Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Very-long-chain 3-oxoacyl-CoA reductase

Gene

Hsd17b12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation.By similarity

Catalytic activityi

A very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ = a very-long-chain 3-oxoacyl-CoA + NADPH.By similarity
17-beta-estradiol + NAD(P)+ = estrone + NAD(P)H.By similarity

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Pathwayi: estrogen biosynthesis

This protein is involved in the pathway estrogen biosynthesis, which is part of Steroid biosynthesis.By similarity
View all proteins of this organism that are known to be involved in the pathway estrogen biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei189SubstrateBy similarity1
Active sitei202Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi50 – 79NADPBy similarityAdd BLAST30

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis
LigandNADP

Enzyme and pathway databases

ReactomeiR-RNO-193048 Androgen biosynthesis
R-RNO-75876 Synthesis of very long-chain fatty acyl-CoAs
UniPathwayiUPA00094
UPA00769

Names & Taxonomyi

Protein namesi
Recommended name:
Very-long-chain 3-oxoacyl-CoA reductaseCurated (EC:1.1.1.330By similarity)
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 12By similarity
Short name:
17-beta-HSD 12By similarity
3-ketoacyl-CoA reductaseBy similarity
Short name:
KARBy similarity
Estradiol 17-beta-dehydrogenase 12By similarity (EC:1.1.1.62By similarity)
Gene namesi
Name:Hsd17b12Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi708367 Hsd17b12

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei4 – 24HelicalSequence analysisAdd BLAST21
Transmembranei182 – 202HelicalSequence analysisAdd BLAST21
Transmembranei271 – 291HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002483701 – 312Very-long-chain 3-oxoacyl-CoA reductaseAdd BLAST312

Proteomic databases

PaxDbiQ6P7R8
PRIDEiQ6P7R8

PTM databases

iPTMnetiQ6P7R8
PhosphoSitePlusiQ6P7R8
SwissPalmiQ6P7R8

Expressioni

Gene expression databases

BgeeiENSRNOG00000009630
ExpressionAtlasiQ6P7R8 baseline and differential
GenevisibleiQ6P7R8 RN

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249879, 1 interactor
STRINGi10116.ENSRNOP00000012806

Structurei

3D structure databases

ProteinModelPortaliQ6P7R8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi308 – 312Di-lysine motifBy similarity5

Domaini

The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1014 Eukaryota
COG0300 LUCA
GeneTreeiENSGT00390000010069
HOGENOMiHOG000039237
HOVERGENiHBG005478
InParanoidiQ6P7R8
KOiK10251
OMAiYLVTSAM
OrthoDBiEOG091G06T2
PhylomeDBiQ6P7R8
TreeFamiTF314591

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PfamiView protein in Pfam
PF00106 adh_short, 1 hit
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

Sequencei

Sequence statusi: Complete.

Q6P7R8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERALPAAGF LYWVGASTIA YLTLRASYSL FRAFQVWCVG NQAFVGPRLG
60 70 80 90 100
EWAVVTGGTD GIGKSYAEEL AKRGMKIVLI SRSQDKLKEV SNNIKEKFNV
110 120 130 140 150
ETRTIAVDFS LDDIYDKIKT GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL
160 170 180 190 200
DNTIKKLINI NVLSICKVTR LVLPGMVERS KGVILNISSA SGMLPVPLLT
210 220 230 240 250
VYSATKAFVD FFSQCLHEEY KSKGIFVQSV LPFFVATKLA KIRKPTLDKP
260 270 280 290 300
SAETFVKSAI KTVGLQTRTT GYVIHAIMGS INSILPRWIY FKTIMGFNKS
310
LRNRYLKKTK KN
Length:312
Mass (Da):34,841
Last modified:July 5, 2004 - v1
Checksum:i8531943458EFC711
GO

Sequence cautioni

The sequence AAD00504 differs from that shown. Reason: Frameshift at position 272.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti236A → S in AAD00504 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81186 mRNA Translation: AAD00504.1 Frameshift.
BC061543 mRNA Translation: AAH61543.1
RefSeqiNP_114455.1, NM_032066.1
XP_006234661.1, XM_006234599.3
UniGeneiRn.203283

Genome annotation databases

EnsembliENSRNOT00000012806; ENSRNOP00000012806; ENSRNOG00000009630
GeneIDi84013
KEGGirno:84013
UCSCiRGD:708367 rat

Similar proteinsi

Entry informationi

Entry nameiDHB12_RAT
AccessioniPrimary (citable) accession number: Q6P7R8
Secondary accession number(s): Q9Z1B9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 5, 2004
Last modified: May 23, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health