AFLD_ASPPU
ID AFLD_ASPPU Reviewed; 271 AA.
AC Q00278; A0A0F0I0S7; Q6UEH1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Norsolorinic acid ketoreductase {ECO:0000303|PubMed:10584035};
DE EC=1.1.1.349 {ECO:0000269|PubMed:10584035};
DE AltName: Full=Aflatoxin biosynthesis ketoreductase nor-1 {ECO:0000305};
DE AltName: Full=Aflatoxin biosynthesis protein D {ECO:0000303|PubMed:15006741};
DE AltName: Full=Short chain dehydrogenase aflD {ECO:0000305};
GN Name=aflD {ECO:0000303|PubMed:15006741};
GN Synonyms=nor-1 {ECO:0000303|PubMed:7993094}; ORFNames=P875_00052988;
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=7993094; DOI=10.1128/aem.60.11.4078-4085.1994;
RA Trail F., Chang P.-K., Cary J., Linz J.E.;
RT "Structural and functional analysis of the nor-1 gene involved in the
RT biosynthesis of aflatoxins by Aspergillus parasiticus.";
RL Appl. Environ. Microbiol. 60:4078-4085(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15094053; DOI=10.1016/s0014-5793(04)00327-8;
RA Yu J., Bhatnagar D., Cleveland T.E.;
RT "Completed sequence of aflatoxin pathway gene cluster in Aspergillus
RT parasiticus.";
RL FEBS Lett. 564:126-130(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=1339261; DOI=10.1128/aem.58.11.3527-3537.1992;
RA Skory C.D., Chang P.K., Cary J., Linz J.E.;
RT "Isolation and characterization of a gene from Aspergillus parasiticus
RT associated with the conversion of versicolorin A to sterigmatocystin in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 58:3527-3537(1992).
RN [5]
RP FUNCTION.
RX PubMed=8434913; DOI=10.1128/aem.59.2.479-484.1993;
RA Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
RA Ullah A.H.J.;
RT "Purification of a 40-kilodalton methyltransferase active in the aflatoxin
RT biosynthetic pathway.";
RL Appl. Environ. Microbiol. 59:479-484(1993).
RN [6]
RP FUNCTION.
RX PubMed=8368836; DOI=10.1128/aem.59.8.2486-2492.1993;
RA Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
RT "Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic
RT acid to averufin.";
RL Appl. Environ. Microbiol. 59:2486-2492(1993).
RN [7]
RP FUNCTION.
RX PubMed=8368837; DOI=10.1128/aem.59.8.2493-2500.1993;
RA Yabe K., Hamasaki T.;
RT "Stereochemistry during aflatoxin biosynthesis: cyclase reaction in the
RT conversion of versiconal to versicolorin B and racemization of versiconal
RT hemiacetal acetate.";
RL Appl. Environ. Microbiol. 59:2493-2500(1993).
RN [8]
RP FUNCTION.
RX PubMed=10543813; DOI=10.1128/aem.65.11.4987-4994.1999;
RA Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
RT "Cloning and characterization of the O-methyltransferase I gene (dmtA) from
RT Aspergillus parasiticus associated with the conversions of
RT demethylsterigmatocystin to sterigmatocystin and
RT dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in aflatoxin
RT biosynthesis.";
RL Appl. Environ. Microbiol. 65:4987-4994(1999).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10584035; DOI=10.1128/aem.65.12.5639-5641.1999;
RA Zhou R., Linz J.E.;
RT "Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
RT Aspergillus parasiticus.";
RL Appl. Environ. Microbiol. 65:5639-5641(1999).
RN [10]
RP FUNCTION.
RX PubMed=11055914; DOI=10.1128/aem.66.11.4715-4719.2000;
RA Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G., Bhatnagar D.,
RA Cleveland T.E.;
RT "adhA in Aspergillus parasiticus is involved in conversion of 5'-
RT hydroxyaverantin to averufin.";
RL Appl. Environ. Microbiol. 66:4715-4719(2000).
RN [11]
RP FUNCTION.
RX PubMed=16256699; DOI=10.1006/bioo.2001.1216;
RA Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
RA Townsend C.A.;
RT "Hexanoate synthase, a specialized type I fatty acid synthase in aflatoxin
RT B1 biosynthesis.";
RL Bioorg. Chem. 29:293-307(2001).
RN [12]
RP FUNCTION.
RX PubMed=11996570; DOI=10.1021/ja012185v;
RA Udwary D.W., Casillas L.K., Townsend C.A.;
RT "Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
RT cytochrome P-450 in the final step of aflatoxin biosynthesis.";
RL J. Am. Chem. Soc. 124:5294-5303(2002).
RN [13]
RP REVIEW, FUNCTION, PATHWAY, AND NOMENCLATURE.
RX PubMed=15006741; DOI=10.1128/aem.70.3.1253-1262.2004;
RA Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D., Cleveland T.E.,
RA Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
RT "Clustered pathway genes in aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 70:1253-1262(2004).
RN [14]
RP FUNCTION.
RX PubMed=15528514; DOI=10.1128/aem.70.11.6518-6524.2004;
RA Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
RT "Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
RT formation.";
RL Appl. Environ. Microbiol. 70:6518-6524(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=14722624; DOI=10.1007/s00203-003-0643-3;
RA Lee L.W., Chiou C.H., Klomparens K.L., Cary J.W., Linz J.E.;
RT "Subcellular localization of aflatoxin biosynthetic enzymes Nor-1, Ver-1,
RT and OmtA in time-dependent fractionated colonies of Aspergillus
RT parasiticus.";
RL Arch. Microbiol. 181:204-214(2004).
RN [16]
RP INDUCTION.
RX PubMed=15054098; DOI=10.1074/jbc.m400075200;
RA Roze L.V., Miller M.J., Rarick M., Mahanti N., Linz J.E.;
RT "A novel cAMP-response element, CRE1, modulates expression of nor-1 in
RT Aspergillus parasiticus.";
RL J. Biol. Chem. 279:27428-27439(2004).
RN [17]
RP INDUCTION.
RX PubMed=15746358; DOI=10.1128/aem.71.3.1539-1545.2005;
RA Miller M.J., Roze L.V., Trail F., Linz J.E.;
RT "Role of cis-acting sites NorL, a TATA box, and AflR1 in nor-1
RT transcriptional activation in Aspergillus parasiticus.";
RL Appl. Environ. Microbiol. 71:1539-1545(2005).
RN [18]
RP FUNCTION.
RX PubMed=15932995; DOI=10.1128/aem.71.6.2999-3006.2005;
RA Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K., Nakajima H.;
RT "Aspergillus parasiticus cyclase catalyzes two dehydration steps in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 71:2999-3006(2005).
RN [19]
RP FUNCTION.
RX PubMed=16332900; DOI=10.1128/aem.71.12.8963-8965.2005;
RA Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
RT "An aflatoxin biosynthesis cluster gene encodes a novel oxidase required
RT for conversion of versicolorin a to sterigmatocystin.";
RL Appl. Environ. Microbiol. 71:8963-8965(2005).
RN [20]
RP FUNCTION.
RX PubMed=15771506; DOI=10.1021/ja0455188;
RA Henry K.M., Townsend C.A.;
RT "Ordering the reductive and cytochrome P450 oxidative steps in
RT demethylsterigmatocystin formation yields general insights into the
RT biosynthesis of aflatoxin and related fungal metabolites.";
RL J. Am. Chem. Soc. 127:3724-3733(2005).
RN [21]
RP FUNCTION.
RX PubMed=16461654; DOI=10.1128/aem.72.2.1096-1101.2006;
RA Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
RT "The aflatoxin biosynthesis cluster gene, aflX, encodes an oxidoreductase
RT involved in conversion of versicolorin A to demethylsterigmatocystin.";
RL Appl. Environ. Microbiol. 72:1096-1101(2006).
RN [22]
RP FUNCTION.
RX PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
RA Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y., Adachi Y.,
RA Nakajima H., Yabe K.;
RT "Involvement of the nadA gene in formation of G-group aflatoxins in
RT Aspergillus parasiticus.";
RL Fungal Genet. Biol. 45:1081-1093(2008).
RN [23]
RP FUNCTION.
RX PubMed=18403714; DOI=10.1126/science.1154711;
RA Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L., Kelleher N.L.,
RA Townsend C.A.;
RT "Deconstruction of iterative multidomain polyketide synthase function.";
RL Science 320:243-246(2008).
RN [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19217941; DOI=10.1016/j.mycres.2009.01.013;
RA Hong S.Y., Linz J.E.;
RT "Functional expression and sub-cellular localization of the early aflatoxin
RT pathway enzyme Nor-1 in Aspergillus parasiticus.";
RL Mycol. Res. 113:591-601(2009).
RN [25]
RP DISRUPTION PHENOTYPE.
RX PubMed=22069731; DOI=10.3390/toxins3060647;
RA Abdel-Hadi A.M., Caley D.P., Carter D.R., Magan N.;
RT "Control of aflatoxin production of Aspergillus flavus and Aspergillus
RT parasiticus using RNA silencing technology by targeting aflD (nor-1)
RT gene.";
RL Toxins 3:647-659(2011).
RN [26]
RP INDUCTION.
RX PubMed=23113196;
RA Jahanshiri Z., Shams-Ghahfarokhi M., Allameh A., Razzaghi-Abyaneh M.;
RT "Effect of curcumin on Aspergillus parasiticus growth and expression of
RT major genes involved in the early and late stages of aflatoxin
RT biosynthesis.";
RL Iran. J. Public Health 41:72-79(2012).
RN [27]
RP INDUCTION.
RX PubMed=24294264; DOI=10.1590/s1517-83822013000200045;
RA Yahyaraeyat R., Khosravi A.R., Shahbazzadeh D., Khalaj V.;
RT "The potential effects of Zataria multiflora Boiss essential oil on growth,
RT aflatoxin production and transcription of aflatoxin biosynthesis pathway
RT genes of toxigenic Aspergillus parasiticus.";
RL Braz. J. Microbiol. 44:643-649(2013).
RN [28]
RP INDUCTION.
RX PubMed=26217023; DOI=10.3382/ps/pev207;
RA Yin H.B., Chen C.H., Kollanoor-Johny A., Darre M.J., Venkitanarayanan K.;
RT "Controlling Aspergillus flavus and Aspergillus parasiticus growth and
RT aflatoxin production in poultry feed using carvacrol and trans-
RT cinnamaldehyde.";
RL Poult. Sci. 94:2183-2190(2015).
CC -!- FUNCTION: Norsolorinic acid ketoreductase; part of the gene cluster
CC that mediates the biosynthesis of aflatoxins, a group of polyketide-
CC derived furanocoumarins, and part of the most toxic and carcinogenic
CC compounds among the known mycotoxins (PubMed:7993094, PubMed:15006741).
CC The four major aflatoxins produced by A.parasiticus are aflatoxin B1
CC (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2
CC (AFG2) (PubMed:15006741). The first step of the pathway is the
CC conversion of acetate to norsolorinic acid (NOR) and requires the fatty
CC acid synthase subunits aflA and aflB, as well as the PKS aflC
CC (PubMed:15006741). AflC combines a hexanoyl starter unit and 7 malonyl-
CC CoA extender units to synthesize the precursor NOR (PubMed:18403714).
CC The hexanoyl starter unit is provided to the acyl-carrier protein (ACP)
CC domain by the fungal fatty acid synthase aflA/aflB (PubMed:16256699).
CC The second step is the conversion of NOR to averantin (AVN) and
CC requires the norsolorinic acid ketoreductase aflD, which catalyzes the
CC dehydration of norsolorinic acid to form (1'S)-averantin
CC (PubMed:10584035, PubMed:19217941). The norsolorinic acid reductases
CC aflE and aflF may also play a role in the conversion of NOR to AVN
CC (PubMed:15006741). The cytochrome P450 monooxygenase aflG then
CC catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN)
CC (PubMed:8368836). The next step is performed by the 5'-hydroxyaverantin
CC dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which
CC is further converted to averufin (AVF) by aflK that plays a dual role
CC in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion
CC of 5'-oxoaverantin, as well as a versicolorin B synthase in a later
CC step in the pathway (PubMed:15006741, PubMed:11055914,
CC PubMed:15932995). The averufin oxidase aflI catalyzes the conversion of
CC AVF to versiconal hemiacetal acetate (VHA) (PubMed:15006741). VHA is
CC then the substrate for the versiconal hemiacetal acetate esterase aflJ
CC to yield versiconal (VAL) (PubMed:15006741). Versicolorin B synthase
CC aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran
CC ring of aflatoxin which is required for DNA-binding, thus giving to
CC aflatoxin its activity as a mutagen (PubMed:15006741, PubMed:8368837,
CC PubMed:15932995). Then, the activity of the versicolorin B desaturase
CC aflL leads to versicolorin A (VERA) (PubMed:15006741, PubMed:8368837).
CC A branch point starts from VERB since it can also be converted to
CC dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA
CC being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins
CC B2 and G2 (PubMed:15006741). Next, the versicolorin reductase aflM and
CC the cytochrome P450 monooxygenase aflN are involved in conversion of
CC VERA to demethylsterigmatocystin (DMST) (PubMed:15006741,
CC PubMed:1339261, PubMed:15771506). AflX and aflY seem also involved in
CC this step, through probable aflX-mediated epoxide ring-opening step
CC following versicolorin A oxidation and aflY-mediated Baeyer-Villiger
CC oxidation required for the formation of the xanthone ring
CC (PubMed:16332900, PubMed:16461654). The methyltransferase aflO then
CC leads to the modification of DMST to sterigmatocystin (ST), and of
CC DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both ST and
CC DHST are then substrates of the O-methyltransferase aflP to yield O-
CC methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin
CC (DHOMST), respectively (PubMed:8434913). Finally OMST is converted to
CC aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the
CC action of several enzymes including O-methylsterigmatocystin
CC oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also
CC the NADH-dependent flavin oxidoreductase nadA which is specifically
CC required for the synthesis of AFG1 (PubMed:15006741, PubMed:11996570,
CC PubMed:15528514, PubMed:18486503). {ECO:0000269|PubMed:10543813,
CC ECO:0000269|PubMed:10584035, ECO:0000269|PubMed:11055914,
CC ECO:0000269|PubMed:11996570, ECO:0000269|PubMed:1339261,
CC ECO:0000269|PubMed:15528514, ECO:0000269|PubMed:15771506,
CC ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:16256699,
CC ECO:0000269|PubMed:16332900, ECO:0000269|PubMed:16461654,
CC ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:18486503,
CC ECO:0000269|PubMed:19217941, ECO:0000269|PubMed:7993094,
CC ECO:0000269|PubMed:8368836, ECO:0000269|PubMed:8368837,
CC ECO:0000269|PubMed:8434913, ECO:0000305|PubMed:15006741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1'S)-averantin + NADP(+) = H(+) + NADPH + norsolorinic acid;
CC Xref=Rhea:RHEA:35447, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:71533, ChEBI:CHEBI:77899;
CC EC=1.1.1.349; Evidence={ECO:0000269|PubMed:10584035};
CC -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC {ECO:0000269|PubMed:15094053, ECO:0000305|PubMed:15006741}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14722624,
CC ECO:0000269|PubMed:19217941}. Vacuole {ECO:0000269|PubMed:19217941}.
CC -!- INDUCTION: Expression is stimulated by gluscoe (PubMed:15054098). The
CC promoter contains a CRE1 element (5'-TGACATAA-3') required for cAMP-
CC mediated stimulation of expression (PubMed:15054098). Expression is
CC also positively regulated by the cluster-specific transcription factor
CC aflR that binds to an AFLR1 element (5'-TCGGCCAGCGA-3')
CC (PubMed:15054098, PubMed:15746358). The promoter contains also an aflD-
CC specific element called NorL (residues -210 to -238) and required for
CC full transcription (PubMed:15746358). Natural plant compounds carvacrol
CC (CR) and trans-cinnamaldehyde (TC) strongly reduce the expression
CC (PubMed:26217023). Zataria multiflora essential oil reduces gene
CC expression (PubMed:24294264). Expression is also repressed by curcumin
CC (PubMed:23113196). {ECO:0000269|PubMed:15054098,
CC ECO:0000269|PubMed:15746358, ECO:0000269|PubMed:23113196,
CC ECO:0000269|PubMed:24294264, ECO:0000269|PubMed:26217023}.
CC -!- DISRUPTION PHENOTYPE: Leads to accumulation of norsolorinic acid and a
CC substantial reduced production of aflatoxin AFB1 (PubMed:7993094).
CC {ECO:0000269|PubMed:7993094}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KJK60791.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L27801; AAA58798.1; -; Genomic_DNA.
DR EMBL; AY371490; AAS66005.1; -; Genomic_DNA.
DR EMBL; JZEE01000728; KJK60791.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q00278; -.
DR SMR; Q00278; -.
DR STRING; 1403190.Q00278; -.
DR EnsemblFungi; KJK60791; KJK60791; P875_00052988.
DR KEGG; ag:AAA58798; -.
DR BioCyc; MetaCyc:MON-14027; -.
DR BRENDA; 1.1.1.349; 523.
DR BRENDA; 1.1.1.B25; 523.
DR UniPathway; UPA00287; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0140393; F:norsolorinic acid ketoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NADP; Oxidoreductase; Reference proteome; Vacuole.
FT CHAIN 1..271
FT /note="Norsolorinic acid ketoreductase"
FT /id="PRO_0000054736"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 57..58
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
FT BINDING 164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6PQJ9"
SQ SEQUENCE 271 AA; 29569 MW; 34059A857672059A CRC64;
MNGSLSQHDQ ERLSTPYRDG PPEETVYLVT GASRGIGRGL IEAFLQRPKS TVVAWLRNVR
TATPALSALT VAEGSRMIIV QLNSDSETDA QAAVQTLREE HGVTHLDVVV ANAAMATNFG
PASTMPLEHL QAHMMVNMYA PVLLFQATRL MLQQSKQQAK FVLIGAPIST ITNMHDYSRA
PLTAYGVSKL AANYMVRKFH FENKWLTAFI IDPGHVQTDM GDQGARLMGR PQAPTTVADS
VAGICARIDE ATKETTSGHF VIHTDGSQLP W
