AOXA_RAT
ID AOXA_RAT Reviewed; 1333 AA.
AC Q9Z0U5; Q9R240;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Aldehyde oxidase 1 {ECO:0000312|RGD:620528};
DE EC=1.2.3.1 {ECO:0000250|UniProtKB:O54754};
DE AltName: Full=Azaheterocycle hydroxylase 1 {ECO:0000305|PubMed:9224775};
DE EC=1.17.3.- {ECO:0000269|PubMed:9224775};
GN Name=Aox1 {ECO:0000312|RGD:620528}; Synonyms=Ao;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, BLOCKAGE OF
RP N-TERMINUS, HOMODIMER, AND VARIANTS 119-ALA-ARG-120; THR-649; LEU-1276 AND
RP ARG-1315.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9920943; DOI=10.1074/jbc.274.6.3878;
RA Wright R.M., Clayton D.A., Riley M.G., McManaman J.L., Repine J.E.;
RT "cDNA cloning, sequencing, and characterization of male and female rat
RT liver aldehyde oxidase (rAOX1). Differences in redox status may distinguish
RT male and female forms of hepatic APX.";
RL J. Biol. Chem. 274:3878-3886(1999).
RN [2]
RP FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND KINETIC PARAMETERS.
RX PubMed=9224775;
RA Rashidi M.R., Smith J.A., Clarke S.E., Beedham C.;
RT "In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde
RT oxidase from human, guinea pig, rabbit, and rat liver.";
RL Drug Metab. Dispos. 25:805-813(1997).
RN [3]
RP FUNCTION IN SUPEROXIDE PRODUCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, HOMODIMER, AND COFACTOR.
RX PubMed=17353002; DOI=10.1016/j.abb.2006.12.032;
RA Kundu T.K., Hille R., Velayutham M., Zweier J.L.;
RT "Characterization of superoxide production from aldehyde oxidase: an
RT important source of oxidants in biological tissues.";
RL Arch. Biochem. Biophys. 460:113-121(2007).
RN [4]
RP FUNCTION IN NITRIC OXIDE PRODUCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RX PubMed=19801639; DOI=10.1074/jbc.m109.019125;
RA Li H., Kundu T.K., Zweier J.L.;
RT "Characterization of the magnitude and mechanism of aldehyde oxidase-
RT mediated nitric oxide production from nitrite.";
RL J. Biol. Chem. 284:33850-33858(2009).
RN [5]
RP IDENTIFICATION OF PARALOGS.
RX PubMed=23263164; DOI=10.1007/s00018-012-1229-5;
RA Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., Perretta G.,
RA Terao M., Garattini E.;
RT "Structure and evolution of vertebrate aldehyde oxidases: from gene
RT duplication to gene suppression.";
RL Cell. Mol. Life Sci. 70:1807-1830(2013).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=23282065; DOI=10.3109/00498254.2012.755228;
RA Hamzeh-Mivehroud M., Rahmani S., Rashidi M.R., Hosseinpour Feizi M.A.,
RA Dastmalchi S.;
RT "Structure-based investigation of rat aldehyde oxidase inhibition by
RT flavonoids.";
RL Xenobiotica 43:661-670(2013).
CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic
CC azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium
CC and phthalazine, as well as aldehydes, such as benzaldehyde, retinal,
CC pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics
CC and drugs containing aromatic azaheterocyclic substituents.
CC Participates in the bioactivation of prodrugs such as famciclovir,
CC catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir,
CC which is a potent antiviral agent. Is probably involved in the
CC regulation of reactive oxygen species homeostasis. Is a prominent
CC source of superoxide generation via the one-electron reduction of
CC molecular oxygen. Also catalyzes nitric oxide (NO) production; under
CC anaerobic conditions, reduces nitrite to NO with NADH or aldehyde as
CC electron donor, but under aerobic conditions, NADH is the preferred
CC substrate. These reactions may be catalyzed by several isozymes. May
CC play a role in adipogenesis. {ECO:0000269|PubMed:17353002,
CC ECO:0000269|PubMed:19801639, ECO:0000269|PubMed:23282065,
CC ECO:0000269|PubMed:9224775, ECO:0000269|PubMed:9920943}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067; EC=1.2.3.1;
CC Evidence={ECO:0000250|UniProtKB:O54754};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + retinal = H(+) + H2O2 + retinoate;
CC Xref=Rhea:RHEA:56736, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240; Evidence={ECO:0000250|UniProtKB:O54754};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:17353002};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000269|PubMed:17353002};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17353002};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17353002};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:O54754};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:O54754};
CC -!- ACTIVITY REGULATION: Inhibited by menadione and isovanillin. Not
CC inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor.
