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Protein

Cytochrome P450 11B1, mitochondrial

Gene

CYP11B1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

A steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11-beta- hydroxysteroid + 2 oxidized adrenodoxin + H2O.

Cofactori

hemeBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi450 – 4501Iron (heme axial ligand)

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. steroid 11-beta-monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. steroid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism, Steroidogenesis

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 11B1, mitochondrial
Alternative name(s):
CYPXIB1
Cytochrome P450C11
Steroid 11-beta-hydroxylase (EC:1.14.15.4)
Gene namesi
Name:CYP11B1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionAdd
BLAST
Chaini25 – 503479Cytochrome P450 11B1, mitochondrialPRO_0000003594Add
BLAST

Proteomic databases

PRIDEiP15150.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000037225.

Structurei

3D structure databases

ProteinModelPortaliP15150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP15150.
KOiK00497.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15150-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALWAKARVR MAGPWLSLHE ARLLGTRGAA APKAVLPFEA MPRCPGNKWM
60 70 80 90 100
RMLQIWKEQS SENMHLDMHQ TFQELGPIFR YDVGGRHMVF VMLPEDVERL
110 120 130 140 150
QQADSHHPQR MILEPWLAYR QARGHKCGVF LLNGPQWRLD RLRLNPDVLS
160 170 180 190 200
LPALQKYTPL VDGVARDFSQ TLKARVLQNA RGSLTLDIAP SVFRYTIEAS
210 220 230 240 250
TLVLYGERLG LLTQQPNPDS LNFIHALEAM LKSTVQLMFV PRRLSRWMST
260 270 280 290 300
NMWREHFEAW DYIFQYANRA IQRIYQELAL GHPWHYSGIV AELLMRADMT
310 320 330 340 350
LDTIKANTID LTAGSVDTTA FPLLMTLFEL ARNPEVQQAV RQESLVAEAR
360 370 380 390 400
ISENPQRAIT ELPLLRAALK ETLRLYPVGI TLEREVSSDL VLQNYHIPAG
410 420 430 440 450
TLVKVLLYSL GRNPAVFARP ESYHPQRWLD RQGSGSRFPH LAFGFGVRQC
460 470 480 490 500
LGRRVAEVEM LLLLHHVLKN FLVETLEQED IKMVYRFILM PSTLPLFTFR

AIQ
Length:503
Mass (Da):57,847
Last modified:November 1, 1990 - v2
Checksum:i9FBEEC132975FD72
GO

Sequence cautioni

The sequence BAA00127.1 differs from that shown. Reason: Frameshift at positions 186 and 192. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1922SV → RL in AAA83383. (PubMed:3499608)Curated
Sequence conflicti337 – 3371Q → T in BAA00347. (PubMed:2753866)Curated
Sequence conflicti337 – 3371Q → T no nucleotide entry (PubMed:1965187)Curated
Sequence conflicti347 – 3471A → P in AAA83383. (PubMed:3499608)Curated
Sequence conflicti502 – 5021I → Y in BAA00347. (PubMed:2753866)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti30 – 301A → V in 11-beta-3.
Natural varianti60 – 601S → G in 11-beta-3.
Natural varianti106 – 1061H → R in 11-beta-3.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00185 mRNA. Translation: BAA00127.1. Frameshift.
D00361 mRNA. Translation: BAA00268.1.
M17843 mRNA. Translation: AAA83383.1.
D00455 Genomic DNA. Translation: BAA00347.1.
PIRiA28415.
JX0071.
JX0151.
RefSeqiNP_777063.2. NM_174638.3.
UniGeneiBt.4297.

Genome annotation databases

GeneIDi282422.
KEGGibta:282422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00185 mRNA. Translation: BAA00127.1. Frameshift.
D00361 mRNA. Translation: BAA00268.1.
M17843 mRNA. Translation: AAA83383.1.
D00455 Genomic DNA. Translation: BAA00347.1.
PIRiA28415.
JX0071.
JX0151.
RefSeqiNP_777063.2. NM_174638.3.
UniGeneiBt.4297.

3D structure databases

ProteinModelPortaliP15150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000037225.

Chemistry

BindingDBiP15150.
ChEMBLiCHEMBL2927.

Proteomic databases

PRIDEiP15150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282422.
KEGGibta:282422.

Organism-specific databases

CTDi1584.

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP15150.
KOiK00497.

Miscellaneous databases

NextBioi20806202.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-3).
    Tissue: Adrenal cortex.
  3. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiC11B1_BOVIN
AccessioniPrimary (citable) accession number: P15150
Secondary accession number(s): Q29457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1990
Last modified: January 7, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown is that of isozyme 11-beta-2.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.