ID   CP4AA_MOUSE             Reviewed;         509 AA.
AC   O88833; Q9DCS5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   26-MAY-2009, entry version 69.
DE   RecName: Full=Cytochrome P450 4A10;
DE   AltName: Full=CYPIVA10;
DE   AltName: Full=Lauric acid omega-hydroxylase;
DE            EC=1.14.15.3;
DE   AltName: Full=P450-LA-omega 1;
DE   AltName: Full=P452;
GN   Name=Cyp4a10; Synonyms=Cyp4a-10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   PubMed=8031839;
RA   Henderson C.J., Bammler T., Wolf C.R.;
RT   "Deduced amino acid sequence of a murine cytochrome P-450 Cyp4a
RT   protein: developmental and hormonal regulation in liver and kidney.";
RL   Biochim. Biophys. Acta 1200:182-190(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ddY; TISSUE=Liver;
RA   Yasumura N., Ikeda T.;
RT   "Polymorphism of cyp 4A10 sequence between C57BL/6 and ddY mouse.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC       monooxygenases. In liver microsomes, this enzyme is involved in an
CC       NADPH-dependent electron transport pathway. It oxidizes a variety
CC       of structurally unrelated compounds, including steroids, fatty
CC       acids, and xenobiotics.
CC   -!- CATALYTIC ACTIVITY: Octane + reduced rubredoxin + O(2) = 1-octanol
CC       + oxidized rubredoxin + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; X69296; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB018421; BAA33804.1; -; mRNA.
DR   EMBL; AK002528; BAB22165.1; -; mRNA.
DR   EMBL; BC010747; AAH10747.1; -; mRNA.
DR   EMBL; BC051049; AAH51049.1; -; mRNA.
DR   IPI; IPI00322218; -.
DR   PIR; S47553; S47553.
DR   UniGene; Mm.10742; -.
DR   Ensembl; ENSMUSG00000066072; Mus musculus.
DR   KEGG; mmu:13117; -.
DR   MGI; MGI:88611; Cyp4a10.
DR   HOGENOM; O88833; -.
DR   HOVERGEN; O88833; -.
DR   BRENDA; 1.14.15.3; 244.
DR   NextBio; 283142; -.
DR   ArrayExpress; O88833; -.
DR   Bgee; O88833; -.
DR   GermOnline; ENSMUSG00000066072; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:UniProtKB.
DR   GO; GO:0018685; F:alkane 1-monooxygenase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; TAS:UniProtKB.
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    509       Cytochrome P450 4A10.
FT                                /FTId=PRO_0000051815.
FT   METAL       456    456       Iron (heme axial ligand) (By similarity).
FT   BINDING     320    320       Heme (covalent; via 1 link) (By
FT                                similarity).
FT   CONFLICT     62     62       H -> L (in Ref. 1; X69296).
FT   CONFLICT     64     64       Q -> K (in Ref. 1; X69296 and 3;
FT                                BAB22165).
FT   CONFLICT     69     69       H -> Q (in Ref. 1; X69296 and 3;
FT                                BAB22165).
FT   CONFLICT    234    234       I -> N (in Ref. 1; X69296).
SQ   SEQUENCE   509 AA;  58339 MW;  0D679AC757D8EB10 CRC64;
     MSVSALSPTR FADSLSGFLQ VASVLGLLLL LVKAVQFYLH RQWLLKAFQQ FPSPPFHWFF
     GHEQFKGDHE LQEIVSCIEN FPSAFPRWFW GSKAYLTVYD PDYMKVILGR SDPKANGAYR
     LLAPWIGYGL LLLNGQPWFQ HRRMLTPAFH YDILKPYVKN MADSIRLMLD KWERLADQDS
     SIEIFQHISL MTLDTVMKCA FSHKGSVQVD GNYRTYLQAI GDLNNLFHSR VRNIFHQNDT
     IYKLSSNGRL AKQACQLAHD HTDGVIKLRK DQLQDEGELE KIKKKRRLDF LDILLFARME
     NGDSMSDKDL RAEVDTFMFE GHDTTASGVS WIFYALATHP DHQQRCREEV QSLLGDGSSI
     TWDHLDQIPY TTMCIKEALR LYPPVPGIVR ELSTSVTFPD GRSLPKGVQV TLSIYGLHHN
     PKVWPNPEVF DPSRFAPDSP RHSHSFLPFS GGARNCIGKQ FAMSELKVIV ALTLLRFELL
     PDPTRVPMPL ARLVLKSKNG IYLHLKKLH
//