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Protein

7-dehydrocholesterol reductase

Gene

dhcr7

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC).By similarity

Catalytic activityi

Cholesterol + NADP+ = cholesta-5,7-dien-3-beta-ol + NADPH.

Pathwayi: cholesterol biosynthesis

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei356NADPBy similarity1
Binding sitei360NADPBy similarity1
Binding sitei393NADP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei398NADPBy similarity1
Binding sitei445NADPBy similarity1
Binding sitei460NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi405 – 406NADPBy similarity2
Nucleotide bindingi449 – 453NADPBy similarity5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00063.

Names & Taxonomyi

Protein namesi
Recommended name:
7-dehydrocholesterol reductase (EC:1.3.1.21)
Short name:
7-DHC reductase
Alternative name(s):
Sterol Delta(7)-reductase
Gene namesi
Name:dhcr7
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei36 – 56HelicalSequence analysisAdd BLAST21
Transmembranei97 – 117HelicalSequence analysisAdd BLAST21
Transmembranei175 – 195HelicalSequence analysisAdd BLAST21
Transmembranei264 – 284HelicalSequence analysisAdd BLAST21
Transmembranei304 – 324HelicalSequence analysisAdd BLAST21
Transmembranei329 – 349HelicalSequence analysisAdd BLAST21
Transmembranei419 – 439HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002075061 – 4737-dehydrocholesterol reductaseAdd BLAST473

Structurei

3D structure databases

ProteinModelPortaliQ7ZXH1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ERG4/ERG24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG007825.
KOiK00213.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7ZXH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGERRRANAS RGDKKVANGE KQHVGQWGRA WEVDYFSLAS VIFLLAFAPL
60 70 80 90 100
IVYYFVMSCD QYQCALTAPV LDLYSGKARL SDIWDKTPAL TWTAVKIYLA
110 120 130 140 150
WVSFQVFLYM FLPDILHKFV PGYEGGVQEG ARTPAGLINK YQVNGLQAWT
160 170 180 190 200
ITHLLWFANA YHFHWFSPTI VIDNWIPLLW CANLLGYSVA TFALVKANFF
210 220 230 240 250
PTNANDCKFT GNFFYDYMMG IEFNPRIGKW FDFKLFFNGR PGIVAWTLIN
260 270 280 290 300
LSYAAKQQEL YGQVTNSMIL VNVLQAIYVV DFFWNESWYL KTIDICHDHF
310 320 330 340 350
GWYLGWGDCV WLPYLYTLQG LYLVYNPVEL STTAAVAVLL LGLIGYYIFR
360 370 380 390 400
MTNHQKDLFR RTNGNCKIWG KKPKSIECFY VSADGKRHYS KLMISGFWGV
410 420 430 440 450
ARHLNYTGDL MGSLAYCLAC GFDHLLPYFY FIYMTILLVH RCIRDEHRCS
460 470
SKYGKDWKLY TSAVPYRLLP GLF
Length:473
Mass (Da):54,823
Last modified:June 1, 2003 - v1
Checksum:i8EB14E8186BDC463
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC044995 mRNA. Translation: AAH44995.1.
RefSeqiNP_001079586.1. NM_001086117.1.
UniGeneiXl.2547.

Genome annotation databases

GeneIDi379273.
KEGGixla:379273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC044995 mRNA. Translation: AAH44995.1.
RefSeqiNP_001079586.1. NM_001086117.1.
UniGeneiXl.2547.

3D structure databases

ProteinModelPortaliQ7ZXH1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi379273.
KEGGixla:379273.

Organism-specific databases

CTDi1717.

Phylogenomic databases

HOVERGENiHBG007825.
KOiK00213.

Enzyme and pathway databases

UniPathwayiUPA00063.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHCR7_XENLA
AccessioniPrimary (citable) accession number: Q7ZXH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.