[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0167-4781(93)90281-H; PubMed=8439551 [NCBI, ExPASy, EBI, Israel, Japan] Nishimoto M., Noshiro M., Okuda K.; "Structure of the gene encoding human liver cholesterol 7 alpha-hydroxylase."; Biochim. Biophys. Acta 1172:147-150(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-347. DOI=10.1016/0014-5793(90)80992-R; PubMed=2384150 [NCBI, ExPASy, EBI, Israel, Japan] Noshiro M., Okuda K.; "Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7 alpha-hydroxylase."; FEBS Lett. 268:137-140(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-100. DOI=10.1016/0006-291X(92)91665-D; PubMed=1610352 [NCBI, ExPASy, EBI, Israel, Japan] Karam W.G., Chiang J.Y.; "Polymorphisms of human cholesterol 7 alpha-hydroxylase."; Biochem. Biophys. Res. Commun. 185:588-595(1992).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-140. TISSUE=Placenta; DOI=10.1006/geno.1994.1177; PubMed=8020987 [NCBI, ExPASy, EBI, Israel, Japan] Wang D.P., Chiang J.Y.; "Structure and nucleotide sequences of the human cholesterol 7 alpha-hydroxylase gene (CYP7)."; Genomics 20:320-323(1994).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25. DOI=10.1021/bi00124a014; PubMed=1312351 [NCBI, ExPASy, EBI, Israel, Japan] Molowa D.T., Chen W.S., Cimis G.M., Tan C.P.; "Transcriptional regulation of the human cholesterol 7 alpha-hydroxylase gene."; Biochemistry 31:2539-2544(1992).
[7]	VARIANTS SER-233 AND ASN-347. DOI=10.1007/s10038-003-0021-7; PubMed=12721789 [NCBI, ExPASy, EBI, Israel, Japan] Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., Nakamura Y.; "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population."; J. Hum. Genet. 48:249-270(2003).

Comments

CATALYTIC ACTIVITY: Cholesterol + NADPH + O₂ = 7-alpha-hydroxycholesterol + NADP⁺ + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Lipid metabolism; bile acid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
SIMILARITY: Belongs to the cytochrome P450 family.
WEB RESOURCE: Name=Wikipedia; Note=Cholesterol-7 alpha-hydroxylase entry; URL="http://en.wikipedia.org/wiki/Cholesterol_7_alpha-hydroxylase";.

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

X56088; CAA39568.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M93133; AAA58435.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101777; AAI01778.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112184; AAI12185.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L13460; AAA61350.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M89647; AAA58423.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S29818; JH0659.

NP_000771.2; -.

3D structure databases

PDB

3DAX; X-ray; 2.15 A; A/B=25-503.

[ExPASy / RCSB / EBI]

PDBsum

3DAX; -.

ModBase

P22680.

Enzyme and pathway databases

Reactome

REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

HGNC:2651; CYP7A1.

HPA010970; -.

118455; gene. [NCBI / EBI]

PharmGKB

PA132; -.

GeneCards

P22680.

Gene expression databases

ArrayExpress

P22680; -.

CleanEx

HS_CYP7A1; -.

GermOnline

ENSG00000167910; Homo sapiens.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0008123;	Molecular function: cholesterol 7-alpha-monooxygenase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002403; Cyt_P450_E_grp-IV.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00465; EP450IV.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

ProtoNet

P22680.

Genome annotation databases

Ensembl

ENSG00000167910; Homo sapiens. [Contig view]

GeneID

1581; -.

KEGG

hsa:1581; -.

Phylogenomic databases

HOGENOM

P22680; -.

HOVERGEN

P22680; -.

Other

NextBio

6495; -.

SOURCE

CYP7A1; Homo sapiens.

UniRef

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

Keywords

3D-structure; Cholesterol metabolism; Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Steroid metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 504`	`504`	`Cytochrome P450 7A1.`	`PRO_0000051901`
`METAL`	`444 444`		`Iron (heme axial ligand) (By similarity).`
`VARIANT`	`100 100`	`1`	`F -> S.`	`VAR_001259`
`VARIANT`	`233 233`	`1`	`N -> S.`	`VAR_018376`
`VARIANT`	`347 347`	`1`	`D -> N.`	`VAR_018377`
`CONFLICT`	`385 385`		`D -> S (in Ref. 2; CAA39568).`

Sequence information

Length: 504 AA [This is the length of the unprocessed precursor]

Molecular weight: 57661 Da [This is the MW of the unprocessed precursor]

CRC64: D8067E0FF6342949 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMTTSLIWGI AIAACCCLWL ILGIRRRQTG EPPLENGLIP YLGCALQFGA NPLEFLRANQ 

        70         80         90        100        110        120 
RKHGHVFTCK LMGKYVHFIT NPLSYHKVLC HGKYFDWKKF HFATSAKAFG HRSIDPMDGN 

       130        140        150        160        170        180 
TTENINDTFI KTLQGHALNS LTESMMENLQ RIMRPPVSSN SKTAAWVTEG MYSFCYRVMF 

       190        200        210        220        230        240 
EAGYLTIFGR DLTRRDTQKA HILNNLDNFK QFDKVFPALV AGLPIHMFRT AHNAREKLAE 

       250        260        270        280        290        300 
SLRHENLQKR ESISELISLR MFLNDTLSTF DDLEKAKTHL VVLWASQANT IPATFWSLFQ 

       310        320        330        340        350        360 
MIRNPEAMKA ATEEVKRTLE NAGQKVSLEG NPICLSQAEL NDLPVLDSII KESLRLSSAS 

       370        380        390        400        410        420 
LNIRTAKEDF TLHLEDGSYN IRKDDIIALY PQLMHLDPEI YPDPLTFKYD RYLDENGKTK 

       430        440        450        460        470        480 
TTFYCNGLKL KYYYMPFGSG ATICPGRLFA IHEIKQFLIL MLSYFELELI EGQAKCPPLD 

       490        500 
QSRAGLGILP PLNDIEFKYK FKHL

P22680 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