ID   C11B1_PIG               Reviewed;         503 AA.
AC   Q29552;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   26-MAY-2009, entry version 51.
DE   RecName: Full=Cytochrome P450 11B1, mitochondrial;
DE   AltName: Full=CYPXIB1;
DE   AltName: Full=P450C11;
DE   AltName: Full=Steroid 11-beta-hydroxylase;
DE            EC=1.14.15.4;
DE   Flags: Precursor;
GN   Name=CYP11B1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RX   MEDLINE=95210125; PubMed=7696143; DOI=10.1016/0960-0760(94)00167-K;
RA   Sun T., Zhao Y., Nonaka Y., Okamoto M.;
RT   "Cloning and expression of cytochrome P450(11 beta) of porcine adrenal
RT   cortex.";
RL   J. Steroid Biochem. Mol. Biol. 52:227-232(1995).
CC   -!- FUNCTION: Converts 11-deoxycorticosterone to corticosterone and
CC       18-hydroxycorticosterone, and also produces aldosterone. May play
CC       a role in the biosynthesis of glucocorticoids as well as
CC       mineralocorticoids. In addition to this activity, the 18 or 19-
CC       hydroxylation of steroids and the aromatization of androstendione
CC       to estrone have also been ascribed to cytochrome P450 XIB.
CC   -!- CATALYTIC ACTIVITY: A steroid + reduced adrenal ferredoxin + O(2)
CC       = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D38590; BAA07600.1; -; mRNA.
DR   HSSP; P00189; 1SCC.
DR   HOVERGEN; Q29552; -.
DR   BRENDA; 1.14.15.4; 249.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IEA:EC.
DR   GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Mitochondrion; Monooxygenase;
KW   Oxidoreductase; Steroidogenesis; Transit peptide.
FT   TRANSIT       1     24       Mitochondrion (By similarity).
FT   CHAIN        25    503       Cytochrome P450 11B1, mitochondrial.
FT                                /FTId=PRO_0000003602.
FT   METAL       450    450       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   503 AA;  57340 MW;  4C40B1EEAAC49B05 CRC64;
     MAIWAKAEAW LAGPWLALNR ARTLGTRAVL APKGVLPFEA IPQFPGKKWM RVLQLWREQG
     FENNHLEMHQ TFQELGPIFR FDVGGRNMVL VMLPEDVERC QKVEGLHPQR DVPGPWLAYR
     HLRGHKCGVF LLNGPTWRLD RLQLNPGVLS LQAMQKFTPL VDGVARDFSQ ALRARVMQNA
     RGSLTLDIKP SIFRYTIEAS NLVLFGERLG LLAHQPNPES LDFIHALEVM FKSTVQLMFM
     PRSLSRWTST GTWKEHFEAW DCIFQYANKA IQRLYQELTL GHPWHYSGVV AELLTHANMT
     VDAIKANSID LTAGSVDTTA YPLLMTLFEL ARNPEVQQAL RQESLAAAAR ISENPQKAIT
     ELPLLRAALK ETLRLYPVGI FLDRCVTSDL VLQNYHIPAG TLVKVLLYSL GRNPAVFARP
     ERYHPQRWLD NQGSGTRFPH LAFGFGMRQC LGRRLAQVEM LLLLHHVLKN FLVETLVQED
     IKMIYRFIMT PSTLPLLTFR AIS
//