ID CP4S3_DROME Reviewed; 495 AA. AC Q9VXY0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 16-DEC-2008, entry version 64. DE RecName: Full=Probable cytochrome P450 4s3; DE EC=1.14.-.-; DE AltName: Full=CYPIVS3; GN Name=Cyp4s3; ORFNames=CG9081; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: May be involved in the metabolism of insect hormones and CC in the breakdown of synthetic insecticides (By similarity). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- INTERACTION: CC Q9W1K5-1:-; NbExp=1; IntAct=EBI-133844, EBI-212772; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein (Potential). Microsome membrane; Peripheral 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; AE014298; AAF48426.1; -; Genomic_DNA. DR RefSeq; NP_573003.2; -. DR UniGene; Dm.19710; -. DR HSSP; P14779; 1JPZ. DR DIP; DIP:19604N; -. DR IntAct; Q9VXY0; 1. DR Ensembl; CG9081; Drosophila melanogaster. DR GeneID; 32444; -. DR KEGG; dme:Dmel_CG9081; -. DR NMPDR; fig|7227.3.peg.17896; -. DR FlyBase; FBgn0030615; Cyp4s3. DR HOGENOM; Q9VXY0; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-001936-MON; -. DR NextBio; 778491; -. DR ArrayExpress; Q9VXY0; -. DR GermOnline; CG9081; Drosophila melanogaster. DR GO; GO:0005789; C:endoplasmic reticulum 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:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001128; Cyt_P450. 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 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase. FT CHAIN 1 495 Probable cytochrome P450 4s3. FT /FTId=PRO_0000051848. FT METAL 436 436 Iron (heme axial ligand) (By similarity). FT BINDING 307 307 Heme (covalent; via 1 link) (By FT similarity). SQ SEQUENCE 495 AA; 57189 MW; 4AE96B1BFF502891 CRC64; MSTLALVAFV LWAAFLRYLP KILNFLRLQR FAKTLPGPTI GELIANVKKG EILNWLKELR EKHGPVFRIW FGKDLMVMFT DPEDIKQLLG NNQLLTKSRN YELLEPWLGK GLLTNGGESW HRRRKLLTPG FHFRILSEFK EPMEENCRIL VRRLRTKANG ESFDIYPYIT LFALDAICET AMGIKKHAQL QSDSEYVQAV QSICRVMHKQ SFSFWQRLNV FFKHTKPGKE REAALKVLHD ETNRVIRLRR EQLIQERNEW KPEAEQDDVG AKRRLAFLDM LLLTQMEGGA ELSDTDIREE VDTFMFEGHD TTSSAIAFAL SLLSKNPDVQ QRAFEEASEL EGREKESMPY LEAVIKETLR IYPSVPFFSR KVLEDLEVGK LTVPKGASIS CLIYMLHRDP KNFPDPERFD PDRFLVNEKQ MHPFAFAAFS AGPRNCIGQK FAMLELKTSL AMLLRSYRFL PDKDHQPKPL AELVTKSGNG IRLRILPRDE NGTTA //