BADH1_ARATH
ID BADH1_ARATH Reviewed; 501 AA.
AC Q9S795; Q56ZQ8;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic {ECO:0000305};
DE EC=1.2.1.- {ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
DE AltName: Full=4-trimethylammoniobutyraldehyde dehydrogenase ALDH10A8 {ECO:0000305};
DE EC=1.2.1.47 {ECO:0000269|PubMed:32845293};
DE AltName: Full=Aldehyde dehydrogenase family 10 member A8 {ECO:0000303|PubMed:15358267};
DE AltName: Full=Aminobutyraldehyde dehydrogenase ALDH10A8 {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
DE AltName: Full=Betaine aldehyde dehydrogenase ALDH10A8 {ECO:0000305};
DE EC=1.2.1.8 {ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
DE AltName: Full=Gamma-guanidinobutyraldehyde dehydrogenase ALDH10A8 {ECO:0000305};
DE EC=1.2.1.54 {ECO:0000269|PubMed:32845293};
GN Name=ALDH10A8 {ECO:0000303|PubMed:15358267};
GN OrderedLocusNames=At1g74920 {ECO:0000312|Araport:AT1G74920};
GN ORFNames=F25A4.11 {ECO:0000312|EMBL:AAD55284.1},
GN F9E10.23 {ECO:0000312|EMBL:AAG51938.1};
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].
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].
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 [LARGE SCALE MRNA] OF 390-501.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21053011; DOI=10.1007/s00425-010-1297-4;
RA Missihoun T.D., Schmitz J., Klug R., Kirch H.H., Bartels D.;
RT "Betaine aldehyde dehydrogenase genes from Arabidopsis with different sub-
RT cellular localization affect stress responses.";
RL Planta 233:369-382(2011).
RN [8]
RP FUNCTION.
RX PubMed=26169197; DOI=10.1093/pcp/pcv105;
RA Missihoun T.D., Willee E., Guegan J.P., Berardocco S., Shafiq M.R.,
RA Bouchereau A., Bartels D.;
RT "Overexpression of ALDH10A8 and ALDH10A9 genes provides insight into their
RT role in glycine betaine synthesis and affects primary metabolism in
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 56:1798-1807(2015).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27725774; DOI=10.1038/srep35115;
RA Zarei A., Trobacher C.P., Shelp B.J.;
RT "Arabidopsis aldehyde dehydrogenase 10 family members confer salt tolerance
RT through putrescine-derived 4-aminobutyrate (GABA) production.";
RL Sci. Rep. 6:35115-35115(2016).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32845293; DOI=10.1093/jxb/eraa394;
RA Jacques F., Zhao Y., Kopecna M., Koncitikova R., Kopecny D., Rippa S.,
RA Perrin Y.;
RT "Roles for ALDH10 enzymes in gamma-butyrobetaine synthesis, seed
RT development, germination, and salt tolerance in Arabidopsis.";
RL J. Exp. Bot. 71:7088-7102(2020).
CC -!- FUNCTION: Dehydrogenase that catalyzes the oxidation of several
CC aminoaldehydes (PubMed:27725774, PubMed:32845293). Metabolizes and
CC detoxifies aldehyde products of polyamine degradation to non-toxic
CC amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and
CC 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively
CC (PubMed:27725774, PubMed:32845293). Production of 4-aminobutinoate by
CC ALDH10A8 may confer tolerance to salt stress (PubMed:27725774).
CC Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-
CC guanidinobutanal to 4-trimethylammoniobutanoate and 4-
CC guanidinobutanoate, respectively (PubMed:32845293). Involved in glycine
CC betaine biosynthesis (PubMed:26169197, PubMed:27725774,
CC PubMed:32845293). Catalyzes with low efficiency the oxidation of
CC betaine aldehyde to glycine betaine (PubMed:27725774, PubMed:32845293).
CC {ECO:0000269|PubMed:26169197, ECO:0000269|PubMed:27725774,
CC ECO:0000269|PubMed:32845293, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966,
CC ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:27725774,
CC ECO:0000269|PubMed:32845293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696;
CC Evidence={ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-
CC (trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244,
CC ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47;
CC Evidence={ECO:0000269|PubMed:32845293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17986;
CC Evidence={ECO:0000269|PubMed:32845293};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-guanidinobutanal + H2O + NAD(+) = 4-guanidinobutanoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:14381, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57486, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57854, ChEBI:CHEBI:57945; EC=1.2.1.54;
CC Evidence={ECO:0000269|PubMed:32845293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14382;
CC Evidence={ECO:0000269|PubMed:32845293};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8;
CC Evidence={ECO:0000269|PubMed:27725774};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000269|PubMed:27725774};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25.1 uM for 4-aminobutanal {ECO:0000269|PubMed:27725774};
CC KM=19 uM for 4-aminobutanal {ECO:0000269|PubMed:32845293};
CC KM=14.4 uM for 3-aminopropanal {ECO:0000269|PubMed:27725774};
CC KM=2 uM for 3-aminopropanal {ECO:0000269|PubMed:32845293};
CC KM=15 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:32845293};
CC KM=4 uM for 4-guanidinobutanal {ECO:0000269|PubMed:32845293};
CC KM=20.8 uM for NAD(+) with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:27725774};
CC KM=13.2 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:27725774};
CC KM=16 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:32845293};
CC Vmax=1.6 umol/min/mg enzyme with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:27725774};
CC Vmax=15.8 umol/min/mg enzyme with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:27725774};
CC Vmax=0.8 umol/min/mg enzyme toward NAD(+) in presence of 4-
CC aminobutanal {ECO:0000269|PubMed:27725774};
CC Vmax=3.6 umol/min/mg enzyme toward NAD(+) in presence of 3-
CC aminopropanal {ECO:0000269|PubMed:27725774};
CC pH dependence:
CC Optimum pH is 10.75 with 4-aminobutanal as substrate. Optimum pH is
CC 10.5 with 3-aminopropanal as substrate.
CC {ECO:0000269|PubMed:27725774};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21053011,
CC ECO:0000269|PubMed:27725774}. Plastid, chloroplast
CC {ECO:0000269|PubMed:27725774}. Note=Localizes in small organelles that
CC may be leucoplasts. {ECO:0000269|PubMed:21053011}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9S795-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:32845293}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:21053011, PubMed:27725774). Mutant seedlings exhibit
CC increased sensitivity to salt stress (PubMed:21053011,
CC PubMed:27725774). Mutant seedling exhibit increased sensitivity to
CC drought stress (PubMed:21053011). {ECO:0000269|PubMed:21053011,
CC ECO:0000269|PubMed:27725774}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AC008263; AAD55284.1; -; Genomic_DNA.
DR EMBL; AC013258; AAG51938.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35649.1; -; Genomic_DNA.
DR EMBL; AY093071; AAM13070.1; -; mRNA.
DR EMBL; BT008872; AAP68311.1; -; mRNA.
DR EMBL; AY087395; AAM64944.1; -; mRNA.
DR EMBL; AK220905; BAD94340.1; -; mRNA.
DR PIR; H96778; H96778.
DR RefSeq; NP_565094.1; NM_106150.4. [Q9S795-1]
DR AlphaFoldDB; Q9S795; -.
DR SMR; Q9S795; -.
DR BioGRID; 29050; 6.
DR STRING; 3702.AT1G74920.1; -.
DR iPTMnet; Q9S795; -.
DR PaxDb; Q9S795; -.
DR PRIDE; Q9S795; -.
DR ProteomicsDB; 240844; -. [Q9S795-1]
DR EnsemblPlants; AT1G74920.1; AT1G74920.1; AT1G74920. [Q9S795-1]
DR GeneID; 843831; -.
DR Gramene; AT1G74920.1; AT1G74920.1; AT1G74920. [Q9S795-1]
DR KEGG; ath:AT1G74920; -.
DR Araport; AT1G74920; -.
DR TAIR; locus:2027186; AT1G74920.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; Q9S795; -.
DR OMA; EGGHYSF; -.
DR PhylomeDB; Q9S795; -.
DR BioCyc; ARA:AT1G74920-MON; -.
DR BRENDA; 1.2.1.19; 399.
DR BRENDA; 1.2.1.8; 399.
DR UniPathway; UPA00529; UER00386.
DR PRO; PR:Q9S795; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S795; baseline and differential.
DR Genevisible; Q9S795; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009516; C:leucoplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0047107; F:gamma-guanidinobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0031402; F:sodium ion binding; ISS:UniProtKB.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:UniProtKB.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IDA:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP: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; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Cytoplasm; Metal-binding; NAD;
KW Oxidoreductase; Plastid; Reference proteome; Sodium.
FT CHAIN 1..501
FT /note="Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic"
FT /id="PRO_0000007179"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 99
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 189
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 238..245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 238..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 393
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
SQ SEQUENCE 501 AA; 54432 MW; BA8B03C28C22453B CRC64;
MAIPMPTRQL FIDGEWREPI LKKRIPIVNP ATEEVIGDIP AATTEDVDVA VNAARRALSR
NKGKDWAKAP GAVRAKYLRA IAAKVNERKT DLAKLEALDC GKPLDEAVWD MDDVAGCFEF
YADLAEGLDA KQKAPVSLPM ESFKSYVLKQ PLGVVGLITP WNYPLLMAVW KVAPSLAAGC
TAILKPSELA SVTCLELADI CREVGLPPGV LNVLTGFGSE AGAPLASHPG VDKIAFTGSF
ATGSKVMTAA AQLVKPVSME LGGKSPLIVF DDVDLDKAAE WALFGCFWTN GQICSATSRL
LVHESIASEF IEKLVKWSKN IKISDPMEEG CRLGPVVSKG QYEKILKFIS TAKSEGATIL
HGGSRPEHLE KGFFIEPTII TDVTTSMQIW REEVFGPVLC VKTFASEDEA IELANDSHYG
LGAAVISNDT ERCDRISEAF EAGIVWINCS QPCFTQAPWG GVKRSGFGRE LGEWGLDNYL
SVKQVTLYTS NDPWGWYKSP N
