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Database: UniProt
Entry: Q9DBW0
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ID   CP4V2_MOUSE             Reviewed;         525 AA.
AC   Q9DBW0;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   26-NOV-2014, entry version 105.
DE   RecName: Full=Cytochrome P450 4V2;
DE            EC=1.14.13.-;
DE   AltName: Full=Docosahexaenoic acid omega-hydroxylase CYP4V2 {ECO:0000305};
DE            EC=1.14.13.199 {ECO:0000250|UniProtKB:Q6ZWL3};
GN   Name=Cyp4v2; Synonyms=Cyp4v3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Fujita Y., Kase K., Ohi H.;
RT   "Mouse mRNA for cytochrome P450, cDNA clone KK-1.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
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   [3]
RP   PROTEIN SEQUENCE OF 472-478, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Omega-hydroxylase that oxidizes medium-chain saturated
CC       fatty acids and polyunsaturated omega-3 fatty acids, and which
CC       plays a role in fatty acid and steroid metabolism in the eye.
CC       Catalyzes the omega-hydroxylation of medium-chain saturated fatty
CC       acids such as laurate, myristate and palmitate in an NADPH-
CC       dependent pathway. The substrate specificity is higher for
CC       myristate > laurate > palmitate (C14>C16>C12). Acts as a
CC       polyunsaturated omega-3 fatty acids hydroxylase by mediating
CC       oxidation of docosahexaenoate (DHA) to 22-hydroxydocosahexaenoate.
CC       Also produces some 21-hydroxydocosahexaenoate. Also converts
CC       eicosapentaenoate (EPA) to 20-hydroxyeicosapentaenoate (20-OH-
CC       EPA). {ECO:0000250|UniProtKB:Q6ZWL3}.
CC   -!- CATALYTIC ACTIVITY: Docosahexaenoate + NADPH + O(2) = 22-
CC       hydroxydocosahexaenoate + NADP(+) + H(2)O.
CC       {ECO:0000250|UniProtKB:Q6ZWL3}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P51869};
CC   -!- ENZYME REGULATION: Inhibited by N-hydroxy-N'-(4-n-butyl-2-
CC       methylphenyl formamidine)(HET0016) with an IC(50) of 38 nM.
CC       {ECO:0000250|UniProtKB:Q6ZWL3}.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q6ZWL3}; Single-pass membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB056457; BAB33032.1; -; mRNA.
DR   EMBL; AK004724; BAB23507.1; -; mRNA.
DR   CCDS; CCDS22276.1; -.
DR   RefSeq; NP_598730.1; NM_133969.2.
DR   UniGene; Mm.245297; -.
DR   ProteinModelPortal; Q9DBW0; -.
DR   SMR; Q9DBW0; 62-520.
DR   MINT; MINT-1863146; -.
DR   STRING; 10090.ENSMUSP00000092966; -.
DR   PhosphoSite; Q9DBW0; -.
DR   MaxQB; Q9DBW0; -.
DR   PaxDb; Q9DBW0; -.
DR   PRIDE; Q9DBW0; -.
DR   Ensembl; ENSMUST00000095328; ENSMUSP00000092966; ENSMUSG00000079057.
DR   GeneID; 102294; -.
DR   KEGG; mmu:102294; -.
DR   UCSC; uc009lou.1; mouse.
DR   CTD; 102294; -.
DR   MGI; MGI:2142763; Cyp4v3.
DR   eggNOG; COG2124; -.
DR   GeneTree; ENSGT00760000118816; -.
DR   HOVERGEN; HBG000182; -.
DR   InParanoid; Q9DBW0; -.
DR   KO; K07427; -.
DR   OMA; MSEMIFR; -.
DR   PhylomeDB; Q9DBW0; -.
DR   TreeFam; TF105088; -.
DR   NextBio; 355392; -.
DR   PRO; PR:Q9DBW0; -.
DR   Bgee; Q9DBW0; -.
DR   ExpressionAtlas; Q9DBW0; baseline and differential.
DR   Genevestigator; Q9DBW0; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0010430; P:fatty acid omega-oxidation; ISS:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
KW   Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Monooxygenase;
KW   NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    525       Cytochrome P450 4V2.
FT                                /FTId=PRO_0000051861.
FT   TRANSMEM     14     34       Helical. {ECO:0000255}.
FT   METAL       467    467       Iron (heme axial ligand).
FT                                {ECO:0000250|UniProtKB:P51869}.
FT   BINDING     329    329       Heme (covalent; via 1 link).
FT                                {ECO:0000250|UniProtKB:P51869}.
SQ   SEQUENCE   525 AA;  60939 MW;  71BB341589BD10A6 CRC64;
     MLWLWLGLSG QKLLLWGAAS AVSLAGATIL ISIFPMLVSY ARKWQQMRSI PSVARAYPLV
     GHALYMKPNN AEFFQQLIYY TEEFRHLPII KLWIGPVPLV ALYKAENVEV ILTSSKQIDK
     SFLYKFLQPW LGLGLLTSTG SKWRTRRKML TPTFHFTILE NFLDVMNEQA NILVNKLEKH
     VNQEAFNCFF YITLCALDII CETAMGKNIG AQSNNDSEYV RTVYRMSDMI YRRMKMPWLW
     FDLWYLVFKE GRDHKRGLKC LHTFTNNVIA ERVKERKAEE DWTGAGRGPI PSKNKRKAFL
     DLLLSVTDEE GNRLSQEDIR EEVDTFMFEG HDTTAAAINW SLYLLGTNPE VQRKVDQELD
     EVFGRSHRPV TLEDLKKLKY LDCVIKETLR VFPSVPLFAR SLSEDCEVGG YKVTKGTEAI
     IIPYALHRDP RYFPDPEEFR PERFFPENSQ GRHPYAYVPF SAGPRNCIGQ KFAVMEEKTI
     LACILRQFWV ESNQKREELG LAGDLILRPN NGIWIKLKRR HEDDP
//
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