ID   CP26A_DANRE             Reviewed;         492 AA.
AC   P79739;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   13-OCT-2009, entry version 66.
DE   RecName: Full=Cytochrome P450 26A1;
DE            EC=1.14.-.-;
DE   AltName: Full=Retinoic acid-metabolizing cytochrome;
DE   AltName: Full=P450RAI;
DE   AltName: Full=Retinoic acid 4-hydroxylase;
GN   Name=cyp26a1; Synonyms=cyp26;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX   MEDLINE=97094702; PubMed=8939936; DOI=10.1074/jbc.271.47.29922;
RA   White J.A., Guo Y.-D., Baetz K., Beckett-Jones B., Bonasoro J.,
RA   Hsu K.E., Dilworth F.J., Jones G., Petkovich M.;
RT   "Identification of the retinoic acid-inducible all-trans-retinoic acid
RT   4-hydroxylase.";
RL   J. Biol. Chem. 271:29922-29927(1996).
CC   -!- FUNCTION: Plays a key role in retinoic acid metabolism. Acts on
CC       retinoids, including all-trans-retinoic acid (RA) and its
CC       stereoisomer 9-cis-RA. Capable of 4-hydroxylation. Responsible for
CC       generation of several hydroxylated forms of RA, including 4-OH-RA
CC       and 4-oxo-RA.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By retinoic acid.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; U68234; AAC60045.1; -; mRNA.
DR   IPI; IPI00489219; -.
DR   UniGene; Dr.75754; -.
DR   STRING; P79739; -.
DR   Ensembl; ENSDART00000041728; ENSDARP00000041727; ENSDARG00000033999; Danio rerio.
DR   ZFIN; ZDB-GENE-990415-44; cyp26a1.
DR   HOGENOM; P79739; -.
DR   HOVERGEN; P79739; -.
DR   ArrayExpress; P79739; -.
DR   Bgee; P79739; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; 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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN         1    492       Cytochrome P450 26A1.
FT                                /FTId=PRO_0000051983.
FT   METAL       438    438       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   492 AA;  56281 MW;  FD471435B2F30509 CRC64;
     MGLYTLMVTF LCTIVLPVLL FLAAVKLWEM LMIRRVDPNC RSPLPPGTMG LPFIGETLQL
     ILQRRKFLRM KRQKYGCIYK THLFGNPTVR VMGADNVRQI LLGEHKLVSV QWPASVRTIL
     GSDTLSNVHG VQHKNKKKAI MRAFSRDALE HYIPVIQQEV KSAIQEWLQK DSCVLVYPEM
     KKLMFRIAMR ILLGFEPEQI KTDEQELVEA FEEMIKNLFS LPIDVPFSGL YRGLRARNFI
     HSKIEENIRK KIQDDDNENE QKYKDALQLL IENSRRSDEP FSLQAMKEAA TELLFGGHET
     TASTATSLVM FLGLNTEVVQ KVREEVQEKV EMGMYTPGKG LSMELLDQLK YTGCVIKETL
     RINPPVPGGF RVALKTFELN GYQIPKGWNV IYSICDTHDV ADVFPNKEEF QPERFMSKGL
     EDGSRFNYIP FGGGSRMCVG KEFAKVLLKI FLVELTQHCN WILSNGPPTM KTGPTIYPVD
     NLPTKFTSYV RN
//