AL3H1_ARATH
ID AL3H1_ARATH Reviewed; 484 AA.
AC Q70DU8; A8MQF0; Q8LFT7; Q9C6Y7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Aldehyde dehydrogenase family 3 member H1;
DE Short=AtALDH4;
DE Short=Ath-ALDH4;
DE EC=1.2.1.3;
GN Name=ALDH3H1; Synonyms=ALDH4; OrderedLocusNames=At1g44170;
GN ORFNames=T7O23.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-484 (ISOFORM ALPHA), AND INDUCTION.
RX PubMed=15830124; DOI=10.1007/s11103-004-7796-6;
RA Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.;
RT "Detailed expression analysis of selected genes of the aldehyde
RT dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana.";
RL Plant Mol. Biol. 57:315-332(2005).
RN [6]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=11849595; DOI=10.1046/j.1365-313x.2001.01176.x;
RA Kirch H.-H., Nair A., Bartels D.;
RT "Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated
RT from the resurrection plant Craterostigma plantagineum and Arabidopsis
RT thaliana.";
RL Plant J. 28:555-567(2001).
RN [7]
RP NOMENCLATURE.
RX PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004;
RA Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
RT "The ALDH gene superfamily of Arabidopsis.";
RL Trends Plant Sci. 9:371-377(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP MUTAGENESIS OF CYS-45; ILE-200; CYS-247 AND CYS-253, ACTIVITY REGULATION,
RP AND 3D-STRUCTURE MODELING.
RX PubMed=21166653; DOI=10.1042/bj20101337;
RA Stiti N., Adewale I.O., Petersen J., Bartels D., Kirch H.H.;
RT "Engineering the nucleotide coenzyme specificity and sulfhydryl redox
RT sensitivity of two stress-responsive aldehyde dehydrogenase isoenzymes of
RT Arabidopsis thaliana.";
RL Biochem. J. 434:459-471(2011).
RN [9]
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22442412; DOI=10.1093/jxb/ers081;
RA Missihoun T.D., Kirch H.H., Bartels D.;
RT "T-DNA insertion mutants reveal complex expression patterns of the aldehyde
RT dehydrogenase 3H1 locus in Arabidopsis thaliana.";
RL J. Exp. Bot. 63:3887-3898(2012).
RN [10]
RP 3D-STRUCTURE MODELING, AND MUTAGENESIS OF GLU-149; VAL-178 AND ILE-200.
RX PubMed=24463048; DOI=10.1016/j.bbapap.2014.01.008;
RA Stiti N., Podgorska K., Bartels D.;
RT "Aldehyde dehydrogenase enzyme ALDH3H1 from Arabidopsis thaliana:
RT Identification of amino acid residues critical for cofactor specificity.";
RL Biochim. Biophys. Acta 1844:681-693(2014).
CC -!- FUNCTION: Involved in oxidative stress tolerance by detoxifying
CC reactive aldehydes derived from lipid peroxidation. Medium- to long-
CC chain saturated aldehydes are preferred substrates, while the short-
CC chain aldehyde propanal is a weak substrate. Is strictely NAD(+)
CC specific. {ECO:0000269|PubMed:21166653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000269|PubMed:21166653};
CC -!- ACTIVITY REGULATION: Thiol-based regulation. Inactivation after
CC dimerization under oxidizing conditions. {ECO:0000269|PubMed:21166653}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=510 uM for propionaldehyde {ECO:0000269|PubMed:21166653};
CC KM=71 uM for hexanal {ECO:0000269|PubMed:21166653};
CC KM=29 uM for octanal {ECO:0000269|PubMed:21166653};
CC KM=8 uM for nonanal {ECO:0000269|PubMed:21166653};
CC KM=5 uM for dodecanal {ECO:0000269|PubMed:21166653};
CC KM=180 uM for trans-2-hexenal {ECO:0000269|PubMed:21166653};
CC KM=3 uM for trans-2-nonenal {ECO:0000269|PubMed:21166653};
CC KM=40.3 uM for 4-hydroxynonenal {ECO:0000269|PubMed:21166653};
CC KM=421 uM for NAD(+) (in the presence of hexanal as co-substrate)
CC {ECO:0000269|PubMed:21166653};
CC KM=119 uM for NAD(+) (in the presence of trans-2-nonenal as co-
CC substrate) {ECO:0000269|PubMed:21166653};
CC Vmax=7.3 umol/min/mg enzyme with propionaldehyde as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=12 umol/min/mg enzyme with hexanal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=18 umol/min/mg enzyme with octanal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=19.2 umol/min/mg enzyme with nonanal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=23.9 umol/min/mg enzyme with dodecanal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=2.4 umol/min/mg enzyme with trans-2-hexenal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=2.9 umol/min/mg enzyme with trans-2-nonenal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=1.4 umol/min/mg enzyme with 4-hydroxynonenal as substrate
CC {ECO:0000269|PubMed:21166653};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:21166653};
CC -!- SUBUNIT: Homodimer and homomultimer. {ECO:0000269|PubMed:21166653}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. An alternative promoter within intron 1 may direct
CC expression of several alternative transcripts, including isoform
CC beta.;
CC Name=alpha;
CC IsoId=Q70DU8-1; Sequence=Displayed;
CC Name=beta;
CC IsoId=Q70DU8-2; Sequence=VSP_054869;
CC -!- TISSUE SPECIFICITY: Isoform alpha is expressed in expanded leaves and
CC flowers. Detected in seedlings. Isoform beta is mainly expressed in
CC flowers. Detected in leaves and seedlings.
CC {ECO:0000269|PubMed:22442412}.
CC -!- INDUCTION: By abscisic acid (ABA), dehydration and salt stress in
CC roots. Isoform alpha is up-regulated in leaves but not in roots upon
CC salt treatment. Isoforn beta is up-regulated by salt treatment in both
CC roots and leaves. {ECO:0000269|PubMed:11849595,
CC ECO:0000269|PubMed:15830124, ECO:0000269|PubMed:22442412}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to salt stress.
CC {ECO:0000269|PubMed:22442412}.
CC -!- MISCELLANEOUS: [Isoform alpha]: Major isoform.
CC -!- MISCELLANEOUS: [Isoform beta]: Produced by alternative splicing. Maybe
CC not translated into a protein or accumulates at a level below
CC detection. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AC074228; AAG50550.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32025.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32026.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32027.1; -; Genomic_DNA.
DR EMBL; AY072122; AAL59944.1; -; mRNA.
DR EMBL; AY084648; AAM61211.1; -; mRNA.
DR EMBL; AJ585241; CAE51203.1; -; mRNA.
DR PIR; H96505; H96505.
DR RefSeq; NP_001077676.1; NM_001084207.1. [Q70DU8-2]
DR RefSeq; NP_175081.1; NM_103541.3. [Q70DU8-1]
DR RefSeq; NP_849770.1; NM_179439.4. [Q70DU8-1]
DR AlphaFoldDB; Q70DU8; -.
DR SMR; Q70DU8; -.
DR STRING; 3702.AT1G44170.2; -.
DR iPTMnet; Q70DU8; -.
DR PaxDb; Q70DU8; -.
DR PRIDE; Q70DU8; -.
DR ProteomicsDB; 244811; -. [Q70DU8-1]
DR EnsemblPlants; AT1G44170.1; AT1G44170.1; AT1G44170. [Q70DU8-1]
DR EnsemblPlants; AT1G44170.2; AT1G44170.2; AT1G44170. [Q70DU8-1]
DR EnsemblPlants; AT1G44170.3; AT1G44170.3; AT1G44170. [Q70DU8-2]
DR GeneID; 841020; -.
DR Gramene; AT1G44170.1; AT1G44170.1; AT1G44170. [Q70DU8-1]
DR Gramene; AT1G44170.2; AT1G44170.2; AT1G44170. [Q70DU8-1]
DR Gramene; AT1G44170.3; AT1G44170.3; AT1G44170. [Q70DU8-2]
DR KEGG; ath:AT1G44170; -.
DR Araport; AT1G44170; -.
DR TAIR; locus:2205851; AT1G44170.
DR eggNOG; KOG2456; Eukaryota.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; Q70DU8; -.
DR OMA; RRITWAA; -.
DR PhylomeDB; Q70DU8; -.
DR BioCyc; ARA:AT1G44170-MON; -.
DR BRENDA; 1.2.1.3; 399.
DR PRO; PR:Q70DU8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q70DU8; baseline and differential.
DR Genevisible; Q70DU8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; ISS:TAIR.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; ISS:TAIR.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:TAIR.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009269; P:response to desiccation; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Disulfide bond; NAD;
KW Oxidoreductase; Reference proteome; Stress response.
FT CHAIN 1..484
FT /note="Aldehyde dehydrogenase family 3 member H1"
FT /id="PRO_0000256060"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 196..201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 45
FT /note="Interchain"
FT VAR_SEQ 1..71
FT /note="MAAKKVFGSAEASNLVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEI
FT VAALRDDLGKPELESSVYE -> MFYQQRVL (in isoform beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_054869"
FT MUTAGEN 45
FT /note="C->S: Decreased solubility, loss of dimerization and
FT strongly decreased activity."
FT /evidence="ECO:0000269|PubMed:21166653"
FT MUTAGEN 149
FT /note="E->D: Small effect on NAD(+) interaction, but 40%
FT loss of efficiency. Ability to use NADP(+). 70% loss of
FT efficiency with NAD(+); when associated with V-200.
FT Impaired affinity for both cofactors and decreased
FT catalytic efficiency; when associated with G-200."
FT /evidence="ECO:0000269|PubMed:24463048"
FT MUTAGEN 149
FT /note="E->N: Ability to use NADP(+) and 33% decreased
FT efficiency with NAD(+). 70% loss of efficiency with NAD(+);
FT when associated with V-200. Impaired affinity for both
FT cofactors and decreased catalytic efficiency; when
FT associated with G-200."
FT /evidence="ECO:0000269|PubMed:24463048"
FT MUTAGEN 149
FT /note="E->Q: Loss of specificity for NAD(+) and loss of 25%
FT efficiency. 15% efficiency with NAD(+); when associated
FT with V-200. Impaired affinity for both cofactors and
FT decreased catalytic efficiency; when associated with G-
FT 200."
FT /evidence="ECO:0000269|PubMed:24463048"
FT MUTAGEN 149
FT /note="E->T: Loss of specificity and increased NADP(+)
FT binding. Decerased catalytic efficiency. Loss of cofactor
FT specificity and same lower efficiency with both; when
FT associated with V-200. Impaired affinity for both cofactors
FT and decreased catalytic efficiency; when associated with G-
FT 200. Changed coenzyme preference from NAD(+) to NADP(+),
FT but no effect on the catalytic efficiency; when associated
FT with R-178 and V-200."
FT /evidence="ECO:0000269|PubMed:24463048"
FT MUTAGEN 178
FT /note="V->R: Changed coenzyme preference from NAD(+) to
FT NADP(+), but no effect on the catalytic efficiency; when
FT associated with T-149 and V-200."
FT /evidence="ECO:0000269|PubMed:24463048"
FT MUTAGEN 200
FT /note="I->G: Changed coenzyme preference from NAD(+) to
FT NADP(+), but impaired affinities for both cofactors. No
FT effect on the interaction with the substrate. Impaired
FT affinities for both cofactors and decreased catalytic
FT efficiencies; when associated with D-149, Q-149, N-149 or
FT T-149."
FT /evidence="ECO:0000269|PubMed:21166653,
FT ECO:0000269|PubMed:24463048"
FT MUTAGEN 200
FT /note="I->V: Also able to use NADP(+) as coenzyme, but no
FT effect on the interaction with the substrate. 15%
FT efficiency with NAD(+); when associated with Q-149. 70%
FT loss of efficiency with NAD(+); when associated with D-149
FT or N-149. Loss of cofactor specificity and same lower
FT efficiency with both; when associated with T-149. Changed
FT coenzyme preference from NAD(+) to NADP(+), but no effect
FT on the catalytic efficiency; when associated with T-149 and
FT R-178."
FT /evidence="ECO:0000269|PubMed:21166653,
FT ECO:0000269|PubMed:24463048"
FT MUTAGEN 247
FT /note="C->S: No effect on solubility, but 10% loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:21166653"
FT MUTAGEN 253
FT /note="C->S: No effect on solubility, but loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:21166653"
FT CONFLICT 200
FT /note="I -> V (in Ref. 5; CAE51203)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="A -> D (in Ref. 5; CAE51203)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="F -> L (in Ref. 5; CAE51203)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="A -> T (in Ref. 4; AAM61211)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="F -> S (in Ref. 5; CAE51203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53159 MW; 5D931EF77293F668 CRC64;
MAAKKVFGSA EASNLVTELR RSFDDGVTRG YEWRVTQLKK LMIICDNHEP EIVAALRDDL
GKPELESSVY EVSLLRNSIK LALKQLKNWM APEKAKTSLT TFPASAEIVS EPLGVVLVIS
AWNYPFLLSI DPVIGAISAG NAVVLKPSEL APASSALLTK LLEQYLDPSA VRVVEGAVTE
TSALLEQKWD KIFYTGSSKI GRVIMAAAAK HLTPVVLELG GKSPVVVDSD TDLKVTVRRI
IVGKWGCNNG QACVSPDYIL TTKEYAPKLI DAMKLELEKF YGKNPIESKD MSRIVNSNHF
DRLSKLLDEK EVSDKIVYGG EKDRENLKIA PTILLDVPLD SLIMSEEIFG PLLPILTLNN
LEESFDVIRS RPKPLAAYLF THNKKLKERF AATVSAGGIV VNDIAVHLAL HTLPFGGVGE
SGMGAYHGKF SFDAFSHKKA VLYRSLFGDS AVRYPPYSRG KLRLLKALVD SNIFDLFKVL
LGLA
