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   27-MAR-2024, entry version 142.
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
CC         co-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.Q70DU8; -.
DR   iPTMnet; Q70DU8; -.
DR   PaxDb; 3702-AT1G44170-2; -.
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; AT1G44170; ALDH3H1.
DR   eggNOG; KOG2456; Eukaryota.
DR   HOGENOM; CLU_005391_3_1_1; -.
DR   InParanoid; Q70DU8; -.
DR   OMA; RRITWAA; -.
DR   OrthoDB; 1205055at2759; -.
DR   PhylomeDB; Q70DU8; -.
DR   BioCyc; ARA:AT1G44170-MONOMER; -.
DR   BRENDA; 1.2.1.3; 399.
DR   PRO; PR:Q70DU8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q70DU8; baseline and differential.
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; IEA:InterPro.
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   CDD; cd07137; ALDH_F3FHI; 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; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   Genevisible; Q70DU8; AT.
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
FT                   G-200."
FT                   /evidence="ECO:0000269|PubMed:24463048"
FT   MUTAGEN         149
FT                   /note="E->T: Loss of specificity and increased NADP(+)
FT                   binding. Decreased 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
FT                   G-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
//