3; X-ray; 1.50 A; A=1-154. DR PDB; 5Z7E; X-ray; 1.80 A; A=2-154. DR PDB; 5Z7F; X-ray; 1.90 A; A=2-154. DR PDB; 5ZZE; X-ray; 1.42 A; A=2-153. DR PDB; 6LS8; X-ray; 2.30 A; A/C/E/G/I/K=2-154. DR PDB; 6LTL; X-ray; 1.25 A; A/B=2-154. DR PDB; 6LTM; X-ray; 1.65 A; A/B=2-154. DR PDB; 7DGJ; X-ray; 1.60 A; A/B=2-154. DR PDB; 7DGK; X-ray; 1.75 A; A/B=2-154. DR PDB; 7DGL; X-ray; 1.91 A; A/B=2-154. DR PDB; 7DGM; X-ray; 1.62 A; A/B=2-154. DR PDB; 7DGN; X-ray; 2.35 A; A/B=2-154. DR PDB; 7DGO; X-ray; 2.00 A; A/B=2-154. DR PDB; 7V5P; X-ray; 1.16 A; A/B=2-154. DR PDB; 7V5Q; X-ray; 1.38 A; A/B=2-154. DR PDB; 7V5R; X-ray; 1.39 A; A/B=2-154. DR PDBsum; 1AZI; -. DR PDBsum; 1BJE; -. DR PDBsum; 1DWR; -. DR PDBsum; 1DWS; -. DR PDBsum; 1DWT; -. DR PDBsum; 1GJN; -. DR PDBsum; 1HRM; -. DR PDBsum; 1HSY; -. DR PDBsum; 1NPF; -. DR PDBsum; 1NPG; -. DR PDBsum; 1NZ2; -. DR PDBsum; 1NZ3; -. DR PDBsum; 1NZ4; -. DR PDBsum; 1NZ5; -. DR PDBsum; 1RSE; -. DR PDBsum; 1WLA; -. DR PDBsum; 1XCH; -. DR PDBsum; 1YMA; -. DR PDBsum; 1YMB; -. DR PDBsum; 1YMC; -. DR PDBsum; 2FRF; -. DR PDBsum; 2FRI; -. DR PDBsum; 2FRJ; -. DR PDBsum; 2FRK; -. DR PDBsum; 2IN4; -. DR PDBsum; 2NSR; -. DR PDBsum; 2NSS; -. DR PDBsum; 2O58; -. DR PDBsum; 2O5B; -. DR PDBsum; 2O5L; -. DR PDBsum; 2O5M; -. DR PDBsum; 2O5O; -. DR PDBsum; 2O5Q; -. DR PDBsum; 2O5S; -. DR PDBsum; 2O5T; -. DR PDBsum; 2V1E; -. DR PDBsum; 2V1F; -. DR PDBsum; 2V1G; -. DR PDBsum; 2V1H; -. DR PDBsum; 2V1I; -. DR PDBsum; 2V1J; -. DR PDBsum; 2V1K; -. DR PDBsum; 2VLX; -. DR PDBsum; 2VLY; -. DR PDBsum; 2VLZ; -. DR PDBsum; 2VM0; -. DR PDBsum; 3BA2; -. DR PDBsum; 3HC9; -. DR PDBsum; 3HEN; -. DR PDBsum; 3HEO; -. DR PDBsum; 3HEP; -. DR PDBsum; 3LR7; -. DR PDBsum; 3LR9; -. DR PDBsum; 3RJ6; -. DR PDBsum; 3RJN; -. DR PDBsum; 3V2V; -. DR PDBsum; 3V2Z; -. DR PDBsum; 3VAU; -. DR PDBsum; 3VM9; -. DR PDBsum; 3WFT; -. DR PDBsum; 3WFU; -. DR PDBsum; 3WI8; -. DR PDBsum; 3WYO; -. DR PDBsum; 4DC7; -. DR PDBsum; 4DC8; -. DR PDBsum; 4NS2; -. DR PDBsum; 4TWU; -. DR PDBsum; 4TWV; -. DR PDBsum; 5AZQ; -. DR PDBsum; 5AZR; -. DR PDBsum; 5CMV; -. DR PDBsum; 5CN4; -. DR PDBsum; 5CN5; -. DR PDBsum; 5CN6; -. DR PDBsum; 5CN7; -. DR PDBsum; 5CN8; -. DR PDBsum; 5CN9; -. DR PDBsum; 5CNB; -. DR PDBsum; 5CNC; -. DR PDBsum; 5CND; -. DR PDBsum; 5CNE; -. DR PDBsum; 5CNF; -. DR PDBsum; 5CNG; -. DR PDBsum; 5D5R; -. DR PDBsum; 5YCG; -. DR PDBsum; 5YL3; -. DR