Steroid 21-hydroxylase - Cyp21 - Mus musculus (Mouse)

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P03940 (CP21A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Steroid 21-hydroxylase
EC=1.14.99.10

Alternative name(s):
21-OHase
Cytochrome P-450c21
Cytochrome P450 21
Cytochrome P450 XXI
Cytochrome P450-C21

Gene names

Name:	Cyp21
Synonyms:	Cyp21a-1, Cyp21a1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Specifically catalyzes the 21-hydroxylation of steroids. Required for the adrenal synthesis of mineralocorticoids and glucocorticoids.
Catalytic activity	A C₂₁ steroid + (reduced NADPH--hemoprotein reductase) + O₂ = a 21-hydroxy-C(21)-steroid + (oxidized NADPH--hemoprotein reductase) + H₂O.
Cofactor	Heme group By similarity.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Domain	The leucine-rich hydrophobic amino acid N-terminal region probably helps to anchor the protein to the microsomal membrane.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Steroidogenesis
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Lipid-binding Metal-binding Steroid-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro steroid 21-monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-EC steroid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 487

487

Steroid 21-hydroxylase

PRO_0000051977

Regions

Region

334 – 350

Steroid-binding By similarity

Sites

Metal binding

420

Iron (heme axial ligand)

Experimental info

Sequence conflict

31 – 32

PP → LR in AAA37114. Ref.1

Sequence conflict

M → L in AAA37114. Ref.1

Sequence conflict

218

L → F in BAA31153. Ref.3

Sequence conflict

238

Q → R in BAA31153. Ref.3

Sequence conflict

238

Q → R in AAC05278. Ref.4

Sequence conflict

241

D → E in AAA37114. Ref.1

Sequence conflict

314

E → A in AAA37114. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P03940 [UniParc].

Last modified April 26, 2005. Version 3.
Checksum: CAD32B606004449F
Show »

FASTA

487

55,328

        10         20         30         40         50         60 
MLLPGLLLLL LLLAGTRWLW GQWKLRKLHL PPLAPGFLHF LQPNLPIYLL GLTQKLGPIY 

        70         80         90        100        110        120 
RIRLGMQDVV VLNSNRTIEE ALIQKWVDFA GRPHMLNGKM DLDLSLGDYS LMWKAHKKLS 

       130        140        150        160        170        180 
RSALMLGMRD SMEPLIEQLT QEFCERMRAQ AGTPVAIHKE FSFLTCSIIS CLTFGDKDST 

       190        200        210        220        230        240 
LVQTLHDCVQ DLLQAWNHWS IQILTIIPLL RFLPNPGLQK LKQIQESRDH IVKQQLKQHK 

       250        260        270        280        290        300 
DSLVAGQWKD MIDYMLQGVE KQRDGKDEER LHEGHVHMSV VDLFIGGTET TATTLSWAVA 

       310        320        330        340        350        360 
FLLHHPEIQK RLQEELDLKL GPGSQLLYRN RMQLPLLMAT IAEVLRLRPV VPLALPHRAT 

       370        380        390        400        410        420 
RASSISGYDI PKDMVIIPNI QGANLDEMVW ELPSKFWPDR FLEPGKNPRT PSFGCGARVC 

       430        440        450        460        470        480 
LGEPLARLEL FVVLARLLQA FTLLPPPDGT LPSLQPQPYA GINLPIPPFQ VRLQPRNLAP 


QDQGERP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence analysis of murine 21-hydroxylase genes: mutations affecting gene expression." Chaplin D.D., Galbraith L.J., Seidman J.G., White P.C., Parker K.L. Proc. Natl. Acad. Sci. U.S.A. 83:9601-9605(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The murine Slp gene: additional evidence that sex-limited protein has no biological function." Zepf N.E., Ogata R.T. J. Immunol. 147:2756-2763(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B10.WR.
[3]	"Mus musculus 5' truncated pseudogene of tenascin-X, steroid 21-hydroxylase (Cyp21), and sex-limited protein (Slp) genes, partial cds and complete sequences." Matsumoto K., Ikuta T. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6 X CBA.
[4]	"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse." Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L. Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 129.
[5]	"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].
[6]	"Liver mRNA probes disclose two cytochrome P-450 genes duplicated in tandem with the complement C4 loci of the mouse H-2S region." Amor M., Tosi M., Duponchel C., Steinmetz M., Meo T. Proc. Natl. Acad. Sci. U.S.A. 82:4453-4457(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-487.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M15009 Genomic DNA. Translation: AAA37114.1. M64933 Genomic DNA. Translation: AAA40118.1. AB015623 Genomic DNA. Translation: BAA31153.1. AF049850 Genomic DNA. Translation: AAC05278.1. BC127167 mRNA. Translation: AAI27168.1.
CCDS	CCDS28658.1.
PIR	A26660. S54785.
RefSeq	NP_034125.2. NM_009995.2.
UniGene	Mm.440407.
3D structure databases
ProteinModelPortal	P03940.
SMR	P03940. Positions 29-475.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000025223.
PTM databases
PhosphoSite	P03940.
Proteomic databases
MaxQB	P03940.
PRIDE	P03940.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025223; ENSMUSP00000025223; ENSMUSG00000024365.
GeneID	13079.
KEGG	mmu:13079.
UCSC	uc008cdo.2. mouse.
Organism-specific databases
CTD	13079.
MGI	MGI:88591. Cyp21a1.
Phylogenomic databases
eggNOG	COG2124.
GeneTree	ENSGT00750000117317.
HOVERGEN	HBG106944.
InParanoid	A0JP50.
KO	K00513.
OrthoDB	EOG7BCNBG.
PhylomeDB	P03940.
TreeFam	TF105095.
Gene expression databases
ArrayExpress	P03940.
Bgee	P03940.
Genevestigator	P03940.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
SUPFAM	SSF48264. SSF48264. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	283032.
PRO	P03940.
SOURCE	Search...

Entry information

Entry name

CP21A_MOUSE

Accession

Primary (citable) accession number: P03940
Secondary accession number(s): A0JP50

Q9QX14

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	April 26, 2005
Last modified:	July 9, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents