DHB12_HUMAN
ID DHB12_HUMAN Reviewed; 312 AA.
AC Q53GQ0; A8K9B0; D3DR23; Q96EA9; Q96JU2; Q9Y6G8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305};
DE EC=1.1.1.330 {ECO:0000269|PubMed:12482854};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 12 {ECO:0000303|PubMed:16166196};
DE Short=17-beta-HSD 12 {ECO:0000303|PubMed:16166196};
DE AltName: Full=3-ketoacyl-CoA reductase {ECO:0000303|PubMed:12482854};
DE Short=KAR {ECO:0000303|PubMed:12482854};
DE AltName: Full=Estradiol 17-beta-dehydrogenase 12 {ECO:0000303|PubMed:16166196};
DE EC=1.1.1.62 {ECO:0000269|PubMed:16166196};
DE AltName: Full=Short chain dehydrogenase/reductase family 12C member 1;
GN Name=HSD17B12 {ECO:0000312|HGNC:HGNC:18646}; Synonyms=SDR12C1;
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] (ISOFORM 1).
RA Liu T., Zhang J., Fu G., Zhang Q., Ye M., Zhou J., Wu J., Shen Y., Yu M.,
RA Chen S., Mao M., Chen Z.;
RT "Human steroid dehydrogenase homologue, complete cds.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-280.
RC TISSUE=Liver, Placenta, Thymus, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-280.
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-280.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Pancreas;
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 [7]
RP PROTEIN SEQUENCE OF 26-35; 65-72; 104-117; 157-179 AND 207-221, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12482854; DOI=10.1074/jbc.m211684200;
RA Moon Y.-A., Horton J.D.;
RT "Identification of two mammalian reductases involved in the two-carbon
RT fatty acyl elongation cascade.";
RL J. Biol. Chem. 278:7335-7343(2003).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=16113833; DOI=10.1160/th05-01-0037;
RA Gnatenko D.V., Cupit L.D., Huang E.C., Dhundale A., Perrotta P.L.,
RA Bahou W.F.;
RT "Platelets express steroidogenic 17beta-hydroxysteroid dehydrogenases.
RT Distinct profiles predict the essential thrombocythemic phenotype.";
RL Thromb. Haemost. 94:412-421(2005).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF VAL-196 AND PHE-234.
RX PubMed=16166196; DOI=10.1210/me.2005-0058;
RA Luu-The V., Tremblay P., Labrie F.;
RT "Characterization of type 12 17beta-hydroxysteroid dehydrogenase, an
RT isoform of type 3 17beta-hydroxysteroid dehydrogenase responsible for
RT estradiol formation in women.";
RL Mol. Endocrinol. 20:437-443(2006).
RN [11]
RP INTERACTION WITH ELOVL1 AND LASS2.
RX PubMed=20937905; DOI=10.1073/pnas.1005572107;
RA Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y.,
RA Sassa T., Kihara A.;
RT "ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
RT synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Catalyzes the second of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of two carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has
CC a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-
CC hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby,
CC it may participate in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. May also catalyze
CC the transformation of estrone (E1) into estradiol (E2) and play a role
CC in estrogen formation. {ECO:0000269|PubMed:12482854,
CC ECO:0000269|PubMed:16166196}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-
CC long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330;
CC Evidence={ECO:0000269|PubMed:12482854};
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:16166196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62;
CC Evidence={ECO:0000269|PubMed:16166196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxooctadecanoyl-CoA + H(+) + NADPH = (3R)-
CC hydroxyoctadecanoyl-CoA + NADP(+); Xref=Rhea:RHEA:39151,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:71407, ChEBI:CHEBI:76374;
CC Evidence={ECO:0000269|PubMed:12482854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + H(+) + NADPH =
CC (3R)-hydroxy-(7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:39323, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:73852, ChEBI:CHEBI:76415;
CC Evidence={ECO:0000269|PubMed:12482854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + H(+) + NADPH
CC = (3R)-hydroxy-(7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:39459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:73863, ChEBI:CHEBI:76460;
CC Evidence={ECO:0000269|PubMed:12482854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + H(+) + NADPH = (3R)-
CC hydroxy-(8Z,11Z,14Z)-eicosatrienoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:39311, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:71481, ChEBI:CHEBI:76411;
CC Evidence={ECO:0000269|PubMed:12482854};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 uM for estrone {ECO:0000269|PubMed:16166196};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:12482854}.
CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC {ECO:0000269|PubMed:16166196}.
CC -!- SUBUNIT: Interacts with ELOVL1 and LASS2.
CC {ECO:0000269|PubMed:20937905}.
CC -!- INTERACTION:
CC Q53GQ0; P28329-3: CHAT; NbExp=3; IntAct=EBI-2963255, EBI-25837549;
CC Q53GQ0; P22607: FGFR3; NbExp=3; IntAct=EBI-2963255, EBI-348399;
CC Q53GQ0; P06396: GSN; NbExp=3; IntAct=EBI-2963255, EBI-351506;
CC Q53GQ0; P01112: HRAS; NbExp=3; IntAct=EBI-2963255, EBI-350145;
CC Q53GQ0; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-2963255, EBI-741480;
CC Q53GQ0; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-2963255, EBI-10173939;
CC Q53GQ0; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2963255, EBI-947187;
CC Q53GQ0; PRO_0000037541 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-2963255, EBI-6863754;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12482854}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12482854}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53GQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53GQ0-2; Sequence=VSP_056380, VSP_056381;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues tested. Highly expressed
CC in the ovary and mammary. Expressed in platelets.
CC {ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:16113833,
CC ECO:0000269|PubMed:16166196}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 17-beta-HSD 3 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK027882; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF078850; AAD44482.1; -; mRNA.
DR EMBL; AK027882; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK074952; BAG52039.1; -; mRNA.
DR EMBL; AK075216; BAG52086.1; -; mRNA.
DR EMBL; AK222881; BAD96601.1; -; mRNA.
DR EMBL; AK292625; BAF85314.1; -; mRNA.
DR EMBL; AC023085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68082.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68087.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68088.1; -; Genomic_DNA.
DR EMBL; BC012043; AAH12043.1; -; mRNA.
DR EMBL; BC012536; AAH12536.1; -; mRNA.
DR CCDS; CCDS7905.1; -. [Q53GQ0-1]
DR RefSeq; NP_057226.1; NM_016142.2. [Q53GQ0-1]
DR AlphaFoldDB; Q53GQ0; -.
DR SMR; Q53GQ0; -.
DR BioGRID; 119328; 176.
DR IntAct; Q53GQ0; 61.
DR MINT; Q53GQ0; -.
DR STRING; 9606.ENSP00000278353; -.
DR ChEMBL; CHEMBL5998; -.
DR SwissLipids; SLP:000000433; -.
DR GlyGen; Q53GQ0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q53GQ0; -.
DR PhosphoSitePlus; Q53GQ0; -.
DR SwissPalm; Q53GQ0; -.
DR BioMuta; HSD17B12; -.
DR DMDM; 158931120; -.
DR EPD; Q53GQ0; -.
DR jPOST; Q53GQ0; -.
DR MassIVE; Q53GQ0; -.
DR MaxQB; Q53GQ0; -.
DR PaxDb; Q53GQ0; -.
DR PeptideAtlas; Q53GQ0; -.
DR PRIDE; Q53GQ0; -.
DR ProteomicsDB; 62486; -. [Q53GQ0-1]
DR ProteomicsDB; 76390; -.
DR Antibodypedia; 3090; 206 antibodies from 24 providers.
DR DNASU; 51144; -.
DR Ensembl; ENST00000278353.10; ENSP00000278353.4; ENSG00000149084.13. [Q53GQ0-1]
DR Ensembl; ENST00000395700.4; ENSP00000379052.4; ENSG00000149084.13. [Q53GQ0-2]
DR GeneID; 51144; -.
DR KEGG; hsa:51144; -.
DR MANE-Select; ENST00000278353.10; ENSP00000278353.4; NM_016142.3; NP_057226.1.
DR UCSC; uc001mxq.5; human. [Q53GQ0-1]
DR CTD; 51144; -.
DR DisGeNET; 51144; -.
DR GeneCards; HSD17B12; -.
DR HGNC; HGNC:18646; HSD17B12.
DR HPA; ENSG00000149084; Low tissue specificity.
DR MIM; 609574; gene.
DR neXtProt; NX_Q53GQ0; -.
DR OpenTargets; ENSG00000149084; -.
DR PharmGKB; PA38618; -.
DR VEuPathDB; HostDB:ENSG00000149084; -.
DR eggNOG; KOG1014; Eukaryota.
DR GeneTree; ENSGT00940000154860; -.
DR HOGENOM; CLU_010194_38_0_1; -.
DR InParanoid; Q53GQ0; -.
DR OMA; FLQHWSS; -.
DR OrthoDB; 895581at2759; -.
DR PhylomeDB; Q53GQ0; -.
DR TreeFam; TF314591; -.
DR BioCyc; MetaCyc:HS07581-MON; -.
DR BRENDA; 1.1.1.62; 2681.
DR PathwayCommons; Q53GQ0; -.
DR Reactome; R-HSA-193048; Androgen biosynthesis.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SABIO-RK; Q53GQ0; -.
DR SignaLink; Q53GQ0; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00769; -.
DR BioGRID-ORCS; 51144; 362 hits in 1094 CRISPR screens.
DR ChiTaRS; HSD17B12; human.
DR GeneWiki; HSD17B12; -.
DR GenomeRNAi; 51144; -.
DR Pharos; Q53GQ0; Tbio.
DR PRO; PR:Q53GQ0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q53GQ0; protein.
DR Bgee; ENSG00000149084; Expressed in endothelial cell and 203 other tissues.
DR ExpressionAtlas; Q53GQ0; baseline and differential.
DR Genevisible; Q53GQ0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0009923; C:fatty acid elongase complex; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; EXP:Reactome.
DR GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..312
FT /note="Very-long-chain 3-oxoacyl-CoA reductase"
FT /id="PRO_0000248368"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 308..312
FT /note="Di-lysine motif"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 50..79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 95..98
FT /note="KEKF -> SNYT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056380"
FT VAR_SEQ 99..312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056381"
FT VARIANT 280
FT /note="S -> L (in dbSNP:rs11555762)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.5"
FT /id="VAR_027277"
FT MUTAGEN 196
FT /note="V->W: No effect."
FT /evidence="ECO:0000269|PubMed:16166196"
FT MUTAGEN 234
FT /note="F->A: Allows the conversion of androstenedione to
FT testosterone."
FT /evidence="ECO:0000269|PubMed:16166196"
SQ SEQUENCE 312 AA; 34324 MW; 8518336D7F514E50 CRC64;
MESALPAAGF LYWVGAGTVA YLALRISYSL FTALRVWGVG NEAGVGPGLG EWAVVTGSTD
GIGKSYAEEL AKHGMKVVLI SRSKDKLDQV SSEIKEKFKV ETRTIAVDFA SEDIYDKIKT
GLAGLEIGIL VNNVGMSYEY PEYFLDVPDL DNVIKKMINI NILSVCKMTQ LVLPGMVERS
KGAILNISSG SGMLPVPLLT IYSATKTFVD FFSQCLHEEY RSKGVFVQSV LPYFVATKLA
KIRKPTLDKP SPETFVKSAI KTVGLQSRTN GYLIHALMGS IISNLPSWIY LKIVMNMNKS
TRAHYLKKTK KN