PDBsum; 5Z7E; -. DR PDBsum; 5Z7F; -. DR PDBsum; 5ZZE; -. DR PDBsum; 6LS8; -. DR PDBsum; 6LTL; -. DR PDBsum; 6LTM; -. DR PDBsum; 7DGJ; -. DR PDBsum; 7DGK; -. DR PDBsum; 7DGL; -. DR PDBsum; 7DGM; -. DR PDBsum; 7DGN; -. DR PDBsum; 7DGO; -. DR PDBsum; 7V5P; -. DR PDBsum; 7V5Q; -. DR PDBsum; 7V5R; -. DR AlphaFoldDB; P68082; -. DR BMRB; P68082; -. DR PCDDB; P68082; -. DR SASBDB; P68082; -. DR SMR; P68082; -. DR STRING; 9796.ENSECAP00000015509; -. DR Allergome; 10877; Equ c Myoglobin. DR CarbonylDB; P68082; -. DR CPTAC; CPTAC-1474; -. DR PaxDb; 9796-ENSECAP00000015509; -. DR ABCD; P68082; 1 sequenced antibody. DR Ensembl; ENSECAT00000036478.2; ENSECAP00000026577.1; ENSECAG00000017982.4. DR GeneID; 100054434; -. DR KEGG; ecb:100054434; -. DR CTD; 4151; -. DR VGNC; VGNC:20004; MB. DR GeneTree; ENSGT00940000160809; -. DR HOGENOM; CLU_003827_18_0_1; -. DR InParanoid; P68082; -. DR OrthoDB; 4233999at2759; -. DR TreeFam; TF332967; -. DR SABIO-RK; P68082; -. DR EvolutionaryTrace; P68082; -. DR Proteomes; UP000002281; Chromosome 28. DR Bgee; ENSECAG00000017982; Expressed in gluteus medius and 12 other cell types or tissues. DR GO; GO:0016528; C:sarcoplasm; ISS:UniProtKB. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0098809; F:nitrite reductase activity; IDA:UniProtKB. DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central. DR GO; GO:0005344; F:oxygen carrier activity; ISS:UniProtKB. DR GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB. DR GO; GO:0015671; P:oxygen transport; IBA:GO_Central. DR GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB. DR CDD; cd08926; Mb; 1. DR Gene3D; 6.10.140.2100; -; 1. DR Gene3D; 6.10.140.2110; -; 1. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin-like_sf. DR InterPro; IPR002335; Myoglobin. DR PANTHER; PTHR47132; MYOGLOBIN; 1. DR PANTHER; PTHR47132:SF1; MYOGLOBIN; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00613; MYOGLOBIN. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Heme; Iron; KW Metal-binding; Muscle protein; Oxidoreductase; Oxygen transport; KW Phosphoprotein; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2302197, FT ECO:0000269|PubMed:4902609, ECO:0000269|Ref.2" FT CHAIN 2..154 FT /note="Myoglobin" FT /id="PRO_0000053302" FT BINDING 65 FT /ligand="nitrite" FT /ligand_id="ChEBI:CHEBI:16301" FT /evidence="ECO:0000269|PubMed:22430128, FT ECO:0007744|PDB:3VAU" FT BINDING 65 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:P02189, FT ECO:0000255|PROSITE-ProRule:PRU00238" FT BINDING 94 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="proximal binding residue" FT /evidence="ECO:0000269|PubMed:10706294, FT ECO:0000269|PubMed:2359126, ECO:0000269|PubMed:7654702, FT ECO:0007744|PDB:1AZI, ECO:0007744|PDB:1BJE, FT ECO:0007744|PDB:1DWR, ECO:0007744|PDB:1DWS, FT ECO:0007744|PDB:1DWT, ECO:0007744|PDB:1GJN, FT ECO:0007744|PDB:1HSY, ECO:0007744|PDB:1NPF, FT ECO:0007744|PDB:1NPG, ECO:0007744|PDB:1NZ2, FT ECO:0007744|PDB:1NZ3, ECO:0007744|PDB:1NZ4, FT ECO:0007744|PDB:1NZ5, ECO:0007744|PDB:1RSE, FT ECO:0007744|PDB:1WLA, ECO:0007744|PDB:1XCH, FT ECO:0007744|PDB:1YMA, ECO:0007744|PDB:1YMB, FT ECO:0007744|PDB:2FRF, ECO:0007744|PDB:2FRI, FT ECO:0007744|PDB:2FRJ, ECO:0007744|PDB:2FRK, FT ECO:0007744|PDB:2NSR, ECO:0007744|PDB:2NSS, FT ECO:0007744|PDB:2V1E, ECO:0007744|PDB:2V1F, FT ECO:0007744|PDB:2V1G, ECO:0007744|PDB:2V1H, FT ECO:0007744|PDB:2V1I, ECO:0007744|PDB:2V1J, FT ECO:0007744|PDB:2V1K, ECO:0007744|PDB:2VLX, FT ECO:0007744|PDB:2VLY, ECO:0007744|PDB:2VLZ, FT ECO:0007744|PDB:2VM0, ECO:0007744|PDB:3HC9, FT ECO:0007744|PDB:3HEN, ECO:0007744|PDB:3HEO, FT ECO:0007744|PDB:3HEP, ECO:0007744|PDB:3LR7, FT ECO:0007744|PDB:3LR9, ECO:0007744|PDB:3RJ6, FT ECO:0007744|PDB:3VM9, ECO:0007744|PDB:3WYO, FT ECO:0007744|PDB:4DC7, ECO:0007744|PDB:4DC8, FT ECO:0007744|PDB:4NS2" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QZ76" FT CONFLICT 123 FT /note="D -> N (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 5..19 FT /evidence="ECO:0007829|PDB:3VM9" FT HELIX 22..36 FT /evidence="ECO:0007829|PDB:3VM9" FT HELIX 38..41 FT /evidence="ECO:0007829|PDB:3VM9" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:3VM9" FT HELIX 53..58 FT /evidence="ECO:0007829|PDB:3VM9" FT HELIX 60..96 FT /evidence="ECO:0007829|PDB:3VM9" FT HELIX 102..119 FT /evidence="ECO:0007829|PDB:3VM9" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:3VM9" FT HELIX 126..149 FT /evidence="ECO:0007829|PDB:3VM9" FT TURN 150..153 FT /evidence="ECO:0007829|PDB:5AZQ" SQ SEQUENCE 154 AA; 17083 MW; 20EABC4A66ACE975 CRC64; MGLSDGEWQQ VLNVWGKVEA DIAGHGQEVL IRLFTGHPET LEKFDKFKHL KTEAEMKASE DLKKHGTVVL TALGGILKKK GHHEAELKPL AQSHATKHKI PIKYLEFISD AIIHVLHSKH PGDFGADAQG AMTKALELFR NDIAAKYKEL GFQG //