ID AOXA_RABIT Reviewed; 1334 AA.
AC P80456; Q9XTA9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=Aldehyde oxidase 1 {ECO:0000250|UniProtKB:Q06278};
DE EC=1.2.3.1 {ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775};
DE AltName: Full=Azaheterocycle hydroxylase 1 {ECO:0000305|PubMed:9224775};
DE EC=1.17.3.- {ECO:0000269|PubMed:9224775};
DE AltName: Full=Retinal oxidase {ECO:0000303|PubMed:8305467};
DE AltName: Full=Retinoic acid synthase {ECO:0000303|PubMed:8305467};
GN Name=AOX1 {ECO:0000250|UniProtKB:Q06278}; Synonyms=AO;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 857-884; 891-943 AND
RP 1272-1293, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Japanese white; TISSUE=Liver;
RX PubMed=10190983; DOI=10.1006/abbi.1999.1129;
RA Huang D.-Y., Furukawa A., Ichikawa Y.;
RT "Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit
RT and mouse livers and functional expression of recombinant mouse retinal
RT oxidase cDNA in Escherichia coli.";
RL Arch. Biochem. Biophys. 364:264-272(1999).
RN [2]
RP PROTEIN SEQUENCE OF 203-231 AND 574-597, FUNCTION AS OXIDASE, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=7556219; DOI=10.1111/j.1432-1033.1995.tb20856.x;
RA Turner N.A., Doyle W.A., Ventom A.M., Bray R.C.;
RT "Properties of rabbit liver aldehyde oxidase and the relationship of the
RT enzyme to xanthine oxidase and dehydrogenase.";
RL Eur. J. Biochem. 232:646-657(1995).
RN [3]
RP FUNCTION AS OXIDASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, HOMODIMER, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, REACTION MECHANISM, BLOCKAGE OF N-TERMINUS, AND ACTIVITY
RP REGULATION.
RX PubMed=8305467; DOI=10.1016/0167-4838(94)90039-6;
RA Tsujita M., Tomita S., Miura S., Ichikawa Y.;
RT "Characteristic properties of retinal oxidase (retinoic acid synthase) from
RT rabbit hepatocytes.";
RL Biochim. Biophys. Acta 1204:108-116(1994).
RN [4]
RP FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [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).
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 key role in the metabolism of
CC xenobiotics 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. May be a prominent
CC source of superoxide generation via the one-electron reduction of
CC molecular oxygen. May also catalyze nitric oxide (NO) production via
CC the reduction of nitrite to NO with NADH or aldehyde as electron donor.
CC May play a role in adipogenesis. Cannot use hypoxanthine and all-trans-
CC retinol as substrate. {ECO:0000269|PubMed:10190983,
CC ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467,
CC ECO:0000269|PubMed:9224775}.
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; Evidence={ECO:0000269|PubMed:8305467,
CC ECO:0000269|PubMed:9224775};
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:0000269|PubMed:8305467};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + O2 = all-trans-retinoate + H(+) +
CC H2O2; Xref=Rhea:RHEA:22520, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17898,
CC ChEBI:CHEBI:35291; EC=1.2.3.1; Evidence={ECO:0000269|PubMed:8305467};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:7556219,
CC ECO:0000269|PubMed:8305467};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:7556219, ECO:0000269|PubMed:8305467};
CC -!- ACTIVITY REGULATION: Inhibited by hydralazine and menadione. Not
CC inhibited by BOF-4272 or allopurinol, xanthine dehydrogenase potent
CC inhibitors. In contrast to guinea pig, human and rat, isovanillin is
CC not an inhibitor but a substrate for AOX1 in rabbit.
CC {ECO:0000269|PubMed:8305467, ECO:0000269|PubMed:9224775}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 uM for all-trans-retinal {ECO:0000269|PubMed:8305467};
CC KM=13 uM for 9-cis-retinal {ECO:0000269|PubMed:8305467};
CC KM=0.9 mM for 13-cis-retinal {ECO:0000269|PubMed:8305467};
CC KM=0.11 mM for N-methylnicotinamide {ECO:0000269|PubMed:8305467};
CC KM=94.7 uM for O(2) {ECO:0000269|PubMed:8305467};
CC KM=0.44 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:9224775};
CC KM=45 uM for isovanillin (at 37 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:9224775};
CC Vmax=192 nmol/min/mg enzyme with all-trans-retinal as substrate
CC {ECO:0000269|PubMed:8305467};
CC Vmax=57 nmol/min/mg enzyme with 9-cis-retinal as substrate
CC {ECO:0000269|PubMed:8305467};
CC Vmax=105 nmol/min/mg enzyme with 13-cis-retinal as substrate
CC {ECO:0000269|PubMed:8305467};
CC Vmax=267 nmol/min/mg enzyme with N-methylnicotinamide as substrate
CC {ECO:0000269|PubMed:8305467};
CC Vmax=114 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate
CC {ECO:0000269|PubMed:9224775};
CC Vmax=211 nmol/min/mg enzyme with isovanillin as substrate
CC {ECO:0000269|PubMed:9224775};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8305467}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8305467}.
CC -!- TISSUE SPECIFICITY: Very high expression in liver and lung. High
CC expression in kidney, pancreas, brain stem and spinal cord. Moderate
CC expression in heart, testis, eye, cerebral cortex and cerebellum. Low
CC expression in stomach and muscle. {ECO:0000269|PubMed:10190983,
CC ECO:0000269|PubMed:8305467}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: The reaction follows an ordered Bi-Bi kinetic mechanism.
