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Protein

Very-long-chain 3-oxoacyl-CoA reductase

Gene

Hsd17b12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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

  • collagen binding Source: MGI
  • estradiol 17-beta-dehydrogenase activity Source: UniProtKB-EC
  • fibronectin binding Source: MGI
  • heparin binding Source: MGI

GO - Biological processi

  • estrogen biosynthetic process Source: UniProtKB-UniPathway
  • extracellular matrix organization Source: MGI
  • fatty acid biosynthetic process Source: UniProtKB-UniPathway
  • positive regulation of cell-substrate adhesion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

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

Chemistry

SwissLipidsiSLP:000000434.

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)
KIK-I
Gene namesi
Name:Hsd17b12Imported
Synonyms:Kik1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1926967. 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
Transmembranei269 – 28517HelicalSequence 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_0000054576Add
BLAST

Proteomic databases

EPDiO70503.
MaxQBiO70503.
PaxDbiO70503.
PRIDEiO70503.

PTM databases

iPTMnetiO70503.
PhosphoSiteiO70503.
SwissPalmiO70503.

Expressioni

Tissue specificityi

Expressed in most tissues tested.1 Publication

Gene expression databases

BgeeiO70503.
CleanExiMM_HSD17B12.
ExpressionAtlasiO70503. baseline and differential.
GenevisibleiO70503. MM.

Interactioni

GO - Molecular functioni

  • collagen binding Source: MGI
  • fibronectin binding Source: MGI

Protein-protein interaction databases

BioGridi207914. 2 interactions.
IntActiO70503. 5 interactions.
MINTiMINT-1863669.
STRINGi10090.ENSMUSP00000028619.

Structurei

3D structure databases

ProteinModelPortaliO70503.
SMRiO70503. Positions 53-257.
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.
HOGENOMiHOG000039237.
HOVERGENiHBG005478.
InParanoidiO70503.
KOiK10251.
OMAiLAEMGEW.
OrthoDBiEOG7CZK63.
PhylomeDBiO70503.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O70503-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MECAPPAAGF LYWVGASTIA YLALRASYSL FRAFQVWCVG NEALVGPRLG
60 70 80 90 100
EWAVVTGGTD GIGKAYAEEL AKRGMKIVLI SRSQDKLNQV SNNIKEKFNV
110 120 130 140 150
ETRTIAVDFS LDDIYDKIKT GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL
160 170 180 190 200
DNTIKKLINI NVLSVCKVTR LVLPGMVERS KGVILNISSA SGMLPVPLLT
210 220 230 240 250
IYSATKAFVD FFSQCLHEEY KSKGIFVQSV MPYLVATKLA KIQKPTLDKP
260 270 280 290 300
SAETFVKSAI KTVGLQTRTT GYVIHSLMGS INSIMPRWMY FKIIMGFSKS
310
LRNRYLKKRK KN
Length:312
Mass (Da):34,742
Last modified:August 1, 1998 - v1
Checksum:i7D255188FA1F8DDB
GO
Isoform 2 (identifier: O70503-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.

Note: No experimental confirmation available.
Show »
Length:177
Mass (Da):20,127
Checksum:iCAC34046DDAE3A0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21E → V in BAE39915 (PubMed:16141072).Curated
Sequence conflicti256 – 2561V → M in BAE29906 (PubMed:16141072).Curated
Sequence conflicti256 – 2561V → M in BAE31260 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 135135Missing in isoform 2. 1 PublicationVSP_020255Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064635 mRNA. Translation: AAC16885.1.
AK078841 mRNA. Translation: BAC37418.1.
AK081869 mRNA. Translation: BAC38354.1.
AK082715 mRNA. Translation: BAC38583.1.
AK088521 mRNA. Translation: BAC40401.1.
AK150849 mRNA. Translation: BAE29906.1.
AK152489 mRNA. Translation: BAE31260.1.
AK166027 mRNA. Translation: BAE38530.1.
AK167908 mRNA. Translation: BAE39915.1.
BC037620 mRNA. Translation: AAH37620.1.
CCDSiCCDS16458.1. [O70503-1]
RefSeqiNP_062631.1. NM_019657.4. [O70503-1]
UniGeneiMm.22505.

Genome annotation databases

EnsembliENSMUST00000028619; ENSMUSP00000028619; ENSMUSG00000027195. [O70503-1]
GeneIDi56348.
KEGGimmu:56348.
UCSCiuc008lgp.1. mouse. [O70503-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064635 mRNA. Translation: AAC16885.1.
AK078841 mRNA. Translation: BAC37418.1.
AK081869 mRNA. Translation: BAC38354.1.
AK082715 mRNA. Translation: BAC38583.1.
AK088521 mRNA. Translation: BAC40401.1.
AK150849 mRNA. Translation: BAE29906.1.
AK152489 mRNA. Translation: BAE31260.1.
AK166027 mRNA. Translation: BAE38530.1.
AK167908 mRNA. Translation: BAE39915.1.
BC037620 mRNA. Translation: AAH37620.1.
CCDSiCCDS16458.1. [O70503-1]
RefSeqiNP_062631.1. NM_019657.4. [O70503-1]
UniGeneiMm.22505.

3D structure databases

ProteinModelPortaliO70503.
SMRiO70503. Positions 53-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207914. 2 interactions.
IntActiO70503. 5 interactions.
MINTiMINT-1863669.
STRINGi10090.ENSMUSP00000028619.

Chemistry

SwissLipidsiSLP:000000434.

PTM databases

iPTMnetiO70503.
PhosphoSiteiO70503.
SwissPalmiO70503.

Proteomic databases

EPDiO70503.
MaxQBiO70503.
PaxDbiO70503.
PRIDEiO70503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028619; ENSMUSP00000028619; ENSMUSG00000027195. [O70503-1]
GeneIDi56348.
KEGGimmu:56348.
UCSCiuc008lgp.1. mouse. [O70503-1]

Organism-specific databases

CTDi51144.
MGIiMGI:1926967. Hsd17b12.

Phylogenomic databases

eggNOGiKOG1014. Eukaryota.
COG0300. LUCA.
HOGENOMiHOG000039237.
HOVERGENiHBG005478.
InParanoidiO70503.
KOiK10251.
OMAiLAEMGEW.
OrthoDBiEOG7CZK63.
PhylomeDBiO70503.
TreeFamiTF314591.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiHsd17b12. mouse.
NextBioi312340.
PROiO70503.
SOURCEiSearch...

Gene expression databases

BgeeiO70503.
CleanExiMM_HSD17B12.
ExpressionAtlasiO70503. baseline and differential.
GenevisibleiO70503. MM.

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. Gambotto A., Pagliano O., Robbins P., Deleo A.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/cJ.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: BALB/cJ, C57BL/6J and NOD.
    Tissue: Bone marrow, Cerebellum, Colon, Head, Lung and Thymus.
  3. "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] (ISOFORM 2).
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  4. "Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade."
    Moon Y.-A., Horton J.D.
    J. Biol. Chem. 278:7335-7343(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiDHB12_MOUSE
AccessioniPrimary (citable) accession number: O70503
Secondary accession number(s): Q3TID1
, Q3U7V9, Q542N3, Q8CI39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: April 13, 2016
This is version 138 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.