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Q4G1G8

- CH25H_PIG

UniProt

Q4G1G8 - CH25H_PIG

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Protein

Cholesterol 25-hydroxylase

Gene

CH25H

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes. May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing. In testis, production of 25-hydroxycholesterol by macrophages may play a role in Leydig cell differentiation (By similarity).By similarity

Catalytic activityi

Cholesterol + AH2 + O2 = 25-hydroxycholesterol + A + H2O.

Cofactori

Iron.By similarity

GO - Molecular functioni

  1. cholesterol 25-hydroxylase activity Source: UniProtKB-EC
  2. iron ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: InterPro
  2. sterol biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cholesterol 25-hydroxylase (EC:1.14.99.38)
Alternative name(s):
Cholesterol 25-monooxygenase
Gene namesi
Name:CH25H
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Cholesterol 25-hydroxylasePRO_0000226803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi5 – 51N-linked (GlcNAc...)Sequence Analysis
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011138.

Structurei

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei38 – 5821HelicalSequence AnalysisAdd
BLAST
Transmembranei81 – 10323HelicalSequence AnalysisAdd
BLAST
Transmembranei127 – 14721HelicalSequence AnalysisAdd
BLAST
Transmembranei167 – 18721HelicalSequence AnalysisAdd
BLAST
Transmembranei190 – 21021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi142 – 1465Histidine box-1
Motifi157 – 1615Histidine box-2
Motifi238 – 2447Histidine box-3

Sequence similaritiesi

Belongs to the sterol desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3000.
HOGENOMiHOG000015767.
HOVERGENiHBG080944.
InParanoidiQ4G1G8.

Family and domain databases

InterProiIPR006694. Fatty_acid_hydroxylase.
[Graphical view]
PfamiPF04116. FA_hydroxylase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4G1G8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGHNNSELF VLCSSSQLFL QPLWDHLKTW ETLILSPFFP VFFSITTYLG
60 70 80 90 100
FCLPFVVLDV LCPWVPALRR YKIHPDFSPS VWQLLPCLGL TLYQHVVFVF
110 120 130 140 150
PMTLLHWAAS PVLLPPEAPE LLQLVRHIVL CLLLFDTEFF IWHVLHHKVP
160 170 180 190 200
WLYRTFHKMH HQNSSSFALA TQYMSVGELL SLGVFDMVNI MLLRCHPLTV
210 220 230 240 250
LIFHVINIWL SVEDHSGYDF PWSAHRLVPF GWYGGVTHHD LHHSQFNCNF
260 270
APYFTHWDKI LGTLRSAHAK
Length:270
Mass (Da):31,482
Last modified:August 30, 2005 - v1
Checksum:i6BAEA05DBEAE1AA4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY974088 Genomic DNA. Translation: AAY40559.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY974088 Genomic DNA. Translation: AAY40559.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000011138.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3000.
HOGENOMi HOG000015767.
HOVERGENi HBG080944.
InParanoidi Q4G1G8.

Family and domain databases

InterProi IPR006694. Fatty_acid_hydroxylase.
[Graphical view ]
Pfami PF04116. FA_hydroxylase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and identification of a new single gene in pigs."
    Cheng H.C., Deng C.Y., Zhang F.W.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiCH25H_PIG
AccessioniPrimary (citable) accession number: Q4G1G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: August 30, 2005
Last modified: October 29, 2014
This is version 43 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3