PAO1_MAIZE
ID PAO1_MAIZE Reviewed; 500 AA.
AC O64411; Q546R6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Polyamine oxidase 1 {ECO:0000303|Ref.2};
DE EC=1.5.3.14 {ECO:0000269|Ref.4};
DE EC=1.5.3.15 {ECO:0000269|Ref.4};
DE Flags: Precursor;
GN Name=MPAO1 {ECO:0000303|Ref.2};
GN Synonyms=MPAO {ECO:0000303|PubMed:16331971},
GN PAO {ECO:0000303|PubMed:9598979};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-93; 97-111; 115-147;
RP 150-152; 154-162; 164-225; 227-241; 254-266; 270-278; 292-314; 317-323;
RP 329-332; 343-352; 355-383; 385-394; 404-459; 461-471; 477-487 AND 493-496.
RC STRAIN=cv. Paolo; TISSUE=Etiolated seedling;
RX PubMed=9598979; DOI=10.1016/s0014-5793(98)00311-1;
RA Tavladoraki P., Schinina M.E., Cecconi F., Di Agostino S., Manera F.,
RA Rea G., Mariottini P., Federico R., Angelini R.;
RT "Maize polyamine oxidase: primary structure from protein and cDNA
RT sequencing.";
RL FEBS Lett. 426:62-66(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Paolo;
RX DOI=10.1016/S0981-9428(00)01170-0;
RA Cervelli M., Tavladoraki P., Di Agostino S., Angelini R., Federico R.,
RA Mariottini P.;
RT "Isolation and characterization of three polyamine oxidase genes from Zea
RT mays.";
RL Plant Physiol. Biochem. 38:667-677(2000).
RN [3]
RP SUBUNIT, AND COFACTOR.
RX DOI=10.1016/0031-9422(89)85004-6;
RA Federico R., Alisi C., Forlani F.;
RT "Properties of the polyamine oxidase from the cell wall of maize
RT seedlings.";
RL Phytochemistry 28:45-46(1989).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1016/0031-9422(96)00316-0;
RA Federico R., Ercolini L., Laurenzi M., Angelini R.;
RT "Oxidation of acetylpolyamines by maize polyamine oxidase.";
RL Phytochemistry 43:339-341(1996).
RN [5]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=12586904; DOI=10.1104/pp.011379;
RA Cona A., Cenci F., Cervelli M., Federico R., Mariottini P., Moreno S.,
RA Angelini R.;
RT "Polyamine oxidase, a hydrogen peroxide-producing enzyme, is up-regulated
RT by light and down-regulated by auxin in the outer tissues of the maize
RT mesocotyl.";
RL Plant Physiol. 131:803-813(2003).
RN [6]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP LYS-328.
RX PubMed=16331971; DOI=10.1021/bi050983i;
RA Polticelli F., Basran J., Faso C., Cona A., Minervini G., Angelini R.,
RA Federico R., Scrutton N.S., Tavladoraki P.;
RT "Lys300 plays a major role in the catalytic mechanism of maize polyamine
RT oxidase.";
RL Biochemistry 44:16108-16120(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), AND CRYSTALLIZATION.
RX PubMed=10089528; DOI=10.1107/s0907444998005836;
RA Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A.;
RT "Crystallization and preliminary X-ray analysis of polyamine oxidase from
RT Zea mays L.";
RL Acta Crystallogr. D 54:1429-1431(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND
RP SYNTHETIC INHIBITORS, GLYCOSYLATION AT ASN-105, AND DISULFIDE BOND.
RX PubMed=10368296; DOI=10.1016/s0969-2126(99)80037-9;
RA Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A.;
RT "A 30-A-long U-shaped catalytic tunnel in the crystal structure of
RT polyamine oxidase.";
RL Structure 7:265-276(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND
RP SYNTHETIC INHIBITORS, GLYCOSYLATION AT ASN-105, AND DISULFIDE BOND.
RX PubMed=11258887; DOI=10.1021/bi002751j;
RA Binda C., Angelini R., Federico R., Ascenzi P., Mattevi A.;
RT "Structural bases for inhibitor binding and catalysis in polyamine
RT oxidase.";
RL Biochemistry 40:2766-2776(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 29-500 IN COMPLEX WITH SPERMINE
RP AND SPERMIDINE.
