HSDD3_ARATH
ID HSDD3_ARATH Reviewed; 561 AA.
AC A9X4U2; O22856; Q94AR9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3;
DE Short=At3BETAHSD/D3;
DE EC=1.1.1.170;
DE AltName: Full=4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-3;
DE AltName: Full=Reticulon-like protein B20;
DE Short=AtRTNLB20;
DE AltName: Full=Sterol-4-alpha-carboxylate 3-dehydrogenase 3, decarboxylating;
GN Name=3BETAHSD/D3; Synonyms=RTNLB20; OrderedLocusNames=At2g43420;
GN ORFNames=T1O24.16;
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], AND FUNCTION.
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].
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].
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 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3beta-hydroxysteroid-4alpha-carboxylate + NADP(+) = a 3-
CC oxosteroid + CO2 + NADPH; Xref=Rhea:RHEA:34771, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:136966; EC=1.1.1.170;
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=1.1.1.170;
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 4/6.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR EMBL; DQ415280; ABD76542.1; -; mRNA.
DR EMBL; AC002335; AAB64337.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10266.1; -; Genomic_DNA.
DR EMBL; AK117930; BAC42568.1; -; mRNA.
DR EMBL; AY045841; AAK76515.1; -; mRNA.
DR PIR; H84865; H84865.
DR RefSeq; NP_565998.1; NM_129903.3.
DR AlphaFoldDB; A9X4U2; -.
DR SMR; A9X4U2; -.
DR BioGRID; 4279; 66.
DR IntAct; A9X4U2; 66.
DR STRING; 3702.AT2G43420.1; -.
DR PaxDb; A9X4U2; -.
DR PRIDE; A9X4U2; -.
DR ProteomicsDB; 230251; -.
DR EnsemblPlants; AT2G43420.1; AT2G43420.1; AT2G43420.
DR GeneID; 818943; -.
DR Gramene; AT2G43420.1; AT2G43420.1; AT2G43420.
DR KEGG; ath:AT2G43420; -.
DR Araport; AT2G43420; -.
DR TAIR; locus:2058223; AT2G43420.
DR eggNOG; KOG1430; Eukaryota.
DR HOGENOM; CLU_007383_6_8_1; -.
DR InParanoid; A9X4U2; -.
DR OMA; LAQGDDW; -.
DR OrthoDB; 930591at2759; -.
DR PhylomeDB; A9X4U2; -.
DR BioCyc; ARA:AT2G43420-MON; -.
DR UniPathway; UPA00770; UER00757.
DR PRO; PR:A9X4U2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; A9X4U2; baseline and differential.
DR Genevisible; A9X4U2; 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:0009506; C:plasmodesma; HDA: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:0103066; F:4alpha-carboxy-4beta-methyl-5alpha-cholesta-8-en-3beta-ol:NAD(P)+ 3-oxidoreductase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0103067; F:4alpha-carboxy-5alpha-cholesta-8-en-3beta-ol:NAD(P)+ 3-dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0000252; F:C-3 sterol dehydrogenase (C-4 sterol 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; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane; NAD;
KW Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..561
FT /note="3beta-hydroxysteroid-dehydrogenase/decarboxylase
FT isoform 3"
FT /id="PRO_0000371281"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 379..561
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT BINDING 166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="D -> G (in Ref. 1; ABD76542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 63033 MW; 484C8E9BB423F891 CRC64;
MDEDSVHGDS HLKTCVVLGG RGFIGRSLVS RLLRLGNWTV RVADSGHTLH LDESDSLLED
ALSSGRASYH CVDVRDKPQI VKVTEGSYVV FYMGATDLRS HDYFDCYKVI VQGTRNVISA
CRESGVRKLI YNSTADVVFD GSQPIRDGDE SLRRPLKFQS MLTDFKAQAE ALIKLANNRD
GLLTCALRSS IVFGPGDTEF VPFLVNLAKS GYAKFILGSG ENISDFTYSE NVSHAHICAV
KALDSQMEFV AGKEFFITNL KPVRFWDFVS HIVEGLGYPR PSIKLPVRLV LYVFSLLKWT
HEKEGLGSNY DTAHQYALLA SSTRTFNCNA AKKHLGYTPV VTLEDGIAST LQWFSRDLEK
SDDTIIQSTA DQLLGCGKVA DILLWRNEKK TFVSFLVLNL FYYWFFFSGN TFTSSAAQLL
FIFAVALYGV SFVPSKIFGF QVNKIPPWRF EISESAVRDL SSDIVVVWNQ GVRSFKSLSS
GGDWIKFFKI AGSLYLLKLI VSRSLAAFLF TVMSFSFTGF FIYEQYELEL YHLARIFVEC
LTFIKRMVIP VSDASSKPMF M
