HSD5_ARATH
ID HSD5_ARATH Reviewed; 389 AA.
AC Q9T0G0;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase-like 5;
DE EC=1.1.1.-;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase-like 5;
DE EC=1.1.1.-;
DE AltName: Full=Hydroxysteroid dehydrogenase 5;
DE Short=AtHSD5;
GN Name=HSD5; OrderedLocusNames=At4g10020; ORFNames=T5L19.150;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [4]
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 [5]
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 -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BT004103; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL049481; CAB39626.1; -; Genomic_DNA.
DR EMBL; AL161516; CAB78125.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82830.1; -; Genomic_DNA.
DR EMBL; BT004103; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T04006; T04006.
DR RefSeq; NP_192740.1; NM_117070.5.
DR AlphaFoldDB; Q9T0G0; -.
DR SMR; Q9T0G0; -.
DR BioGRID; 11892; 1.
DR STRING; 3702.AT4G10020.1; -.
DR PaxDb; Q9T0G0; -.
DR PRIDE; Q9T0G0; -.
DR ProteomicsDB; 228750; -.
DR EnsemblPlants; AT4G10020.1; AT4G10020.1; AT4G10020.
DR GeneID; 826593; -.
DR Gramene; AT4G10020.1; AT4G10020.1; AT4G10020.
DR KEGG; ath:AT4G10020; -.
DR Araport; AT4G10020; -.
DR TAIR; locus:2140553; AT4G10020.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; Q9T0G0; -.
DR OMA; SWYDIFL; -.
DR OrthoDB; 906746at2759; -.
DR PhylomeDB; Q9T0G0; -.
DR BioCyc; ARA:AT4G10020-MON; -.
DR PRO; PR:Q9T0G0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0G0; baseline and differential.
DR Genevisible; Q9T0G0; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Signal-anchor; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..389
FT /note="11-beta-hydroxysteroid dehydrogenase-like 5"
FT /id="PRO_0000422284"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 337..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 56..82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199..203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 43442 MW; FB9208B2C0A89C94 CRC64;
MVDLLNSVMN LVAPPATMVV MAFAWPLLSF ISFSERAYNS YFATENMEDK VVVITGASSA
IGEQIAYEYA KRGANLVLVA RREQRLRVVS NKAKQIGANH VIIIAADVIK EDDCRRFITQ
AVNYYGRVDH LVNTASLGHT FYFEEVSDTT VFPHLLDINF WGNVYPTYVA LPYLHQTNGR
IVVNASVENW LPLPRMSLYS AAKAALVNFY ETLRFELNGD VGITIATHGW IGSEMSGGKF
MLEEGAEMQW KEEREVPANG GPLEEFAKMI VAGACRGDAY VKFPNWYDVF LLYRVFTPNV
LRWTFKLLLS TEGTRRSSLV GVGSGMPVDE SSSQMKLMLE GGPPRVPASP PRYTASPPHY
TASPPRYPAS PPRYPASPPR FSQFNIQEL
