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 01-MAY-2013, entry version 91.
DE RecName: Full=Cytochrome P450 4V2;
DE EC=1.14.13.-;
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 MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND MASS
RP SPECTROMETRY.
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: Catalyzes the omega-hydroxylation of medium-chain
CC saturated fatty acids such as laurate, myristate and palmitate in
CC an NADPH-dependent pathway. The substrate specificity is higher
CC for myristate > laurate > palmitate (C14>C16>C12) (By similarity).
CC -!- COFACTOR: Heme group (By similarity).
CC -!- ENZYME REGULATION: Inhibited by N-hydroxy-N'-(4-n-butyl-2-
CC methylphenyl formamidine)(HET0016) (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein (Potential).
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; AB056457; BAB33032.1; -; mRNA.
DR EMBL; AK004724; BAB23507.1; -; mRNA.
DR IPI; IPI00120197; -.
DR RefSeq; NP_598730.1; NM_133969.2.
DR UniGene; Mm.245297; -.
DR ProteinModelPortal; Q9DBW0; -.
DR SMR; Q9DBW0; 62-520.
DR STRING; 10090.ENSMUSP00000092966; -.
DR PhosphoSite; Q9DBW0; -.
DR PaxDb; Q9DBW0; -.
DR PRIDE; Q9DBW0; -.
DR Ensembl; ENSMUST00000095328; ENSMUSP00000092966; ENSMUSG00000079057.
DR GeneID; 102294; -.
DR KEGG; mmu:102294; -.
DR CTD; 102294; -.
DR MGI; MGI:2142763; Cyp4v3.
DR eggNOG; COG2124; -.
DR GeneTree; ENSGT00660000095203; -.
DR HOVERGEN; HBG000182; -.
DR InParanoid; Q9DBW0; -.
DR KO; K07427; -.
DR OMA; LKLWVGP; -.
DR OrthoDB; EOG4VMFFC; -.
DR NextBio; 355392; -.
DR ArrayExpress; Q9DBW0; -.
DR Bgee; Q9DBW0; -.
DR Genevestigator; Q9DBW0; -.
DR GermOnline; ENSMUSG00000031640; Mus musculus.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; 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: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; Cytochrome_P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 525 Cytochrome P450 4V2.
FT /FTId=PRO_0000051861.
FT TRANSMEM 14 34 Helical; (Potential).
FT METAL 467 467 Iron (heme axial ligand) (By similarity).
FT BINDING 329 329 Heme (covalent; via 1 link) (By
FT similarity).
FT MOD_RES 403 403 Phosphoserine.
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
//
