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Protein

Very-long-chain 3-oxoacyl-CoA reductase

Gene

Hsd17b12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 to 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei189 – 1891SubstrateBy similarity
Active sitei202 – 2021Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 7930NADPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi708367. Hsd17b12.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2421HelicalSequence analysisAdd
BLAST
Transmembranei182 – 20221HelicalSequence analysisAdd
BLAST
Transmembranei271 – 29121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Very-long-chain 3-oxoacyl-CoA reductasePRO_0000248370Add
BLAST

Proteomic databases

PaxDbiQ6P7R8.
PRIDEiQ6P7R8.

PTM databases

iPTMnetiQ6P7R8.
PhosphoSiteiQ6P7R8.
SwissPalmiQ6P7R8.

Expressioni

Gene expression databases

ExpressionAtlasiQ6P7R8. baseline and differential.
GenevisibleiQ6P7R8. RN.

Interactioni

Protein-protein interaction databases

BioGridi249879. 1 interaction.
MINTiMINT-4580655.
STRINGi10116.ENSRNOP00000012806.

Structurei

3D structure databases

ProteinModelPortaliQ6P7R8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi308 – 3125Di-lysine motifBy similarity

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.
OMAiLAEMGEW.
OrthoDBiEOG7CZK63.
PhylomeDBiQ6P7R8.
TreeFamiTF314591.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

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 AAD00504.1 differs from that shown. Reason: Frameshift at position 272. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361A → S in AAD00504 (Ref. 1) Curated

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_006234599.2.
UniGeneiRn.203283.

Genome annotation databases

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

Cross-referencesi

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_006234599.2.
UniGeneiRn.203283.

3D structure databases

ProteinModelPortaliQ6P7R8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249879. 1 interaction.
MINTiMINT-4580655.
STRINGi10116.ENSRNOP00000012806.

PTM databases

iPTMnetiQ6P7R8.
PhosphoSiteiQ6P7R8.
SwissPalmiQ6P7R8.

Proteomic databases

PaxDbiQ6P7R8.
PRIDEiQ6P7R8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51144.
RGDi708367. Hsd17b12.

Phylogenomic databases

eggNOGiKOG1014. Eukaryota.
COG0300. LUCA.
GeneTreeiENSGT00390000010069.
HOGENOMiHOG000039237.
HOVERGENiHBG005478.
InParanoidiQ6P7R8.
KOiK10251.
OMAiLAEMGEW.
OrthoDBiEOG7CZK63.
PhylomeDBiQ6P7R8.
TreeFamiTF314591.

Enzyme and pathway databases

UniPathwayiUPA00094.
UPA00769.
ReactomeiR-RNO-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiQ6P7R8.

Gene expression databases

ExpressionAtlasiQ6P7R8. baseline and differential.
GenevisibleiQ6P7R8. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Trzyna W.C., Gabbeta V., McHugh K.M.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary anterior lobe.

Entry informationi

Entry nameiDHB12_RAT
AccessioniPrimary (citable) accession number: Q6P7R8
Secondary accession number(s): Q9Z1B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 101 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.