Cytochrome P450 11B1, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P15150 (C11B1_BOVIN)

Last modified May 26, 2009. Version 82. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cytochrome P450 11B1, mitochondrial
Alternative name(s):
    CYPXIB1
    P450C11
    Steroid 11-beta-hydroxylase
    EC=1.14.15.4

Gene names

Name:

CYP11B1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB.
Catalytic activity	A steroid + reduced adrenal ferredoxin + O₂ = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H₂O.
Cofactor	Heme group By similarity.
Subcellular location	Mitochondrion membrane.
Miscellaneous	The sequence shown is that of isozyme 11-beta-2.
Sequence similarities	Belongs to the cytochrome P450 family.

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Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism Steroidogenesis
Cellular component	Membrane Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	C21-steroid hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro steroid 11-beta-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 24

Mitochondrion

Chain

25 – 503

479

Cytochrome P450 11B1, mitochondrial

PRO_0000003594

Sites

Metal binding

450

Iron (heme axial ligand)

Natural variations

Natural variant

A → V in 11-beta-3.

Natural variant

S → G in 11-beta-3.

Natural variant

106

H → R in 11-beta-3.

Experimental info

Sequence conflict

191 – 192

SV → RL in AAA83383. Ref.3

Sequence conflict

337

Q → T Ref.4

Sequence conflict

337

Q → T Ref.5

Sequence conflict

347

A → P in AAA83383. Ref.3

Sequence conflict

502

I → Y in BAA00347. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P15150-1 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 9FBEEC132975FD72
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FASTA

503

57,847

        10         20         30         40         50         60 
MALWAKARVR MAGPWLSLHE ARLLGTRGAA APKAVLPFEA MPRCPGNKWM RMLQIWKEQS 

        70         80         90        100        110        120 
SENMHLDMHQ TFQELGPIFR YDVGGRHMVF VMLPEDVERL QQADSHHPQR MILEPWLAYR 

       130        140        150        160        170        180 
QARGHKCGVF LLNGPQWRLD RLRLNPDVLS LPALQKYTPL VDGVARDFSQ TLKARVLQNA 

       190        200        210        220        230        240 
RGSLTLDIAP SVFRYTIEAS TLVLYGERLG LLTQQPNPDS LNFIHALEAM LKSTVQLMFV 

       250        260        270        280        290        300 
PRRLSRWMST NMWREHFEAW DYIFQYANRA IQRIYQELAL GHPWHYSGIV AELLMRADMT 

       310        320        330        340        350        360 
LDTIKANTID LTAGSVDTTA FPLLMTLFEL ARNPEVQQAV RQESLVAEAR ISENPQRAIT 

       370        380        390        400        410        420 
ELPLLRAALK ETLRLYPVGI TLEREVSSDL VLQNYHIPAG TLVKVLLYSL GRNPAVFARP 

       430        440        450        460        470        480 
ESYHPQRWLD RQGSGSRFPH LAFGFGVRQC LGRRVAEVEM LLLLHHVLKN FLVETLEQED 

       490        500 
IKMVYRFILM PSTLPLFTFR AIQ

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References

[1]	"Molecular cloning and nucleotide sequence of DNA of mitochondrial cytochrome P-450(11 beta) of bovine adrenal cortex." Morohashi K., Yoshioka H., Gotoh O., Okada Y., Yamamoto K., Miyata T., Sogawa K., Fujii-Kuriyama Y., Omura T. J. Biochem. 102:559-568(1987) [PubMed: 3429448] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-2), PARTIAL PROTEIN SEQUENCE.
[2]	"Expression of two kinds of cytochrome P-450(11 beta) mRNA in bovine adrenal cortex." Kirita S., Morohashi K., Hashimoto T., Yoshioka H., Fujii-Kuriyama Y., Omura T. J. Biochem. 104:683-686(1988) [PubMed: 3266212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-3). Tissue: Adrenal cortex.
[3]	"Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11)." Chua S.C., Szabo P., Vitek A., Grzeschik K.H., John M., White P.C. Proc. Natl. Acad. Sci. U.S.A. 84:7193-7197(1987) [PubMed: 3499608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Cloning and characterization of bovine cytochrome P-450(11 beta) genes." Hashimoto T., Morohashi K., Omura T. J. Biochem. 105:676-679(1989) [PubMed: 2753866] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Structural analysis of multiple bovine P-450(11 beta) genes and their promoter activities." Kirita S., Hashimoto T., Kitajima M., Honda S., Morohashi K., Omura T. J. Biochem. 108:1030-1041(1990) [PubMed: 1965187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases
	D00185 mRNA. Translation: BAA00127.1. Sequence problems. D00361 mRNA. Translation: BAA00268.1. M17843 mRNA. Translation: AAA83383.1. D00455 Genomic DNA. Translation: BAA00347.1.
IPI	IPI00696443.
PIR	A28415. JX0071. JX0151.
RefSeq	NP_777063.2.
UniGene	Bt.4297
3D structure databases
HSSP	HSSP built from PDB template 1SCC based on UniProtKB P00189.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000026342. Bos taurus. [Contig view]
GeneID	282422.
KEGG	bta:282422.
Phylogenomic databases
HOVERGEN	P15150.
Enzyme and pathway databases
BRENDA	1.14.15.4. 251.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

C11B1_BOVIN

Accession

Primary (citable) accession number: P15150
Secondary accession number(s): Q29457

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 26, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents