HSDD2_ARATH
ID HSDD2_ARATH Reviewed; 564 AA.
AC Q67ZE1; O64845;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2 {ECO:0000303|PubMed:16835224};
DE Short=At3BETAHSD/D2 {ECO:0000303|PubMed:16835224};
DE EC=1.1.1.418 {ECO:0000269|PubMed:16835224};
DE AltName: Full=4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-2;
DE AltName: Full=Reticulon-like protein B19 {ECO:0000303|PubMed:17604024};
DE Short=AtRTNLB19 {ECO:0000303|PubMed:17604024};
DE AltName: Full=Sterol-4-alpha-carboxylate 3-dehydrogenase 2, decarboxylating;
GN Name=3BETAHSD/D2 {ECO:0000303|PubMed:16835224};
GN Synonyms=RTNLB19 {ECO:0000303|PubMed:17604024};
GN OrderedLocusNames=At2g26260 {ECO:0000312|Araport:AT2G26260};
GN ORFNames=T1D16.10 {ECO:0000312|EMBL:AAC14524.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=87 uM for 4alpha-carboxy-cholest-7-en-3beta-ol
CC {ECO:0000269|PubMed:16835224};
CC KM=81 uM for 3alpha-deutero-4alpha-carboxy-cholest-7-en-3beta-ol
CC {ECO:0000269|PubMed:16835224};
CC KM=655 uM for 4alpha-carboxy-cholest-7-en-3alpha-ol
CC {ECO:0000269|PubMed:16835224};
CC KM=204 uM for 4alpha-carboxy-4beta-methyl-cholest-8,24-dien-3beta-ol
CC {ECO:0000269|PubMed:16835224};
CC KM=3.1 uM for NAD(+) {ECO:0000269|PubMed:16835224};
CC Vmax=66 nmol/h/mg enzyme with 4alpha-carboxy-cholest-7-en-3beta-ol as
CC substrate {ECO:0000269|PubMed:16835224};
CC Vmax=60 nmol/h/mg enzyme with 3alpha-deutero-4alpha-carboxy-cholest-
CC 7-en-3beta-ol as substrate {ECO:0000269|PubMed:16835224};
CC Vmax=12 nmol/h/mg enzyme with 4alpha-carboxy-cholest-7-en-3alpha-ol
CC as substrate {ECO:0000269|PubMed:16835224};
CC Vmax=45 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=3;
CC Name=1;
CC IsoId=Q67ZE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q67ZE1-2; Sequence=VSP_037004, VSP_037005;
CC Name=3;
CC IsoId=Q67ZE1-3; Sequence=VSP_037003;
CC -!- DISRUPTION PHENOTYPE: No noticeable phenotype.
CC {ECO:0000269|PubMed:22673766}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX818951; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ302749; ABC17877.1; -; mRNA.
DR EMBL; AC004484; AAC14524.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07814.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07815.1; -; Genomic_DNA.
DR EMBL; BX818951; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK176177; BAD43940.1; -; mRNA.
DR PIR; C84658; C84658.
DR RefSeq; NP_001031422.1; NM_001036345.1. [Q67ZE1-3]
DR RefSeq; NP_180194.2; NM_128183.4. [Q67ZE1-1]
DR AlphaFoldDB; Q67ZE1; -.
DR SMR; Q67ZE1; -.
DR BioGRID; 2518; 2.
DR STRING; 3702.AT2G26260.1; -.
DR PaxDb; Q67ZE1; -.
DR PRIDE; Q67ZE1; -.
DR ProteomicsDB; 232130; -. [Q67ZE1-1]
DR EnsemblPlants; AT2G26260.1; AT2G26260.1; AT2G26260. [Q67ZE1-1]
DR EnsemblPlants; AT2G26260.2; AT2G26260.2; AT2G26260. [Q67ZE1-3]
DR GeneID; 817166; -.
DR Gramene; AT2G26260.1; AT2G26260.1; AT2G26260. [Q67ZE1-1]
DR Gramene; AT2G26260.2; AT2G26260.2; AT2G26260. [Q67ZE1-3]
DR KEGG; ath:AT2G26260; -.
DR Araport; AT2G26260; -.
DR TAIR; locus:2057786; AT2G26260.
DR eggNOG; KOG1430; Eukaryota.
DR InParanoid; Q67ZE1; -.
DR OMA; LTYGECD; -.
DR OrthoDB; 930591at2759; -.
DR PhylomeDB; Q67ZE1; -.
DR BioCyc; ARA:AT2G26260-MON; -.
DR BioCyc; MetaCyc:AT2G26260-MON; -.
DR BRENDA; 1.1.1.418; 399.
DR UniPathway; UPA00770; UER00757.
DR PRO; PR:Q67ZE1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q67ZE1; baseline and differential.
DR Genevisible; Q67ZE1; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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 InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003388; Reticulon.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR Pfam; PF02453; Reticulon; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS50845; RETICULON; 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..564
FT /note="3beta-hydroxysteroid-dehydrogenase/decarboxylase
FT isoform 2"
FT /id="PRO_0000371280"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 384..564
FT /note="Reticulon"
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 CARBOHYD 146
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 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_037003"
FT VAR_SEQ 384..390
FT /note="VADTLLW -> GMTIYFN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16835224"
FT /id="VSP_037004"
FT VAR_SEQ 391..564
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16835224"
FT /id="VSP_037005"
FT CONFLICT 277
FT /note="G -> E (in Ref. 4; BX818951)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="D -> N (in Ref. 4; BX818951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 61704 MW; 547055E7944E59A9 CRC64;
MSPAATETER WCVVTGGRGF AARHLVEMLV RYEMFCVRIA DLAPAIMLDP QEGNGVLDEG
LRSGRVQYIS ADLRDKSQVV KAFQGAEVVF HMAAPDSSIN NHQLQYSVNV QGTQNVIDAC
VDVGVKRLIY TSSPSVVFDG VHGILNGTES MAYPIKHNDS YSATKAEGEE LIMKANGRNG
LLTCCIRPSS IFGPGDRLLV PSLVAAARAG KSKFIIGDGN NLYDFTYVEN VAHAHVCAER
ALASGGDVST KAAGQAYFIT NMEPIKFWEF MSQLLDGLGY ERPSIKIPAF IMMPIAHLVE
LTYKVLGPYG MTVPQLTPSR VRLLSCSRTF DSTKAKDRLG YAPVVPLQEG IRRTIDSFSH
LTAGSQSKRE GPSKASRILG GGKVADTLLW KDLKQTLIAI FILISIYYNF VATGSTVVTA
LSKALLVASV FLFLHGILPE KIFGYTVEKI PASQFHLSKD SSHDLSLSVI SSWNTTVKAL
RSLCQGNDWS FFFKVVFVLL ALSLAGAISL HSIFVIGLPI AFLAFLVYEK KEQEIDSIVV
SFKSFACKHK SDVYEKLFGS KKHD
