HSD2_ARATH
ID HSD2_ARATH Reviewed; 308 AA.
AC Q9STY8;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase-like 2;
DE EC=1.1.1.-;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase-like 2;
DE EC=1.1.1.-;
DE AltName: Full=Hydroxysteroid dehydrogenase 2;
DE Short=AtHSD2;
GN Name=HSD2; OrderedLocusNames=At3g47350; ORFNames=T21L8.100;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP GENE FAMILY.
RX PubMed=17616511; DOI=10.1104/pp.107.100560;
RA Li F., Asami T., Wu X., Tsang E.W., Cutler A.J.;
RT "A putative hydroxysteroid dehydrogenase involved in regulating plant
RT growth and development.";
RL Plant Physiol. 145:87-97(2007).
RN [4]
RP GENE FAMILY.
RX PubMed=19542545; DOI=10.1093/pcp/pcp092;
RA Baud S., Dichow N.R., Kelemen Z., d'Andrea S., To A., Berger N.,
RA Canonge M., Kronenberger J., Viterbo D., Dubreucq B., Lepiniec L.,
RA Chardot T., Miquel M.;
RT "Regulation of HSD1 in seeds of Arabidopsis thaliana.";
RL Plant Cell Physiol. 50:1463-1478(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9STY8-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AL096860; CAB51207.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78268.1; -; Genomic_DNA.
DR PIR; T12990; T12990.
DR RefSeq; NP_190319.1; NM_114603.3. [Q9STY8-1]
DR AlphaFoldDB; Q9STY8; -.
DR SMR; Q9STY8; -.
DR STRING; 3702.AT3G47350.2; -.
DR PaxDb; Q9STY8; -.
DR PRIDE; Q9STY8; -.
DR ProteomicsDB; 232107; -. [Q9STY8-1]
DR EnsemblPlants; AT3G47350.1; AT3G47350.1; AT3G47350. [Q9STY8-1]
DR GeneID; 823889; -.
DR Gramene; AT3G47350.1; AT3G47350.1; AT3G47350. [Q9STY8-1]
DR KEGG; ath:AT3G47350; -.
DR Araport; AT3G47350; -.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; Q9STY8; -.
DR OMA; NHIGYSY; -.
DR PhylomeDB; Q9STY8; -.
DR BioCyc; ARA:AT3G47350-MON; -.
DR PRO; PR:Q9STY8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STY8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Signal-anchor; Steroid biosynthesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="11-beta-hydroxysteroid dehydrogenase-like 2"
FT /id="PRO_0000422280"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 53..79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196..200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 308 AA; 34684 MW; 3158C16CFEA8609D CRC64;
MDMLHTILNF LLPPLTISFL VLFYPFYLFT KLMSCLKHLH FENVTGKVVL ITGASSGIGE
HVAYEYAKKG AKLALVARRK DRLEIVAETS RQLGSGDVII IPGDVSNVED CKKFIDETIH
HFGKLDHLIN NAGVPQTVIF EDFTQIQDAN SIMDINFWGS TYITYFAIPH LRKSKGKIVV
ISSATAIIPL QAASVYSASK AALVKFFETL RVEISPDIKI TIALPGFIST DMTTPQFKEM
YGSDFILSES VSRCAKAIFR GIGRGEAYVI EPSWIKWIFL IKNVCPEIVD YLLDYIFVSY
LKPYFKRD
