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Database: UniProt
Entry: CADH7_ARATH
LinkDB: CADH7_ARATH
Original site: CADH7_ARATH 
ID   CADH7_ARATH             Reviewed;         357 AA.
AC   Q02971; B9DG76; O65622; Q53ZN3; Q9SZJ9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=Cinnamyl alcohol dehydrogenase 7 {ECO:0000303|PubMed:14745009};
DE            Short=AtCAD7 {ECO:0000303|PubMed:14745009};
DE            EC=1.1.1.195 {ECO:0000269|PubMed:14745009};
DE   AltName: Full=Cinnamyl alcohol dehydrogenase-like protein B;
GN   Name=CAD7; Synonyms=CAD4, CADB1, ELI3-1, LCAD-B;
GN   OrderedLocusNames=At4g37980; ORFNames=F20D10.100;
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 [MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=1464303; DOI=10.1002/j.1460-2075.1992.tb05572.x;
RA   Kiedrowski S., Kawalleck P., Hahlbrock K., Somssich I.E., Dangl J.L.;
RT   "Rapid activation of a novel plant defense gene is strictly dependent on
RT   the Arabidopsis RPM1 disease resistance locus.";
RL   EMBO J. 11:4677-4684(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=14745009; DOI=10.1073/pnas.0307987100;
RA   Kim S.-J., Kim M.-R., Bedgar D.L., Moinuddin S.G.A., Cardenas C.L.,
RA   Davin L.B., Kang C., Lewis N.G.;
RT   "Functional reclassification of the putative cinnamyl alcohol dehydrogenase
RT   multigene family in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:1455-1460(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161.
RC   STRAIN=cv. Columbia;
RX   PubMed=10809443; DOI=10.1023/a:1006368316413;
RA   Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT   "Organization and structural evolution of four multigene families in
RT   Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL   Plant Mol. Biol. 42:703-717(2000).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=16832689; DOI=10.1007/s00425-006-0326-9;
RA   Eudes A., Pollet B., Sibout R., Do C.-T., Seguin A., Lapierre C.,
RA   Jouanin L.;
RT   "Evidence for a role of AtCAD 1 in lignification of elongating stems of
RT   Arabidopsis thaliana.";
RL   Planta 225:23-39(2006).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=17467016; DOI=10.1016/j.phytochem.2007.02.032;
RA   Kim S.-J., Kim K.-W., Cho M.-H., Franceschi V.R., Davin L.B., Lewis N.G.;
RT   "Expression of cinnamyl alcohol dehydrogenases and their putative
RT   homologues during Arabidopsis thaliana growth and development: lessons for
RT   database annotations?";
RL   Phytochemistry 68:1957-1974(2007).
CC   -!- FUNCTION: Involved in lignin biosynthesis. Catalyzes the final step
CC       specific for the production of lignin monomers. Catalyzes the NADPH-
CC       dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde,
CC       sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their
CC       respective alcohols. {ECO:0000269|PubMed:14745009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC         NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC         ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC         Evidence={ECO:0000269|PubMed:14745009};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=320 uM for 4-coumaraldehyde (at pH 6.25-6.5 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:14745009};
CC         KM=3685 uM for caffeyl aldehyde (at pH 6.25 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:14745009};
CC         KM=675 uM for coniferaldehyde (at pH 6.25 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:14745009};
CC         KM=756 uM for 5-hydroxyconiferaldehyde (at pH 6.25 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:14745009};
CC         KM=373 uM for sinapaldehyde (at pH 6.25 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:14745009};
CC         Vmax=28.6 pmol/sec/ug enzyme with 4-coumaraldehyde as substrate (at
CC         pH 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC         Vmax=79.0 pmol/sec/ug enzyme with caffeyl aldehyde as substrate (at
CC         pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC         Vmax=13.0 pmol/sec/ug enzyme with coniferaldehyde as substrate (at pH
CC         6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC         Vmax=2.7 pmol/sec/ug enzyme with 5-hydroxyconiferaldehyde as
CC         substrate (at pH 6.25 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:14745009};
CC         Vmax=0.7 pmol/sec/ug enzyme with sinapaldehyde as substrate (at pH
CC         6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC       {ECO:0000269|PubMed:14745009}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q02971-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q02971-2; Sequence=VSP_037892, VSP_037893;
CC   -!- TISSUE SPECIFICITY: Expressed in the differentiation and elongation
CC       zones of primary and lateral roots. Expressed in the hypocotyl,
CC       cotyledon and leaf veins, hydathodes and trichomes. In stems, expressed
CC       in the vascular cambium region. Expressed in the style, anthers, stamen
CC       filaments, vascular tissues of sepals and stigmatic regions in flowers,
CC       and abscission, style and stigmatic regions of siliques and seed testa.
