BADH2_ARATH
ID BADH2_ARATH Reviewed; 503 AA.
AC Q9STS1; Q42237;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal {ECO:0000305};
DE EC=1.2.1.- {ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
DE AltName: Full=4-trimethylammoniobutyraldehyde dehydrogenase ALDH10A9 {ECO:0000305};
DE EC=1.2.1.47 {ECO:0000269|PubMed:32845293};
DE AltName: Full=Aldehyde dehydrogenase family 10 member A9 {ECO:0000303|PubMed:15358267};
DE AltName: Full=Aminobutyraldehyde dehydrogenase ALDH10A9 {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:21053011, ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
DE AltName: Full=Betaine aldehyde dehydrogenase ALDH10A9 {ECO:0000305};
DE EC=1.2.1.8 {ECO:0000269|PubMed:21053011, 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=ALDH10A9 {ECO:0000303|PubMed:15358267};
GN OrderedLocusNames=At3g48170 {ECO:0000312|Araport:AT3G48170};
GN ORFNames=T24C20.50 {ECO:0000312|EMBL:CAB51064.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [MRNA] OF 417-503.
RC STRAIN=cv. Columbia; TISSUE=Seed;
RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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, AND TISSUE
RP SPECIFICITY.
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:21053011, PubMed:27725774, PubMed:32845293).
CC Metabolizes and detoxifies aldehyde products of polyamine degradation
CC to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-
CC aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine,
CC respectively (PubMed:21053011, PubMed:27725774, PubMed:32845293).
CC Production of 4-aminobutinoate by ALDH10A9 may confer tolerance to salt
CC stress (PubMed:27725774). Catalyzes the oxidation of 3-aminopropanal to
CC beta-alanine (PubMed:21053011, PubMed:27725774, PubMed:32845293).
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:21053011, PubMed:26169197,
CC PubMed:27725774, PubMed:32845293). Catalyzes with low efficiency the
CC oxidation of betaine aldehyde to glycine betaine (PubMed:21053011,
CC PubMed:27725774, PubMed:32845293). {ECO:0000269|PubMed:21053011,
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:21053011, ECO:0000269|PubMed:27725774,
CC ECO:0000269|PubMed:32845293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000269|PubMed:21053011, ECO:0000269|PubMed:27725774,
CC 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:21053011,
CC ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696;
CC Evidence={ECO:0000269|PubMed:21053011, ECO:0000269|PubMed:27725774,
CC 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; Evidence={ECO:0000269|PubMed:21053011,
CC ECO:0000269|PubMed:27725774, ECO:0000269|PubMed:32845293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000269|PubMed:21053011, ECO:0000269|PubMed:27725774,
CC ECO:0000269|PubMed:32845293};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=460 uM for 4-aminobutanal {ECO:0000269|PubMed:27725774};
CC KM=31 uM for 4-aminobutanal {ECO:0000269|PubMed:32845293};
CC KM=17.3 uM for 3-aminopropanal {ECO:0000269|PubMed:27725774};
CC KM=34 uM for 3-aminopropanal {ECO:0000269|PubMed:32845293};
CC KM=17 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:32845293};
CC KM=7 uM for 4-guanidinobutanal {ECO:0000269|PubMed:32845293};
CC KM=73.6 uM for NAD(+) with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:27725774};
CC KM=86 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:27725774};
CC KM=33 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:32845293};
CC Vmax=9.5 umol/min/mg enzyme with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:27725774};
CC Vmax=15 umol/min/mg enzyme with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:27725774};
CC Vmax=4.2 umol/min/mg enzyme toward NAD(+) in presence of 4-
CC aminobutanal {ECO:0000269|PubMed:27725774};
CC Vmax=13.4 umol/min/mg enzyme toward NAD(+) in presence of 3-
CC aminopropanal {ECO:0000269|PubMed:27725774};
CC pH dependence:
CC Optimum pH is 9.75 with 4-aminobutanal as substrate. Optimum pH is
CC 9.5 with 3-aminopropanal as substrate. {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: Peroxisome {ECO:0000269|PubMed:21053011,
CC ECO:0000269|PubMed:27725774}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:32845293}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:27725774). Mutant seedlings exhibit increased
CC sensitivity to salt stress (PubMed:27725774).
CC {ECO:0000269|PubMed:27725774}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL096856; CAB51064.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78376.1; -; Genomic_DNA.
DR EMBL; AF370333; AAK44148.1; -; mRNA.
DR EMBL; AY062987; AAL34161.1; -; mRNA.
DR EMBL; Z29888; CAA82832.1; -; mRNA.
DR PIR; T13006; T13006.
DR RefSeq; NP_190400.1; NM_114686.4.
DR AlphaFoldDB; Q9STS1; -.
DR SMR; Q9STS1; -.
DR BioGRID; 9291; 6.
DR STRING; 3702.AT3G48170.1; -.
DR iPTMnet; Q9STS1; -.
DR MetOSite; Q9STS1; -.
DR PaxDb; Q9STS1; -.
DR PRIDE; Q9STS1; -.
DR ProteomicsDB; 240969; -.
DR EnsemblPlants; AT3G48170.1; AT3G48170.1; AT3G48170.
DR GeneID; 823972; -.
DR Gramene; AT3G48170.1; AT3G48170.1; AT3G48170.
DR KEGG; ath:AT3G48170; -.
DR Araport; AT3G48170; -.
DR TAIR; locus:2100449; AT3G48170.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; Q9STS1; -.
DR OMA; AFTASMH; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; Q9STS1; -.
DR BioCyc; ARA:AT3G48170-MON; -.
DR BioCyc; MetaCyc:AT3G48170-MON; -.
DR BRENDA; 1.2.1.19; 399.
DR BRENDA; 1.2.1.8; 399.
DR UniPathway; UPA00529; UER00386.
DR PRO; PR:Q9STS1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STS1; baseline and differential.
DR Genevisible; Q9STS1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:TAIR.
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:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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; 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 Metal-binding; NAD; Oxidoreductase; Peroxisome; Reference proteome; Sodium.
FT CHAIN 1..503
FT /note="Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal"
FT /id="PRO_0000256063"
FT MOTIF 501..503
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
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 503 AA; 54918 MW; 7E17AE86E9F2784C CRC64;
MAITVPRRQL FIGGQWTEPV LRKTLPVVNP ATEDIIGYIP AATSEDVELA VEAARKAFTR
NNGKDWARAT GAVRAKYLRA IAAKVIERKS ELANLEAIDC GKPLDEAAWD MDDVAGCFEY
YADLAEGLDA KQKTPLSLPM DTFKGYILKE PIGVVGMITP WNYPLLMAVW KVAPSLAAGC
TAILKPSELA SLTCLELADI CREVGLPPGV LNILTGLGTE AGAPLASHPH VDKIVFTGST
TTGSSIMTSA AKLVKPVSLE LGGKSPIIVF DDVDIDKAVE WTMFGCFWTN GQICSATSRL
LVHERIADEF LDKLVKWTKN IKISDPFEEG CRLGPVVSKG QYERVLKFVS NARNEGATVL
CGGVRPEHLK KGYFVEPAIV SNVTTSMEIW REEVFGPALC VKTFSTEDEA IQLANDSQYG
LAGAVLSNDL ERCDRVSKAF QAGIVWVNCS QPCFCQAPWG GTKRSGFGRE LGEWGLENYL
SVKQVTQYIS DEPWGWYKPP SKL