CC During retinal oxidation, incorporates the oxygen of water into
CC retinoate, but not that of molecular oxygen (PubMed:8305467).
CC {ECO:0000305|PubMed:8305467}.
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 ---------------------------------------------------------------------------
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; AB009345; BAA81726.1; -; mRNA.
DR RefSeq; NP_001075459.1; NM_001081990.1.
DR AlphaFoldDB; P80456; -.
DR SMR; P80456; -.
DR STRING; 9986.ENSOCUP00000046241; -.
DR BindingDB; P80456; -.
DR ChEMBL; CHEMBL1641356; -.
DR PaxDb; 9986-ENSOCUP00000012025; -.
DR GeneID; 100008601; -.
DR KEGG; ocu:100008601; -.
DR CTD; 316; -.
DR eggNOG; KOG0430; Eukaryota.
DR InParanoid; P80456; -.
DR OrthoDB; 5485853at2759; -.
DR BRENDA; 1.2.3.1; 1749.
DR SABIO-RK; P80456; -.
DR PRO; PR:P80456; -.
DR Proteomes; UP000001811; 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; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
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: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; 3.30.465.10; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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-like.
DR InterPro; IPR014313; Aldehyde_oxidase.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
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 NCBIfam; TIGR02969; mam_aldehyde_ox; 1.
DR PANTHER; PTHR11908:SF86; ALDEHYDE OXIDASE; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 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 Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_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; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 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; Direct protein sequencing; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Lipid metabolism; Metal-binding; Molybdenum; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1334
FT /note="Aldehyde oxidase 1"
FT /id="PRO_0000166107"
FT DOMAIN 5..92
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 236..421
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1266
FT /note="Proton acceptor; for azaheterocycle hydroxylase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:O54754"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 74
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 113
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 114
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 117
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 149
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 151
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 151
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 264..271
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 345
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 367
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 411
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 802..803
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1043
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1084..1087
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1199
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1264
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
SQ SEQUENCE 1334 AA; 147138 MW; 0747A0569C2C062A CRC64;
MEPAPELLFY VNGRKVVEKQ VDPETMLLPY LRKKLRLTGT KYGCGGGGCG ACTVMISRYN
RVTKKIRHYP VNACLTPICS LYGAAVTTVE GIGSTTTRLH PVQERIAKFH GTQCGFCTPG
MVMSMYALLR NHPEPTLDQL ADALGGNLCR CTGYRPIIEA YKTFCKTSDC CQNKENGFCC
LDQGINGLPE VEEENQTRPN LFSEEEYLPL DPTQELIFPP ELMTMAEKQP QRTRVFSGER
MMWISPVTLK ALLEAKSTYP QAPVVMGNTS VGPGVKFKGI FHPVIISPDS IEELNVVSHT
HSGLTLGAGL SLAQVKDILA DVVQKVPEEN AQTYRALLKH LGTLAGSQIR NMASLGGHII
SRHLDSDLNP LLAVGNCTLN VLSKEGERQI PLDEQFLSRC PEADLKPQEI LASVHIPYSR
KWEFVLAFRQ AQRKQNALAI VNSGMRVFFG EGDGIIRELA ISYGGVGPTI ICAKNSCQKL
IGRSWNEEML DTACRLILDE VSLPGSAPGG KVEFKRTLII SFLFKFYLEV SQILKRMAPG
LSPHLADKYE SALQDLHARY SWSTLKDQDV DARQLSQDPI GHPVMHLSGV KHATGEAIYL
DDMPAVDQEL FMAFVTSPRA HAKIVSTDLL EALSLPGVVD IVTAEHLQDG NTFYTEKLLA
ADEVLCVGQL VCAVIAESEV QAKQAAKQVK IVYEDLEPVI LSIEEAIEQK SFFEPERKLE
YGNVDEAFKV VDQILEGEIH MGGQEHFYME TQSVLVVPKG EDQEMDVYAS TQFPKYIQDM
VAAVLKLPVN KVMCHVKRVG GAFGGKVFKA SIMAAIAAFA ANKHGRAVRC ILERGEDMLI
TGGRHPYLGK YKAGFMNDGR IVALDVEHYS NGGCSLDESL LVIEMGLLKM ENAYKFPNLR
CRGWACRTNL PSNTAFRGFG FPQAGLITEC CITEVAAKCG LSPEKVRAIN FYKEIDQTPY
KQEINAKNLT QCWNECLAKS SYFQRKVAVE KFNAENYWKQ RGLAIIPFKY PRGLGSVAYG
QAAALVHVYL DGSVLVTHGG IEMGQGVHTK MIQVVSRELK MPMSNVHLRG TSTETVPNTN
ASGGSVVADL NGLAVKDACQ TLLKRLEPII NKNPQGTWKE WAQAAFDKSI SLSATGYFRG
YDSNIDWDKG EGHPFEYFVY GAACSEVEID CLTGDHKTIR TDIVMDVGYS INPALDIGQV
EGAFIQGMGL YTIEELHYSP QGILYSRGPN QYKIPAICDI PAELNVTFLP PSEKSNTLYS
SKGLGESGVF MGCSVFFAIR EAVCAARQAR GLSAPWKLSS PLTPEKIRMA CEDKFTKMIP
RDKPGSYVPW NVPV
//