RA Fiorillo A., Ilari A., Tavladoraki P.;
RT "The crystal structure of the mutant Lys300Met of polyamine oxidase from
RT Zea Mays unveils the role of Lys300 in catalysis.";
RL Submitted (NOV-2009) to the PDB data bank.
CC -!- FUNCTION: Flavoenzyme involved in polyamine back-conversion (Ref.4,
CC PubMed:16331971). Catalyzes the oxidation of the secondary amino group
CC of polyamines, such as spermine, spermidine and their acetyl
CC derivatives (Ref.4, PubMed:16331971). Plays an important role in the
CC regulation of polyamine intracellular concentration (Probable).
CC {ECO:0000269|PubMed:16331971, ECO:0000269|Ref.4, ECO:0000305|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + spermidine = 4-aminobutanal + H2O2 + propane-1,3-
CC diamine; Xref=Rhea:RHEA:25820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57484, ChEBI:CHEBI:57834,
CC ChEBI:CHEBI:58264; EC=1.5.3.14; Evidence={ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(8)-acetylspermidine + O2 = 4-acetamidobutanal + H2O2 +
CC propane-1,3-diamine; Xref=Rhea:RHEA:25972, ChEBI:CHEBI:7386,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57484, ChEBI:CHEBI:58535; EC=1.5.3.15;
CC Evidence={ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + spermine = H2O2 + N-(3-aminopropyl)-4-aminobutanal
CC + propane-1,3-diamine; Xref=Rhea:RHEA:25824, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:45725,
CC ChEBI:CHEBI:57484, ChEBI:CHEBI:58869; EC=1.5.3.14;
CC Evidence={ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermine + O2 = H2O2 + N-(3-acetamidopropyl)-
CC 4-aminobutanal + propane-1,3-diamine; Xref=Rhea:RHEA:25996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57484, ChEBI:CHEBI:58101, ChEBI:CHEBI:58858; EC=1.5.3.14;
CC Evidence={ECO:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16331971, ECO:0000269|Ref.3};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|Ref.3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38 uM for spermine {ECO:0000269|Ref.4};
CC KM=40 uM for spermidine {ECO:0000269|Ref.4};
CC KM=62 uM for N(1)-acetylspermine {ECO:0000269|Ref.4};
CC KM=274 uM for N(1)-acetylspermidine {ECO:0000269|Ref.4};
CC KM=100 uM for dioxygen {ECO:0000269|Ref.4};
CC Vmax=6 umol/min/ug enzyme with spermine as substrate
CC {ECO:0000269|Ref.4};
CC Vmax=70 umol/min/ug enzyme with spermidine as substrate
CC {ECO:0000269|Ref.4};
CC Vmax=21 umol/min/ug enzyme with N(1)-acetylspermine as substrate
CC {ECO:0000269|Ref.4};
CC Vmax=2.5 umol/min/ug enzyme with N(1)-acetylspermidine as substrate
CC {ECO:0000269|Ref.4};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:16331971, ECO:0000269|Ref.4};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:12586904}. Secreted, cell wall
CC {ECO:0000269|PubMed:12586904}.
CC -!- INDUCTION: Induced by light (at protein level) (PubMed:12586904). Down-
CC regulated by auxin (at protein level) (PubMed:12586904).
CC {ECO:0000269|PubMed:12586904}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AJ002204; CAA05249.1; -; mRNA.
DR EMBL; AJ251568; CAC03739.1; -; Genomic_DNA.
DR EMBL; AJ251018; CAC04001.1; -; Genomic_DNA.
DR PIR; T03387; T03387.
DR RefSeq; NP_001105106.1; NM_001111636.1.
DR PDB; 1B37; X-ray; 1.90 A; A/B/C=29-500.
DR PDB; 1B5Q; X-ray; 1.90 A; A/B/C=29-500.
DR PDB; 1H81; X-ray; 2.10 A; A/B/C=29-500.
DR PDB; 1H82; X-ray; 1.90 A; A/B/C=29-500.
DR PDB; 1H83; X-ray; 1.90 A; A/B/C=29-500.
DR PDB; 1H84; X-ray; 2.00 A; A/B/C=29-500.
DR PDB; 1H86; X-ray; 2.00 A; A/B/C=29-500.
DR PDB; 3KPF; X-ray; 2.90 A; A/B=29-500.
DR PDB; 3KU9; X-ray; 3.20 A; A/B=29-500.
DR PDB; 3L1R; X-ray; 3.20 A; A/B=29-500.
DR PDBsum; 1B37; -.
DR PDBsum; 1B5Q; -.
DR PDBsum; 1H81; -.
DR PDBsum; 1H82; -.
DR PDBsum; 1H83; -.
DR PDBsum; 1H84; -.
DR PDBsum; 1H86; -.
DR PDBsum; 3KPF; -.
DR PDBsum; 3KU9; -.
DR PDBsum; 3L1R; -.
DR AlphaFoldDB; O64411; -.
DR SMR; O64411; -.
DR STRING; 4577.GRMZM2G034152_P01; -.
DR BindingDB; O64411; -.
DR ChEMBL; CHEMBL6108; -.
DR Allergome; 955; Zea m PAO.
DR iPTMnet; O64411; -.
DR PaxDb; O64411; -.
DR PRIDE; O64411; -.
DR GeneID; 541983; -.
DR KEGG; zma:541983; -.
DR eggNOG; KOG0029; Eukaryota.
DR OrthoDB; 508351at2759; -.
DR BioCyc; MetaCyc:MON-9461; -.
DR BRENDA; 1.5.3.14; 6752.
DR SABIO-RK; O64411; -.
DR UniPathway; UPA00211; -.
DR EvolutionaryTrace; O64411; -.
DR PRO; PR:O64411; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O64411; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0052898; F:N1-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052893; F:N1-acetylspermine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052897; F:N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052896; F:spermidine oxidase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052900; F:spermine oxidase (propane-1,3-diamine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006598; P:polyamine catabolic process; IDA:UniProtKB.
DR GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoplast; Cell wall; Direct protein sequencing;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:9598979"
FT CHAIN 29..500
FT /note="Polyamine oxidase 1"
FT /id="PRO_0000001712"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT BINDING 63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT BINDING 71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT BINDING 87..88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:3KU9,
FT ECO:0007744|PDB:3L1R"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:3KU9,
FT ECO:0007744|PDB:3L1R"
FT BINDING 265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT BINDING 427
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT BINDING 458
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PDB:3KU9,
FT ECO:0007744|PDB:3L1R"
FT BINDING 467..468
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT DISULFID 485..491
FT /evidence="ECO:0000269|PubMed:10368296,
FT ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q,
FT ECO:0007744|PDB:1H82"
FT MUTAGEN 328
FT /note="K->M: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16331971"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1B5Q"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 134..156
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1B37"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1B37"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:1B37"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:3KU9"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1B37"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3KPF"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 390..404
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:3KU9"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:1B37"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1B37"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 440..447
FT /evidence="ECO:0007829|PDB:1B37"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:1B37"
FT TURN 462..466
FT /evidence="ECO:0007829|PDB:1B37"
FT HELIX 468..488
FT /evidence="ECO:0007829|PDB:1B37"
SQ SEQUENCE 500 AA; 56344 MW; 00BB4BAF7A2E41CB CRC64;
MSSSPSFGLL AVAALLLALS LAQHGSLAAT VGPRVIVVGA GMSGISAAKR LSEAGITDLL
ILEATDHIGG RMHKTNFAGI NVELGANWVE GVNGGKMNPI WPIVNSTLKL RNFRSDFDYL
AQNVYKEDGG VYDEDYVQKR IELADSVEEM GEKLSATLHA SGRDDMSILA MQRLNEHQPN
GPATPVDMVV DYYKFDYEFA EPPRVTSLQN TVPLATFSDF GDDVYFVADQ RGYEAVVYYL
AGQYLKTDDK SGKIVDPRLQ LNKVVREIKY SPGGVTVKTE DNSVYSADYV MVSASLGVLQ
SDLIQFKPKL PTWKVRAIYQ FDMAVYTKIF LKFPRKFWPE GKGREFFLYA SSRRGYYGVW
QEFEKQYPDA NVLLVTVTDE ESRRIEQQSD EQTKAEIMQV LRKMFPGKDV PDATDILVPR
WWSDRFYKGT FSNWPVGVNR YEYDQLRAPV GRVYFTGEHT SEHYNGYVHG AYLSGIDSAE
ILINCAQKKM CKYHVQGKYD
