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3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1 (At3BETAHSD/D1) (EC 1.1.1.170) (4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-1) (Reticulon-like protein B24) (AtRTNLB24) (Sterol-4-alpha-carboxylate 3-dehydrogenase 1, decarboxylating)

 HSDD1_ARATH             Reviewed;         439 AA.
Q9FX01; Q0VH36; Q8LER8;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 109.
RecName: Full=3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1;
Short=At3BETAHSD/D1;
EC=1.1.1.170;
AltName: Full=4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-1;
AltName: Full=Reticulon-like protein B24;
Short=AtRTNLB24;
AltName: Full=Sterol-4-alpha-carboxylate 3-dehydrogenase 1, decarboxylating;
Name=3BETAHSD/D1; Synonyms=RTNLB24; OrderedLocusNames=At1g47290;
ORFNames=T3F24.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
STRAIN=cv. Wassilewskija;
PubMed=16835224; DOI=10.1074/jbc.M604431200;
Rahier A., Darnet S., Bouvier F., Camara B., Bard M.;
"Molecular and enzymatic characterizations of novel bifunctional
3beta-hydroxysteroid dehydrogenases/C-4 decarboxylases from
Arabidopsis thaliana.";
J. Biol. Chem. 281:27264-27277(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: A 3-beta-hydroxysteroid-4-alpha-carboxylate +
NAD(P)(+) = a 3-oxosteroid + CO(2) + NAD(P)H.
-!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
from lanosterol: step 4/6.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9FX01-1; Sequence=Displayed;
Name=2;
IsoId=Q9FX01-2; Sequence=VSP_037002;
Note=May be due to a competing acceptor splice site. No
experimental confirmation available. Ref.1 (AAY28502) sequence
differs from that shown due to erroneous initiation (Translation
N-terminally extended). Ref.6 (AAM62504) sequence differs from
that shown due to erroneous initiation (Translation N-terminally
extended). {ECO:0000305};
-!- DOMAIN: The RETICULON domain is partial in comparison with the
other paralogs.
-!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
-!- CAUTION: Lacks one transmembrane, which is a conserved feature of
the family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM62504.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAY28502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY957470; AAY28502.1; ALT_INIT; mRNA.
EMBL; AC015449; AAG11424.1; -; Genomic_DNA.
EMBL; CP002684; AEE32152.1; -; Genomic_DNA.
EMBL; CP002684; AEE32153.1; -; Genomic_DNA.
EMBL; AK117478; BAC42142.1; -; mRNA.
EMBL; BT005166; AAO50699.1; -; mRNA.
EMBL; AY085272; AAM62504.1; ALT_INIT; mRNA.
PIR; F96513; F96513.
RefSeq; NP_564502.1; NM_103623.5. [Q9FX01-2]
RefSeq; NP_849779.1; NM_179448.4. [Q9FX01-1]
UniGene; At.38654; -.
ProteinModelPortal; Q9FX01; -.
BioGrid; 26357; 2.
IntAct; Q9FX01; 2.
STRING; 3702.AT1G47290.2; -.
PaxDb; Q9FX01; -.
EnsemblPlants; AT1G47290.1; AT1G47290.1; AT1G47290. [Q9FX01-2]
EnsemblPlants; AT1G47290.2; AT1G47290.2; AT1G47290. [Q9FX01-1]
GeneID; 841132; -.
Gramene; AT1G47290.1; AT1G47290.1; AT1G47290.
Gramene; AT1G47290.2; AT1G47290.2; AT1G47290.
KEGG; ath:AT1G47290; -.
Araport; AT1G47290; -.
TAIR; locus:2203771; AT1G47290.
eggNOG; KOG1430; Eukaryota.
eggNOG; COG0451; LUCA.
HOGENOM; HOG000167989; -.
InParanoid; Q9FX01; -.
KO; K07748; -.
OMA; ESYPHLQ; -.
OrthoDB; EOG093609X1; -.
PhylomeDB; Q9FX01; -.
BioCyc; ARA:AT1G47290-MONOMER; -.
BioCyc; MetaCyc:AT1G47290-MONOMER; -.
Reactome; R-ATH-191273; Cholesterol biosynthesis.
UniPathway; UPA00770; UER00757.
PRO; PR:Q9FX01; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q9FX01; AT.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
GO; GO:0103066; F:4alpha-carboxy-4beta-methyl-5alpha-cholesta-8-en-3beta-ol:NAD(P)+ 3-oxidoreductase (decarboxylating) activity; IEA:UniProtKB-EC.
GO; GO:0103067; F:4alpha-carboxy-5alpha-cholesta-8-en-3beta-ol:NAD(P)+ 3-dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
GO; GO:0047012; F:sterol-4-alpha-carboxylate 3-dehydrogenase (decarboxylating) activity; IDA:TAIR.
GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF01073; 3Beta_HSD; 1.
SUPFAM; SSF51735; SSF51735; 2.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Lipid biosynthesis; Lipid metabolism; Membrane; NAD; Oxidoreductase;
Reference proteome; Steroid biosynthesis; Steroid metabolism;
Sterol biosynthesis; Sterol metabolism; Transmembrane;
Transmembrane helix.
CHAIN 1 439 3beta-hydroxysteroid-
dehydrogenase/decarboxylase isoform 1.
/FTId=PRO_0000371279.
TRANSMEM 381 401 Helical. {ECO:0000255}.
TRANSMEM 405 425 Helical. {ECO:0000255}.
DOMAIN 371 439 Reticulon; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00170}.
ACT_SITE 161 161 Proton acceptor. {ECO:0000250}.
BINDING 165 165 NAD. {ECO:0000250}.
VAR_SEQ 371 427 Missing (in isoform 2).
{ECO:0000303|PubMed:16835224,
ECO:0000303|Ref.6}.
/FTId=VSP_037002.
CONFLICT 49 49 N -> D (in Ref. 6; AAM62504).
{ECO:0000305}.
CONFLICT 70 70 S -> P (in Ref. 1; AAY28502).
{ECO:0000305}.
CONFLICT 228 228 V -> F (in Ref. 6; AAM62504).
{ECO:0000305}.
CONFLICT 336 336 K -> R (in Ref. 1; AAY28502).
{ECO:0000305}.
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


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