NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=CB;
TISSUE=Bursa of Fabricius;
DOI=10.1186/gb-2004-6-1-r6; PubMed=15642098 [NCBI, ExPASy, EBI, Israel, Japan]
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis.";
Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005).

Comments

CATALYTIC ACTIVITY: 4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O₂ = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)⁺ + H₂O.
CATALYTIC ACTIVITY: 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O₂ = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)⁺ + 2 H₂O.
CATALYTIC ACTIVITY: 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + O₂ = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)⁺ + H₂O.
COFACTOR: Iron (By similarity).
PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 3/6 .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein (Probable).
DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding.
SIMILARITY: Belongs to the sterol desaturase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ719718; CAG31377.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001006438.1; -.

UniGene

Gga.21297

3D structure databases

ModBase

Q5ZLL6.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0000254;	Molecular function: C-4 methylsterol oxidase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0016126;	Biological process: sterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006088; Sterol_desatur.
Graphical view of domain structure.

Pfam

PF01598; Sterol_desat; 1.
Pfam graphical view of domain structure.

ProtoNet

Q5ZLL6.

Genome annotation databases

Ensembl

ENSGALG00000009560; Gallus gallus. [Contig view]

GeneID

422423; -.

KEGG

gga:422423; -.

Phylogenomic databases

HOVERGEN

Q5ZLL6; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Endoplasmic reticulum; Iron; Lipid synthesis; Membrane; NAD; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 296`	`296`	`C-4 methylsterol oxidase.`	`PRO_0000249852`
`TRANSMEM`	`55 75`	`21`	`Potential.`
`TRANSMEM`	`100 120`	`21`	`Potential.`
`TRANSMEM`	`199 219`	`21`	`Potential.`
`MOTIF`	`157 161`	`5`	`Histidine box-1 (By similarity).`
`MOTIF`	`170 174`	`5`	`Histidine box-2 (By similarity).`
`MOTIF`	`249 255`	`7`	`Histidine box-3 (By similarity).`

Sequence information

Length: 296 AA [This is the length of the unprocessed precursor]

Molecular weight: 35485 Da [This is the MW of the unprocessed precursor]

CRC64: 54144716232002A0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVNDSVNIL NSAYLAVEYI DSFLPDNPLQ QPFKNAWNYM LDNYTKFQIA TWGSLLVHEA 

        70         80         90        100        110        120 
SYFLLCVPGF IFQFIPYMQK YKIQPDKPET WEKQWKCFKT LIFNHFFIQL PLICGTYYFT 

       130        140        150        160        170        180 
EYFNIPYEWE EMPRWYVLLA QCFGCAVIED AWHYFLHRLL HHKRIYKYIH KVHHEFVSPF 

       190        200        210        220        230        240 
GMQAEYAHPL ETLILGAGFF IGIVVFCNHV VLLWAWVICR LMETIDVHSG YDIPLNPLHL 

       250        260        270        280        290 
VPFYAGARFH DFHHMNFIGN YASTFTWWDR IFGTDSQFIA YKEKEKKQQL RMKKTN

Q5ZLL6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools