DHB14_HUMAN
ID DHB14_HUMAN Reviewed; 270 AA.
AC Q9BPX1; Q9UKU3;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=17-beta-hydroxysteroid dehydrogenase 14 {ECO:0000305};
DE Short=17-beta-HSD 14;
DE EC=1.1.1.62 {ECO:0000269|PubMed:17067289};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase DHRS10;
DE AltName: Full=Dehydrogenase/reductase SDR family member 10;
DE AltName: Full=Retinal short-chain dehydrogenase/reductase retSDR3;
DE AltName: Full=Short chain dehydrogenase/reductase family 47C member 1;
GN Name=HSD17B14 {ECO:0000312|HGNC:HGNC:23238};
GN Synonyms=DHRS10, SDR3, SDR47C1; ORFNames=UNQ502/PRO474;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], LACK OF STEROID OR RETINOL DEHYDROGENASE
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10800688; DOI=10.1016/s0076-6879(00)16736-9;
RA Haeseleer F., Palczewski K.;
RT "Short-chain dehydrogenases/reductases in retina.";
RL Methods Enzymol. 316:372-383(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=17067289; DOI=10.1042/bj20061319;
RA Lukacik P., Keller B., Bunkoczi G., Kavanagh K., Hwa Lee W., Adamski J.,
RA Oppermann U.;
RT "Structural and biochemical characterization of human orphan DHRS10 reveals
RT a novel cytosolic enzyme with steroid dehydrogenase activity.";
RL Biochem. J. 402:419-427(2007).
CC -!- FUNCTION: Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase
CC activity. Converts oestradiol to oestrone. The physiological substrate
CC is not known. Acts on oestradiol and 5-androstene-3-beta,17-beta-diol
CC (in vitro). {ECO:0000269|PubMed:17067289}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH;
CC Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62;
CC Evidence={ECO:0000269|PubMed:17067289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613;
CC Evidence={ECO:0000305|PubMed:17067289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-en-3beta,17beta-diol + NAD(+) = 3beta-
CC hydroxyandrost-5-en-17-one + H(+) + NADH; Xref=Rhea:RHEA:46220,
CC ChEBI:CHEBI:2710, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:17067289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46221;
CC Evidence={ECO:0000305|PubMed:17067289};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17067289}.
CC -!- INTERACTION:
CC Q9BPX1; Q53H80: AKIRIN2; NbExp=3; IntAct=EBI-742664, EBI-742928;
CC Q9BPX1; Q9BX63: BRIP1; NbExp=3; IntAct=EBI-742664, EBI-3509650;
CC Q9BPX1; P35219: CA8; NbExp=14; IntAct=EBI-742664, EBI-718700;
CC Q9BPX1; P55273: CDKN2D; NbExp=8; IntAct=EBI-742664, EBI-745859;
CC Q9BPX1; P35638: DDIT3; NbExp=6; IntAct=EBI-742664, EBI-742651;
CC Q9BPX1; P35638-2: DDIT3; NbExp=3; IntAct=EBI-742664, EBI-10173632;
CC Q9BPX1; Q9BPX1: HSD17B14; NbExp=8; IntAct=EBI-742664, EBI-742664;
CC Q9BPX1; Q0VD86: INCA1; NbExp=3; IntAct=EBI-742664, EBI-6509505;
CC Q9BPX1; Q53S70: MGC4677; NbExp=3; IntAct=EBI-742664, EBI-10242717;
CC Q9BPX1; P29372: MPG; NbExp=4; IntAct=EBI-742664, EBI-1043398;
CC Q9BPX1; P29372-4: MPG; NbExp=3; IntAct=EBI-742664, EBI-10695618;
CC Q9BPX1; Q9HC98: NEK6; NbExp=3; IntAct=EBI-742664, EBI-740364;
CC Q9BPX1; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-742664, EBI-11750983;
CC Q9BPX1; Q96HA8: NTAQ1; NbExp=13; IntAct=EBI-742664, EBI-741158;
CC Q9BPX1; Q6ZVK8: NUDT18; NbExp=3; IntAct=EBI-742664, EBI-740486;
CC Q9BPX1; Q5T2D3: OTUD3; NbExp=3; IntAct=EBI-742664, EBI-16170539;
CC Q9BPX1; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-742664, EBI-12339509;
CC Q9BPX1; O43189: PHF1; NbExp=8; IntAct=EBI-742664, EBI-530034;
CC Q9BPX1; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-742664, EBI-79165;
CC Q9BPX1; Q9HB75-2: PIDD1; NbExp=3; IntAct=EBI-742664, EBI-12326369;
CC Q9BPX1; P25786: PSMA1; NbExp=3; IntAct=EBI-742664, EBI-359352;
CC Q9BPX1; Q04864-2: REL; NbExp=3; IntAct=EBI-742664, EBI-10829018;
CC Q9BPX1; Q92966: SNAPC3; NbExp=4; IntAct=EBI-742664, EBI-1760638;
CC Q9BPX1; P09234: SNRPC; NbExp=3; IntAct=EBI-742664, EBI-766589;
CC Q9BPX1; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-742664, EBI-10246938;
CC Q9BPX1; Q8N9Q2: SREK1IP1; NbExp=5; IntAct=EBI-742664, EBI-10268630;
CC Q9BPX1; Q9NU19: TBC1D22B; NbExp=7; IntAct=EBI-742664, EBI-8787464;
CC Q9BPX1; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-742664, EBI-10242677;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17067289}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, placenta, liver and
CC kidney. {ECO:0000269|PubMed:10800688, ECO:0000269|PubMed:17067289}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF126781; AAF06940.1; -; mRNA.
DR EMBL; AY358430; AAQ88796.1; -; mRNA.
DR EMBL; BC006294; AAH06294.1; -; mRNA.
DR EMBL; BC006283; AAH06283.1; -; mRNA.
DR CCDS; CCDS12736.1; -.
DR RefSeq; NP_057330.2; NM_016246.2.
DR PDB; 1YDE; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-270.
DR PDB; 5EN4; X-ray; 1.52 A; A=1-270.
DR PDB; 5HS6; X-ray; 2.02 A; A=1-270.
DR PDB; 5ICM; X-ray; 1.68 A; A=1-270.
DR PDB; 5ICS; X-ray; 1.52 A; A/C/D/F=1-270.
DR PDB; 5JS6; X-ray; 2.00 A; A=1-270.
DR PDB; 5JSF; X-ray; 1.84 A; A=1-270.
DR PDB; 5L7T; X-ray; 1.98 A; A=1-270.
DR PDB; 5L7W; X-ray; 1.76 A; A=1-270.
DR PDB; 5L7Y; X-ray; 1.91 A; A=1-270.
DR PDB; 5O42; X-ray; 1.76 A; A=1-270.
DR PDB; 5O43; X-ray; 1.50 A; A=1-270.
DR PDB; 5O6O; X-ray; 1.45 A; A=1-270.
DR PDB; 5O6X; X-ray; 1.35 A; A=1-270.
DR PDB; 5O6Z; X-ray; 1.57 A; A=1-270.
DR PDB; 5O72; X-ray; 1.91 A; A=1-270.
DR PDB; 5O7C; X-ray; 1.60 A; A=1-270.
DR PDB; 6EMM; X-ray; 2.47 A; A=1-270.
DR PDB; 6FFB; X-ray; 1.65 A; A=1-270.
DR PDB; 6G4L; X-ray; 1.44 A; A=1-270.
DR PDB; 6GBT; X-ray; 2.10 A; A=1-270.
DR PDB; 6GTB; X-ray; 1.62 A; A=1-270.
DR PDB; 6GTU; X-ray; 2.25 A; A=1-270.
DR PDB; 6H0M; X-ray; 1.25 A; A=1-270.
DR PDB; 6HNO; X-ray; 1.68 A; A=1-270.
DR PDB; 6QCK; X-ray; 1.68 A; A=1-270.
DR PDB; 6ZDE; X-ray; 1.87 A; A=1-270.
DR PDB; 6ZDI; X-ray; 2.13 A; A=1-270.
DR PDB; 6ZR6; X-ray; 1.50 A; A=1-270.
DR PDB; 6ZRA; X-ray; 1.73 A; A=1-270.
DR PDB; 6ZT2; X-ray; 1.95 A; A=1-270.
DR PDBsum; 1YDE; -.
DR PDBsum; 5EN4; -.
DR PDBsum; 5HS6; -.
DR PDBsum; 5ICM; -.
DR PDBsum; 5ICS; -.
DR PDBsum; 5JS6; -.
DR PDBsum; 5JSF; -.
DR PDBsum; 5L7T; -.
DR PDBsum; 5L7W; -.
DR PDBsum; 5L7Y; -.
DR PDBsum; 5O42; -.
DR PDBsum; 5O43; -.
DR PDBsum; 5O6O; -.
DR PDBsum; 5O6X; -.
DR PDBsum; 5O6Z; -.
DR PDBsum; 5O72; -.
DR PDBsum; 5O7C; -.
DR PDBsum; 6EMM; -.
DR PDBsum; 6FFB; -.
DR PDBsum; 6G4L; -.
DR PDBsum; 6GBT; -.
DR PDBsum; 6GTB; -.
DR PDBsum; 6GTU; -.
DR PDBsum; 6H0M; -.
DR PDBsum; 6HNO; -.
DR PDBsum; 6QCK; -.
DR PDBsum; 6ZDE; -.
DR PDBsum; 6ZDI; -.
DR PDBsum; 6ZR6; -.
DR PDBsum; 6ZRA; -.
DR PDBsum; 6ZT2; -.
DR AlphaFoldDB; Q9BPX1; -.
DR SMR; Q9BPX1; -.
DR BioGRID; 119350; 51.
DR IntAct; Q9BPX1; 28.
DR MINT; Q9BPX1; -.
DR STRING; 9606.ENSP00000263278; -.
DR BindingDB; Q9BPX1; -.
DR ChEMBL; CHEMBL3712868; -.
DR SwissLipids; SLP:000001216; -.
DR iPTMnet; Q9BPX1; -.
DR PhosphoSitePlus; Q9BPX1; -.
DR BioMuta; HSD17B14; -.
DR DMDM; 74752228; -.
DR EPD; Q9BPX1; -.
DR MassIVE; Q9BPX1; -.
DR PaxDb; Q9BPX1; -.
DR PeptideAtlas; Q9BPX1; -.
DR PRIDE; Q9BPX1; -.
DR ProteomicsDB; 78585; -.
DR Antibodypedia; 18422; 148 antibodies from 28 providers.
DR DNASU; 51171; -.
DR Ensembl; ENST00000263278.9; ENSP00000263278.3; ENSG00000087076.9.
DR GeneID; 51171; -.
DR KEGG; hsa:51171; -.
DR MANE-Select; ENST00000263278.9; ENSP00000263278.3; NM_016246.3; NP_057330.2.
DR UCSC; uc002pkv.2; human.
DR CTD; 51171; -.
DR DisGeNET; 51171; -.
DR GeneCards; HSD17B14; -.
DR HGNC; HGNC:23238; HSD17B14.
DR HPA; ENSG00000087076; Low tissue specificity.
DR MIM; 612832; gene.
DR neXtProt; NX_Q9BPX1; -.
DR OpenTargets; ENSG00000087076; -.
DR PharmGKB; PA162391674; -.
DR VEuPathDB; HostDB:ENSG00000087076; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000161346; -.
DR HOGENOM; CLU_010194_1_0_1; -.
DR InParanoid; Q9BPX1; -.
DR OMA; QHGKIDN; -.
DR OrthoDB; 1053465at2759; -.
DR PhylomeDB; Q9BPX1; -.
DR TreeFam; TF354307; -.
DR BRENDA; 1.1.1.62; 2681.
DR PathwayCommons; Q9BPX1; -.
DR Reactome; R-HSA-193144; Estrogen biosynthesis.
DR SignaLink; Q9BPX1; -.
DR BioGRID-ORCS; 51171; 5 hits in 1071 CRISPR screens.
DR ChiTaRS; HSD17B14; human.
DR EvolutionaryTrace; Q9BPX1; -.
DR GenomeRNAi; 51171; -.
DR Pharos; Q9BPX1; Tchem.
DR PRO; PR:Q9BPX1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BPX1; protein.
DR Bgee; ENSG00000087076; Expressed in mucosa of stomach and 155 other tissues.
DR ExpressionAtlas; Q9BPX1; baseline and differential.
DR Genevisible; Q9BPX1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IDA:HGNC-UCL.
DR GO; GO:0006706; P:steroid catabolic process; IDA:HGNC-UCL.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome; Steroid metabolism.
FT CHAIN 1..270
FT /note="17-beta-hydroxysteroid dehydrogenase 14"
FT /id="PRO_0000054654"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT VARIANT 31
FT /note="N -> D (in dbSNP:rs8110220)"
FT /id="VAR_052307"
FT VARIANT 130
FT /note="R -> W (in dbSNP:rs35299026)"
FT /id="VAR_052308"
FT CONFLICT 205
FT /note="T -> S (in Ref. 1; AAF06940)"
FT /evidence="ECO:0000305"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:6H0M"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:6H0M"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:6H0M"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:6H0M"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:6H0M"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 116..132
FT /evidence="ECO:0007829|PDB:6H0M"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 152..172
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6H0M"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:6H0M"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:6H0M"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:6H0M"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6H0M"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:6H0M"
SQ SEQUENCE 270 AA; 28317 MW; DAB68FB8CA422ABC CRC64;
MATGTRYAGK VVVVTGGGRG IGAGIVRAFV NSGARVVICD KDESGGRALE QELPGAVFIL
CDVTQEDDVK TLVSETIRRF GRLDCVVNNA GHHPPPQRPE ETSAQGFRQL LELNLLGTYT
LTKLALPYLR KSQGNVINIS SLVGAIGQAQ AVPYVATKGA VTAMTKALAL DESPYGVRVN
CISPGNIWTP LWEELAALMP DPRATIREGM LAQPLGRMGQ PAEVGAAAVF LASEANFCTG
IELLVTGGAE LGYGCKASRS TPVDAPDIPS
