FRDA_SHEFR
ID FRDA_SHEFR Reviewed; 571 AA.
AC P0C278; Q02469; Q9X969;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Fumarate reductase flavoprotein subunit;
DE EC=1.3.5.4;
DE AltName: Full=Flavocytochrome c;
DE AltName: Full=Flavocytochrome c3;
DE Short=Fcc3;
GN Name=fccA; Synonyms=fcc3;
OS Shewanella frigidimarina.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=56812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-571, AND CRYSTALLIZATION.
RC STRAIN=ACAM591;
RX PubMed=10479620; DOI=10.1006/jsbi.1999.4139;
RA Pealing S.L., Lysek D.A., Taylor P., Alexeev D., Reid G.A., Chapman S.K.,
RA Walkinshaw M.D.;
RT "Crystallization and preliminary X-ray analysis of flavocytochrome c(3),
RT the fumarate reductase from Shewanella frigidimarina.";
RL J. Struct. Biol. 127:76-78(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10581550; DOI=10.1038/70045;
RA Taylor P., Pealing S.L., Reid G.A., Chapman S.K., Walkinshaw M.D.;
RT "Structural and mechanistic mapping of a unique fumarate reductase.";
RL Nat. Struct. Biol. 6:1108-1112(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-365 AND ALA-504 IN
RP COMPLEX WITH FAD; FUMARATE AND HEMES, MUTAGENESIS OF HIS-365; ARG-402 AND
RP HIS-504, AND ACTIVE SITE.
RX PubMed=10978153; DOI=10.1021/bi000871l;
RA Doherty M.K., Pealing S.L., Miles C.S., Moysey R., Taylor P.,
RA Walkinshaw M.D., Reid G.A., Chapman S.K.;
RT "Identification of the active site acid/base catalyst in a bacterial
RT fumarate reductase: a kinetic and crystallographic study.";
RL Biochemistry 39:10695-10701(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-402; LYS-402 AND
RP TYR-402, MUTAGENESIS OF ARG-402, AND ENZYME KINETICS.
RX PubMed=11591148; DOI=10.1021/bi011360h;
RA Mowat C.G., Moysey R., Miles C.S., Leys D., Doherty M.K., Taylor P.,
RA Walkinshaw M.D., Reid G.A., Chapman S.K.;
RT "Kinetic and crystallographic analysis of the key active site acid/base
RT arginine in a soluble fumarate reductase.";
RL Biochemistry 40:12292-12298(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-505 AND TYR-505, AND
RP CHARACTERIZATION.
RX PubMed=12093271; DOI=10.1021/bi020155e;
RA Pankhurst K.L., Mowat C.G., Miles C.S., Leys D., Walkinshaw M.D.,
RA Reid G.A., Chapman S.K.;
RT "Role of His505 in the soluble fumarate reductase from Shewanella
RT frigidimarina.";
RL Biochemistry 41:8551-8556(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS PHE-363 AND
RP PHE-363/ALA-402, CHARACTERIZATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12356299; DOI=10.1021/bi0203177;
RA Mowat C.G., Pankhurst K.L., Miles C.S., Leys D., Walkinshaw M.D.,
RA Reid G.A., Chapman S.K.;
RT "Engineering water to act as an active site acid catalyst in a soluble
RT fumarate reductase.";
RL Biochemistry 41:11990-11996(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ALA-61 AND MET-61 IN
RP COMPLEXES WITH HEME; SUBSTRATE AND FAD, MASS SPECTROMETRY, AND MUTAGENESIS
RP OF HIS-61.
RX PubMed=14609326; DOI=10.1021/bi030159z;
RA Rothery E.L., Mowat C.G., Miles C.S., Walkinshaw M.D., Reid G.A.,
RA Chapman S.K.;
RT "Histidine 61: an important heme ligand in the soluble fumarate reductase
RT from Shewanella frigidimarina.";
RL Biochemistry 42:13160-13169(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANT CYS-251/CYS430.
RX PubMed=15109257; DOI=10.1021/bi030261w;
RA Rothery E.L., Mowat C.G., Miles C.S., Mott S., Walkinshaw M.D., Reid G.A.,
RA Chapman S.K.;
RT "Probing domain mobility in a flavocytochrome.";
RL Biochemistry 43:4983-4989(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ASP-378 AND MET-381,
RP MUTAGENESIS OF GLU-378 AND ARG-381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16699170; DOI=10.1074/jbc.m603077200;
RA Pankhurst K.L., Mowat C.G., Rothery E.L., Hudson J.M., Jones A.K.,
RA Miles C.S., Walkinshaw M.D., Armstrong F.A., Reid G.A., Chapman S.K.;
RT "A proton delivery pathway in the soluble fumarate reductase from
RT Shewanella frigidimarina.";
RL J. Biol. Chem. 281:20589-20597(2006).
CC -!- FUNCTION: Catalyzes fumarate reduction using artificial electron donors
CC such as methyl viologen. The physiological reductant is unknown, but
CC evidence indicates that flavocytochrome c participates in electron
CC transfer from formate to fumarate and possibly also to trimethylamine
CC oxide (TMAO). This enzyme is essentially unidirectional.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10978153}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By anaerobiosis and fumarate.
CC -!- MASS SPECTROMETRY: Mass=63033; Mass_error=10; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:14609326};
CC -!- SIMILARITY: In the C-terminal section; belongs to the FAD-dependent
CC oxidoreductase 2 family. FRD/SDH subfamily. {ECO:0000305}.
CC -!- CAUTION: The N-terminal sequence has been extracted from PDB entry
CC 1LJ1. {ECO:0000305}.
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 EMBL; AJ132010; CAB38558.1; -; Genomic_DNA.
DR PDB; 1E39; X-ray; 1.80 A; A=1-571.
DR PDB; 1JRX; X-ray; 2.00 A; A/B=1-571.
DR PDB; 1JRY; X-ray; 2.00 A; A/B=1-571.
DR PDB; 1JRZ; X-ray; 2.00 A; A/B=1-571.
DR PDB; 1KSS; X-ray; 1.80 A; A=1-571.
DR PDB; 1KSU; X-ray; 2.00 A; A/B=1-571.
DR PDB; 1LJ1; X-ray; 2.00 A; A/B=1-571.
DR PDB; 1M64; X-ray; 1.80 A; A/B=1-571.
DR PDB; 1P2E; X-ray; 2.20 A; A=1-571.
DR PDB; 1P2H; X-ray; 2.10 A; A=1-571.
DR PDB; 1Q9I; X-ray; 1.60 A; A=1-571.
DR PDB; 1QJD; X-ray; 1.80 A; A=1-571.
DR PDB; 1Y0P; X-ray; 1.50 A; A=1-571.
DR PDB; 2B7R; X-ray; 1.70 A; A=1-571.
DR PDB; 2B7S; X-ray; 2.12 A; A=1-571.
DR PDBsum; 1E39; -.
DR PDBsum; 1JRX; -.
DR PDBsum; 1JRY; -.
DR PDBsum; 1JRZ; -.
DR PDBsum; 1KSS; -.
DR PDBsum; 1KSU; -.
DR PDBsum; 1LJ1; -.
DR PDBsum; 1M64; -.
DR PDBsum; 1P2E; -.
DR PDBsum; 1P2H; -.
DR PDBsum; 1Q9I; -.
DR PDBsum; 1QJD; -.
DR PDBsum; 1Y0P; -.
DR PDBsum; 2B7R; -.
DR PDBsum; 2B7S; -.
DR AlphaFoldDB; P0C278; -.
DR SMR; P0C278; -.
DR DrugBank; DB04734; Citraconic acid.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB01677; Fumaric acid.
DR DrugBank; DB03343; Malate Like Intermediate.
DR SABIO-RK; P0C278; -.
DR EvolutionaryTrace; P0C278; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; NAS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; NAS:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019645; P:anaerobic electron transport chain; NAS:UniProtKB.
DR GO; GO:0009061; P:anaerobic respiration; NAS:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR012286; Tetrahaem_cytochrome.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF14537; Cytochrom_c3_2; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01813; flavo_cyto_c; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; FAD; Flavoprotein; Heme; Iron;
KW Metal-binding; Oxidoreductase; Periplasm; Transport.
FT CHAIN 1..571
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000010344"
FT REGION 118..571
FT /note="Flavoprotein-like"
FT ACT_SITE 402
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:10978153"
FT BINDING 8
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 14
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 17
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 18
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 36
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 39
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 40
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 58
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 61
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 68
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 71
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 72
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 75
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 82
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 85
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 86
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 132..143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10978153"
FT BINDING 156..157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10978153"
FT BINDING 164..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10978153"
FT BINDING 169..171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10978153"
FT BINDING 377..378
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT BINDING 504
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT BINDING 544
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT BINDING 549..550
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10978153"
FT MUTAGEN 61
FT /note="H->A: Reduces catalytic activity 10-fold. Reduces
FT affinity for fumarate."
FT /evidence="ECO:0000269|PubMed:14609326"
FT MUTAGEN 61
FT /note="H->M: Reduces catalytic activity 5-fold. Reduces
FT affinity for fumarate."
FT /evidence="ECO:0000269|PubMed:14609326"
FT MUTAGEN 365
FT /note="H->A: Reduces catalytic activity by over 75%."
FT /evidence="ECO:0000269|PubMed:10978153"
FT MUTAGEN 378
FT /note="E->D: Strongly reduced affinity for substrate.
FT Reduces activity 10000-fold."
FT /evidence="ECO:0000269|PubMed:16699170"
FT MUTAGEN 381
FT /note="R->M: Strongly reduced catalytic activity. No effect
FT on substrate affinity."
FT /evidence="ECO:0000269|PubMed:16699170"
FT MUTAGEN 402
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10978153,
FT ECO:0000269|PubMed:11591148"
FT MUTAGEN 402
FT /note="R->K,Y: Reduces activity 10000-fold."
FT /evidence="ECO:0000269|PubMed:10978153,
FT ECO:0000269|PubMed:11591148"
FT MUTAGEN 504
FT /note="H->A: Reduces catalytic activity by over 64%."
FT /evidence="ECO:0000269|PubMed:10978153"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:1Y0P"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1P2H"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:1Y0P"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 206..225
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1Y0P"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 253..267
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 271..283
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:1Y0P"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1JRX"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1P2H"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:1Y0P"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1P2H"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 402..410
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 432..438
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 447..454
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 458..474
FT /evidence="ECO:0007829|PDB:1Y0P"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 494..506
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 525..531
FT /evidence="ECO:0007829|PDB:1Y0P"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:1Y0P"
FT HELIX 548..567
FT /evidence="ECO:0007829|PDB:1Y0P"
SQ SEQUENCE 571 AA; 60621 MW; D2E4FC43C9A6484C CRC64;
ADNLAEFHVQ NQECDSCHTP DGELSNDSLT YENTQCVSCH GTLEEVAETT KHEHYNAHAS
HFPGEVACTS CHSAHEKSMV YCDSCHSFDF NMPYAKKWQR DEPTIAELAK DKSERQAALA
SAPHDTVDVV VVGSGGAGFS AAISATDSGA KVILIEKEPV IGGNAKLAAG GMNAAWTDQQ
KAKKITDSPE LMFEDTMKGG QNINDPALVK VLSSHSKDSV DWMTAMGADL TDVGMMGGAS
VNRAHRPTGG AGVGAHVVQV LYDNAVKRNI DLRMNTRGIE VLKDDKGTVK GILVKGMYKG
YYWVKADAVI LATGGFAKNN ERVAKLDPSL KGFISTNQPG AVGDGLDVAE NAGGALKDMQ
YIQAHPTLSV KGGVMVTEAV RGNGAILVNR EGKRFVNEIT TRDKASAAIL AQTGKSAYLI
FDDSVRKSLS KIDKYIGLGV APTADSLVKL GKMEGIDGKA LTETVARYNS LVSSGKDTDF
ERPNLPRALN EGNYYAIEVT PGVHHTMGGV MIDTKAEVMN AKKQVIPGLY GAGEVTGGVH
GANRLGGNAI SDIITFGRLA GEEAAKYSKK N