CC       {ECO:0000269|PubMed:16832689, ECO:0000269|PubMed:17467016}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X67816; CAA48027.1; -; mRNA.
DR   EMBL; AY302079; AAP59432.1; -; mRNA.
DR   EMBL; AL035538; CAB37538.1; -; Genomic_DNA.
DR   EMBL; AL161592; CAB80463.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86859.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86860.1; -; Genomic_DNA.
DR   EMBL; AF360225; AAK25935.1; -; mRNA.
DR   EMBL; AY040066; AAK64124.1; -; mRNA.
DR   EMBL; AY050407; AAK91423.1; -; mRNA.
DR   EMBL; AY050931; AAK93608.1; -; mRNA.
DR   EMBL; AY056385; AAL08241.1; -; mRNA.
DR   EMBL; BT002729; AAO11645.1; -; mRNA.
DR   EMBL; AK317050; BAH19743.1; -; mRNA.
DR   EMBL; Y16848; CAA76419.1; -; Genomic_DNA.
DR   PIR; T05625; T05625.
DR   RefSeq; NP_001031805.1; NM_001036728.2. [Q02971-2]
DR   RefSeq; NP_195511.1; NM_119959.4. [Q02971-1]
DR   AlphaFoldDB; Q02971; -.
DR   SMR; Q02971; -.
DR   BioGRID; 15234; 1.
DR   STRING; 3702.Q02971; -.
DR   iPTMnet; Q02971; -.
DR   MetOSite; Q02971; -.
DR   PaxDb; 3702-AT4G37980-1; -.
DR   ProteomicsDB; 223862; -. [Q02971-1]
DR   EnsemblPlants; AT4G37980.1; AT4G37980.1; AT4G37980. [Q02971-1]
DR   EnsemblPlants; AT4G37980.2; AT4G37980.2; AT4G37980. [Q02971-2]
DR   GeneID; 829954; -.
DR   Gramene; AT4G37980.1; AT4G37980.1; AT4G37980. [Q02971-1]
DR   Gramene; AT4G37980.2; AT4G37980.2; AT4G37980. [Q02971-2]
DR   KEGG; ath:AT4G37980; -.
DR   Araport; AT4G37980; -.
DR   TAIR; AT4G37980; ELI3-1.
DR   eggNOG; KOG0023; Eukaryota.
DR   InParanoid; Q02971; -.
DR   OMA; EAKFLPF; -.
DR   OrthoDB; 1550at2759; -.
DR   PhylomeDB; Q02971; -.
DR   BioCyc; ARA:AT4G37980-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-17195; -.
DR   BRENDA; 1.1.1.195; 399.
DR   SABIO-RK; Q02971; -.
DR   UniPathway; UPA00711; -.
DR   PRO; PR:Q02971; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q02971; baseline and differential.
DR   Genevisible; Q02971; AT.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010597; P:green leaf volatile biosynthetic process; IGI:TAIR.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEP:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR   CDD; cd05283; CAD1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF57; CINNAMYL ALCOHOL DEHYDROGENASE 7; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Lignin biosynthesis; Metal-binding; NADP;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..357
FT                   /note="Cinnamyl alcohol dehydrogenase 7"
FT                   /id="PRO_0000160808"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..192
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..215
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         297..299
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         291..298
FT                   /note="RKMVVGSM -> MNLFVSHL (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_037892"
FT   VAR_SEQ         299..357
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_037893"
FT   CONFLICT        6
FT                   /note="E -> Q (in Ref. 1; CAA48027)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17
FT                   /note="E -> N (in Ref. 1; CAA48027)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="I -> V (in Ref. 1; CAA48027)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  38246 MW;  2C27B3C2BF030166 CRC64;
     MGKVLEKEAF GLAAKDESGI LSPFSFSRRA TGEKDVRFKV LFCGICHTDL SMAKNEWGLT
     TYPLVPGHEI VGVVTEVGAK VKKFNAGDKV GVGYMAGSCR SCDSCNDGDE NYCPKMILTS
     GAKNFDDTMT HGGYSDHMVC AEDFIIRIPD NLPLDGAAPL LCAGVTVYSP MKYHGLDKPG
     MHIGVVGLGG LGHVAVKFAK AMGTKVTVIS TSERKRDEAV TRLGADAFLV SRDPKQMKDA
     MGTMDGIIDT VSATHPLLPL LGLLKNKGKL VMVGAPAEPL ELPVFPLIFG RKMVVGSMVG
     GIKETQEMVD LAGKHNITAD IELISADYVN TAMERLAKAD VKYRFVIDVA NTMKPTP
//
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