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[1]
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NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
DOI=10.1074/jbc.271.47.29922; PubMed=8939936 [NCBI, ExPASy, EBI, Israel, Japan]
White J.A.,
Guo Y.-D.,
Baetz K.,
Beckett-Jones B.,
Bonasoro J.,
Hsu K.E.,
Dilworth F.J.,
Jones G.,
Petkovich M.;
"Identification of the retinoic acid-inducible all-trans-retinoic acid 4-hydroxylase.";
J. Biol. Chem. 271:29922-29927(1996).
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- FUNCTION: Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of 4-hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA and 4-oxo-RA.
- COFACTOR: Heme group (By similarity).
- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
- INDUCTION: By retinoic acid.
- SIMILARITY: Belongs to the cytochrome P450 family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 492 AA [This is the length of the unprocessed precursor] |
Molecular weight: 56281 Da [This is the MW of the unprocessed precursor] |
CRC64: FD471435B2F30509 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MGLYTLMVTF LCTIVLPVLL FLAAVKLWEM LMIRRVDPNC RSPLPPGTMG LPFIGETLQL
70 80 90 100 110 120
ILQRRKFLRM KRQKYGCIYK THLFGNPTVR VMGADNVRQI LLGEHKLVSV QWPASVRTIL
130 140 150 160 170 180
GSDTLSNVHG VQHKNKKKAI MRAFSRDALE HYIPVIQQEV KSAIQEWLQK DSCVLVYPEM
190 200 210 220 230 240
KKLMFRIAMR ILLGFEPEQI KTDEQELVEA FEEMIKNLFS LPIDVPFSGL YRGLRARNFI
250 260 270 280 290 300
HSKIEENIRK KIQDDDNENE QKYKDALQLL IENSRRSDEP FSLQAMKEAA TELLFGGHET
310 320 330 340 350 360
TASTATSLVM FLGLNTEVVQ KVREEVQEKV EMGMYTPGKG LSMELLDQLK YTGCVIKETL
370 380 390 400 410 420
RINPPVPGGF RVALKTFELN GYQIPKGWNV IYSICDTHDV ADVFPNKEEF QPERFMSKGL
430 440 450 460 470 480
EDGSRFNYIP FGGGSRMCVG KEFAKVLLKI FLVELTQHCN WILSNGPPTM KTGPTIYPVD
490
NLPTKFTSYV RN
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P79739 in FASTA format |
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