CC Inhibited by the flavonoids quercetin, myricetin and genistein. Nitric
CC oxide generation is inhibited by raloxifene and competitively inhibited
CC by an increase in oxygen levels. {ECO:0000269|PubMed:19801639,
CC ECO:0000269|PubMed:23282065, ECO:0000269|PubMed:9224775}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.37 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:9224775};
CC KM=0.08 mM for famciclovir (at 37 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:9224775};
CC KM=3.0 mM for nitrite {ECO:0000269|PubMed:19801639};
CC KM=24 uM for NADH {ECO:0000269|PubMed:19801639};
CC KM=9.6 uM for 4-(dimethylamino)cinnamaldehyde
CC {ECO:0000269|PubMed:19801639};
CC Vmax=26 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate
CC {ECO:0000269|PubMed:9224775};
CC Vmax=41 nmol/min/mg enzyme with famciclovir as substrate
CC {ECO:0000269|PubMed:9224775};
CC Vmax=0.85 umol/sec/mg enzyme for nitrite reduction with NADH as
CC electron donor {ECO:0000269|PubMed:19801639};
CC Vmax=1.35 umol/sec/mg enzyme for nitrite reduction with 4-
CC (dimethylamino)cinnamaldehyde as electron donor
CC {ECO:0000269|PubMed:19801639};
CC pH dependence:
CC Optimum pH is 6.0 for nitrite oxide generation. Activity decreases
CC below pH 5.0 and above pH 8.0 (PubMed:19801639).
CC {ECO:0000269|PubMed:19801639};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17353002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17353002}.
CC -!- TISSUE SPECIFICITY: Expression in liver (at protein level). Also
CC detected in heart, lung, spleen and kidney.
CC {ECO:0000269|PubMed:17353002, ECO:0000269|PubMed:9920943}.
CC -!- PTM: The N-terminus is blocked.
CC -!- POLYMORPHISM: The sequence variants between males and females could be
CC due to differences between individual animals, reflect gender
CC differences or arise from technical problems (PubMed:9920943). The
CC sequence shown here is that of a Sprague-Dawley female.
CC {ECO:0000269|PubMed:9920943}.
CC -!- MISCELLANEOUS: Male and female rats possess kinetically distinct forms
CC which may be due to differences in redox states.
CC {ECO:0000305|PubMed:9920943}.
CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase
CC ancestral precursor via a series of gene duplication and
CC suppression/deletion events. Different animal species contain a
CC different complement of AOX genes encoding an equivalent number of AOX
CC isoenzymes. In mammals, the two extremes are represented by certain
CC rodents such as mice and rats, which are endowed with 4 AOX genes, and
CC by humans, whose genome is characterized by a single active gene
CC (PubMed:23263164). {ECO:0000305|PubMed:23263164}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: The experimental design does not allow to distinguish AOX1
CC from AOX3 in rat liver as the effector of the superoxide and nitric
CC oxide production (PubMed:17353002 and PubMed:19801639). {ECO:0000305}.
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DR EMBL; AF110477; AAD16999.1; -; mRNA.
DR EMBL; AF110478; AAD17000.1; -; mRNA.
DR RefSeq; NP_062236.2; NM_019363.3.
DR AlphaFoldDB; Q9Z0U5; -.
DR SMR; Q9Z0U5; -.
DR STRING; 10116.ENSRNOP00000059651; -.
DR BindingDB; Q9Z0U5; -.
DR ChEMBL; CHEMBL1641355; -.
DR iPTMnet; Q9Z0U5; -.
DR PhosphoSitePlus; Q9Z0U5; -.
DR PaxDb; Q9Z0U5; -.
DR PRIDE; Q9Z0U5; -.
DR GeneID; 54349; -.
DR KEGG; rno:54349; -.
DR UCSC; RGD:620528; rat.
DR CTD; 316; -.
DR RGD; 620528; Aox1.
DR eggNOG; KOG0430; Eukaryota.
DR InParanoid; Q9Z0U5; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q9Z0U5; -.
DR BRENDA; 1.2.3.1; 5301.
DR Reactome; R-RNO-964975; Vitamins B6 activation to pyridoxal phosphate.
DR SABIO-RK; Q9Z0U5; -.
DR PRO; PR:Q9Z0U5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:RGD.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR014313; Aldehyde_oxidase.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Lipid metabolism;
KW Metal-binding; Molybdenum; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1333
FT /note="Aldehyde oxidase 1"
FT /id="PRO_0000166108"
FT DOMAIN 4..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 235..420
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1265
FT /note="Proton acceptor; for azaheterocycle hydroxylase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:O54754"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 112
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 148
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 150
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 263..270
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 353
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 801..802
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1042
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1083..1086
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1198
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1263
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT VARIANT 119..120
FT /note="GM -> AR (in Sprague-Dawley males; could be
FT unrelated to gender)"
FT VARIANT 649
FT /note="A -> T (in Sprague-Dawley males; could be unrelated
FT to gender)"
FT /evidence="ECO:0000269|PubMed:9920943"
FT VARIANT 1276
FT /note="F -> L (in Sprague-Dawley males; could be unrelated
FT to gender)"
FT /evidence="ECO:0000269|PubMed:9920943"
FT VARIANT 1315
FT /note="T -> R (in Sprague-Dawley males; could be unrelated
FT to gender)"
FT /evidence="ECO:0000269|PubMed:9920943"
SQ SEQUENCE 1333 AA; 146921 MW; 516B6CE395EB05C8 CRC64;
MDPPQLLFYV NGQKVVENNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP
STKSIRHHPV NACLTPICSL YGTAVTTVEG IGNTRTRLHP VQERIAKCHS TQCGFCTPGM
VMSMYALLRN HPEPSLDQLT DALGGNLCRC TGYRPIIDAC KTFCRASGCC ESKENGVCCL
DQGINGSAEF QEGDETSPEL FSEKEFQPLD PTQELIFPPE LMRIAEKQPP KTRVFYSNRM
TWISPVTLEE LVEAKFKYPG APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELSIINQTG
DGLTLGAGLS LDQVKDILTD VVQKLPEETT QTYRALLKHL RTLAGSQIRN MASLGGHIVS
RHLDSDLNPL LAVGNCTLNL LSKDGKRQIP LSEQFLRKCP DSDLKPQEVL VSVNIPCSRK
WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIKELSI LYGGVGPTTI GAKNSCQKLI
GRPWNEEMLD TACRLVLDEV TLAGSAPGGK VEFKRTLIIS FLFKFYLEVL QGLKREDPGH
YPSLTNNYES ALEDLHSKHH WRTLTHQNVD SMQLPQDPIG RPIMHLSGIK HATGEAIYCD
DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQDAT TFGTETLLAT
DKVHCVGQLV CAVIADSETR AKQAAKHVKV VYRDLEPLIL TIEEAIQHKS FFESERKLEC
GNVDEAFKIA DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKHIQDIV
AATLKLSVNK VMCHVRRVGG AFGGKVGKTS IMAAITAFAA SKHGRAVRCT LERGEDMLIT
GGRHPYLGKY KVGFMRDGRI VALDVEHYCN GGSSLDESLW VIEMGLLKMD NAYKFPNLRC
RGWACRTNLP SHTALRGFGF PQAGLVTEAC VTEVAIRCGL SPEQVRTINM YKQIDNTHYK
QEFSAKTLFE CWRECMAKCS YSERKTAVGK FNAENSWKKR GMAVIPLKFP VGVGSVAMGQ
AAALVHIYLD GSALVSHGGI EMGQGVHTKM IQVVSRELKM PMSSVHLRGT STETVPNTNA
SGGSVVADLN GLAVKDACQT LLKRLEPIIS KNPQGTWKDW AQTAFDQSVS LSAVGYFRGY
ESNINWEKGE GHPFEYFVYG AACSEVEIDC LTGDHKNIRT DIVMDVGHSI NPALDIGQVE
GAFIQGMGLY TIEELSYSPQ GILYSRGPNQ YKIPAICDIP TEMHISFLPP SEHSNTLYSS
KGLGESGVFL GCSVFFAIHD AVRAARQERG ISGPWKLTSP LTPEKIRMAC EDKFTKMIPR
DEPGSYVPWN IPV
