ID HSDD1_ARATH Reviewed; 439 AA.
AC Q9FX01; Q0VH36; Q8LER8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1 {ECO:0000303|PubMed:16835224};
DE Short=At3BETAHSD/D1 {ECO:0000303|PubMed:16835224};
DE EC=1.1.1.418 {ECO:0000269|PubMed:16835224, ECO:0000269|PubMed:19218365};
DE AltName: Full=4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-1;
DE AltName: Full=Reticulon-like protein B24 {ECO:0000303|PubMed:17604024};
DE Short=AtRTNLB24 {ECO:0000303|PubMed:17604024};
DE AltName: Full=Sterol-4-alpha-carboxylate 3-dehydrogenase 1, decarboxylating;
GN Name=3BETAHSD/D1 {ECO:0000303|PubMed:16835224};
GN Synonyms=RTNLB24 {ECO:0000303|PubMed:17604024};
GN OrderedLocusNames=At1g47290 {ECO:0000312|Araport:AT1G47290};
GN ORFNames=T3F24.9 {ECO:0000312|EMBL:AAG11424.1};
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 [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Wassilewskija;
RX PubMed=16835224; DOI=10.1074/jbc.m604431200;
RA Rahier A., Darnet S., Bouvier F., Camara B., Bard M.;
RT "Molecular and enzymatic characterizations of novel bifunctional 3beta-
RT hydroxysteroid dehydrogenases/C-4 decarboxylases from Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 281:27264-27277(2006).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 2).
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 [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17604024; DOI=10.1016/j.febslet.2007.06.032;
RA Nziengui H., Bouhidel K., Pillon D., Der C., Marty F., Schoefs B.;
RT "Reticulon-like proteins in Arabidopsis thaliana: structural organization
RT and ER localization.";
RL FEBS Lett. 581:3356-3362(2007).
RN [8]
RP FUNCTION, MUTAGENESIS OF ASP-41; ASP-72; THR-131; SER-133; SER-135;
RP TYR-161; LYS-165; ARG-320 AND ARG-328, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CATALYTIC ACTIVITY.
RX PubMed=19218365; DOI=10.1104/pp.108.132282;
RA Rahier A., Bergdoll M., Genot G., Bouvier F., Camara B.;
RT "Homology modeling and site-directed mutagenesis reveal catalytic key amino
RT acids of 3beta-hydroxysteroid-dehydrogenase/C4-decarboxylase from
RT Arabidopsis.";
RL Plant Physiol. 149:1872-1886(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22673766; DOI=10.1007/s10059-012-0102-6;
RA Kim B., Kim G., Fujioka S., Takatsuto S., Choe S.;
RT "Overexpression of 3beta-hydroxysteroid dehydrogenases/C-4 decarboxylases
RT causes growth defects possibly due to abnormal auxin transport in
RT Arabidopsis.";
RL Mol. Cells 34:77-84(2012).
CC -!- FUNCTION: 3beta-hydroxysteroid-dehydrogenase/decarboxylase involved in
CC sterol synthesis (PubMed:16835224). Catalyzes the formation of 3-
CC oxosteroids from 3beta-hydroxysteroids-4alpha-carboxylate
CC (PubMed:16835224). Involved in the regulation of inflorescence
CC internodes and leaves growth, probably by affecting auxin transporter
CC activity possibly by altering sterol composition in the membranes
CC (PubMed:22673766). {ECO:0000269|PubMed:16835224,
CC ECO:0000269|PubMed:22673766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(+) = a 3-
CC oxosteroid + CO2 + NADH; Xref=Rhea:RHEA:34775, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:47788, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:136966; EC=1.1.1.418;
CC Evidence={ECO:0000269|PubMed:16835224, ECO:0000269|PubMed:19218365};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4alpha-carboxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-
CC ergost-24(24(1))-en-3beta-ol + NAD(+) = CO2 + cycloeucalenone + NADH;
CC Xref=Rhea:RHEA:59016, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:142915, ChEBI:CHEBI:142916;
CC EC=1.1.1.418; Evidence={ECO:0000269|PubMed:16835224,
CC ECO:0000269|PubMed:19218365};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for 4alpha-carboxy-5alpha-cholest-7-en-3beta-ol
CC {ECO:0000269|PubMed:19218365};
CC KM=0.26 mM for 4alpha-carboxy-4beta-methyl-5alpha-cholest-8,24-dien-
CC 3beta-ol {ECO:0000269|PubMed:19218365};
CC KM=134 uM for 4alpha-carboxy-cholest-7-en-3beta-ol
CC {ECO:0000269|PubMed:16835224};
CC KM=112 uM for 3alpha-deutero-4alpha-carboxy-cholest-7-en-3beta-ol
CC {ECO:0000269|PubMed:16835224};
CC KM=383 uM for 4alpha-carboxy-cholest-7-en-3alpha-ol
CC {ECO:0000269|PubMed:16835224};
CC KM=274 uM for 4alpha-carboxy-4beta-methyl-cholest-8,24-dien-3beta-ol
CC {ECO:0000269|PubMed:16835224};
CC KM=8 uM for NAD(+) {ECO:0000269|PubMed:16835224};
CC Vmax=88 nmol/h/mg enzyme with 4alpha-carboxy-5alpha-cholest-7-en-
CC 3beta-ol as substrate {ECO:0000269|PubMed:19218365};
CC Vmax=111 nmol/h/mg enzyme with 4alpha-carboxy-4beta-methyl-5alpha-
CC cholest-8,24-dien-3beta-ol as substrate
CC {ECO:0000269|PubMed:19218365};
CC Vmax=86 nmol/h/mg enzyme with 4alpha-carboxy-cholest-7-en-3beta-ol as
CC substrate {ECO:0000269|PubMed:16835224};
CC Vmax=77 nmol/h/mg enzyme with 3alpha-deutero-4alpha-carboxy-cholest-
CC 7-en-3beta-ol as substrate {ECO:0000269|PubMed:16835224};
CC Vmax=5.7 nmol/h/mg enzyme with 4alpha-carboxy-cholest-7-en-3alpha-ol
CC as substrate {ECO:0000269|PubMed:16835224};
CC Vmax=113 nmol/h/mg enzyme with 4alpha-carboxy-4beta-methyl-cholest-
CC 8,24-dien-3beta-ol as substrate {ECO:0000269|PubMed:16835224};
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 4/6. {ECO:0000269|PubMed:16835224}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O43050}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FX01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FX01-2; Sequence=VSP_037002;
CC -!- DOMAIN: The RETICULON domain is partial in comparison with the other
CC paralogs.
CC -!- DISRUPTION PHENOTYPE: No noticeable phenotype.
CC {ECO:0000269|PubMed:22673766}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
CC -!- CAUTION: Lacks one transmembrane, which is a conserved feature of the
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM62504.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAY28502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAM62504.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAY28502.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY957470; AAY28502.1; ALT_INIT; mRNA.
DR EMBL; AC015449; AAG11424.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32152.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32153.1; -; Genomic_DNA.
DR EMBL; AK117478; BAC42142.1; -; mRNA.
DR EMBL; BT005166; AAO50699.1; -; mRNA.
DR EMBL; AY085272; AAM62504.1; ALT_INIT; mRNA.
DR PIR; F96513; F96513.
DR RefSeq; NP_564502.1; NM_103623.5. [Q9FX01-2]
DR RefSeq; NP_849779.1; NM_179448.4. [Q9FX01-1]
DR AlphaFoldDB; Q9FX01; -.
DR SMR; Q9FX01; -.
DR BioGRID; 26357; 4.
DR IntAct; Q9FX01; 2.
DR STRING; 3702.Q9FX01; -.
DR GlyCosmos; Q9FX01; 3 sites, No reported glycans.
DR PaxDb; 3702-AT1G47290-2; -.
DR ProteomicsDB; 232129; -. [Q9FX01-1]
DR EnsemblPlants; AT1G47290.1; AT1G47290.1; AT1G47290. [Q9FX01-2]
DR EnsemblPlants; AT1G47290.2; AT1G47290.2; AT1G47290. [Q9FX01-1]
DR GeneID; 841132; -.
DR Gramene; AT1G47290.1; AT1G47290.1; AT1G47290. [Q9FX01-2]
DR Gramene; AT1G47290.2; AT1G47290.2; AT1G47290. [Q9FX01-1]
DR KEGG; ath:AT1G47290; -.
DR Araport; AT1G47290; -.
DR TAIR; AT1G47290; 3BETAHSD/D1.
DR eggNOG; KOG1430; Eukaryota.
DR InParanoid; Q9FX01; -.
DR OMA; TACARYY; -.
DR OrthoDB; 1133at2759; -.
DR PhylomeDB; Q9FX01; -.
DR BioCyc; ARA:AT1G47290-MONOMER; -.
DR BioCyc; MetaCyc:AT1G47290-MONOMER; -.
DR BRENDA; 1.1.1.418; 399.
DR UniPathway; UPA00770; UER00757.
DR PRO; PR:Q9FX01; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX01; baseline and differential.
DR Genevisible; Q9FX01; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR GO; GO:0102175; F:3-beta-hydroxysteroid dehydrogenase/C4-decarboxylase activity; IEA:RHEA.
DR GO; GO:0102191; F:4alpha-carboxy-5alpha-cholesta-7,24-dien-3beta-ol dehydrogenase/C4-decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0047012; F:sterol-4-alpha-carboxylate 3-dehydrogenase (decarboxylating) activity; IDA:TAIR.
DR GO; GO:0060918; P:auxin transport; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0032409; P:regulation of transporter activity; IMP:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd09813; 3b-HSD-NSDHL-like_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43245; BIFUNCTIONAL POLYMYXIN RESISTANCE PROTEIN ARNA; 1.
DR PANTHER; PTHR43245:SF51; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY 42E, MEMBER 2; 1.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NAD; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..439
FT /note="3beta-hydroxysteroid-dehydrogenase/decarboxylase
FT isoform 1"
FT /id="PRO_0000371279"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 371..439
FT /note="Reticulon; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 16..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT SITE 41
FT /note="Essential for the 3betaHSD/D activity"
FT /evidence="ECO:0000269|PubMed:19218365"
FT SITE 72
FT /note="Essential for the 3betaHSD/D activity"
FT /evidence="ECO:0000269|PubMed:19218365"
FT SITE 131
FT /note="Essential for the 3betaHSD/D activity"
FT /evidence="ECO:0000269|PubMed:19218365"
FT SITE 161
FT /note="Essential for the 3betaHSD/D activity"
FT /evidence="ECO:0000269|PubMed:19218365"
FT SITE 165
FT /note="Essential for the 3betaHSD/D activity"
FT /evidence="ECO:0000269|PubMed:19218365"
FT SITE 328
FT /note="Essential for the 3betaHSD/D activity"
FT /evidence="ECO:0000269|PubMed:19218365"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 371..427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16835224, ECO:0000303|Ref.6"
FT /id="VSP_037002"
FT MUTAGEN 41
FT /note="D->V: Lost activity."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 72
FT /note="D->A,V: Lost activity."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 131
FT /note="T->V: Lost activity."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 133
FT /note="S->A: Reduced activity with slower catalysis and
FT lower substrate binding."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 135
FT /note="S->A: Normal activity, but slower catalysis with
FT 4alpha-carboxysterol as substrate."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 135
FT /note="S->T: Altered activity due to reduced affinity and
FT catalysis and leading to lower amount of C4-demethylated
FT sterols and higher quantities of 4,4-dimethylated sterol
FT intermediates, and a higher ratio of 4,4-dimethylsterols to
FT 4alpha-methylsterols."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 135
FT /note="S->Y: Altered activity leading to an exclusive
FT production of C4-methylated sterols and 4alpha-carboxy-
FT 3beta-hydroxy sterols."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 161
FT /note="Y->F: Lost activity."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 165
FT /note="K->I: Lost activity."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 320
FT /note="R->I: Normal activity."
FT /evidence="ECO:0000269|PubMed:19218365"
FT MUTAGEN 328
FT /note="R->I: Lost activity."
FT /evidence="ECO:0000269|PubMed:19218365"
FT CONFLICT 49
FT /note="N -> D (in Ref. 6; AAM62504)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="S -> P (in Ref. 1; AAY28502)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="V -> F (in Ref. 6; AAM62504)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="K -> R (in Ref. 1; AAY28502)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48125 MW; C976A205FAFD87ED CRC64;
MVMEVTETER WCVVTGGRGF AARHLVEMLV RYQMFHVRIA DLAPAIVLNP HEETGILGEA
IRSGRVQYVS ADLRNKTQVV KGFQGAEVVF HMAAPDSSIN NHQLQYSVNV QGTTNVIDAC
IEVGVKRLIY TSSPSVVFDG VHGTLNADES LPYPPKHNDS YSATKAEGEA LILKANGRSG
LLTCCIRPSS IFGPGDKLMV PSLVTAARAG KSKFIIGDGS NFYDFTYVEN VVHAHVCAER
ALASGGEVCA KAAGQAYFIT NMEPIKFWEF MSQLLEGLGY ERPSIKIPAS LMMPIAYLVE
LAYKLLGPYG MKVPVLTPSR VRLLSCNRTF DSSKAKDRLG YSPVVPLQEG IKRTIDSFSH
LKAQNQPKTE VTETIQWKKQ TLIAIVILIT LYHNFVATTG SSSVIITAVS KVLLVSSIFM
FINGILPEKM KVFGSKKID
//
