CP255_MOUSE
ID CP255_MOUSE Reviewed; 490 AA.
AC Q9D816;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cytochrome P450 2C55;
DE EC=1.14.14.1 {ECO:0000269|PubMed:15102943};
DE AltName: Full=CYPIIC55;
GN Name=Cyp2c55 {ECO:0000312|MGI:MGI:1919332};
GN Synonyms=Cyp2c-55 {ECO:0000250|UniProtKB:P33273};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO52738.1};
RC TISSUE=Colon {ECO:0000269|PubMed:15102943};
RX PubMed=15102943; DOI=10.1124/mol.65.5.1148;
RA Wang H., Zhao Y., Bradbury J.A., Graves J.P., Foley J., Blaisdell J.A.,
RA Goldstein J.A., Zeldin D.C.;
RT "Cloning, expression, and characterization of three new mouse cytochrome
RT p450 enzymes and partial characterization of their fatty acid oxidation
RT activities.";
RL Mol. Pharmacol. 65:1148-1158(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB25759.1};
RC TISSUE=Small intestine {ECO:0000312|EMBL:BAB25759.1};
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH10824.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH10824.1};
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Metabolizes arachidonic acid mainly to 19-
CC hydroxyeicosatetraenoic acid (HETE). {ECO:0000269|PubMed:15102943}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000269|PubMed:15102943};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Highest level in colon. Low levels in liver and
CC small intestine. {ECO:0000269|PubMed:15102943}.
CC -!- INDUCTION: P450 can be induced to high levels in liver and other
CC tissues by various foreign compounds, including drugs, pesticides, and
CC carcinogens. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
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DR EMBL; AY206875; AAO52738.1; -; mRNA.
DR EMBL; AK008580; BAB25759.1; -; mRNA.
DR EMBL; BC010824; AAH10824.1; -; mRNA.
DR CCDS; CCDS29790.1; -.
DR RefSeq; NP_082365.1; NM_028089.3.
DR AlphaFoldDB; Q9D816; -.
DR SMR; Q9D816; -.
DR STRING; 10090.ENSMUSP00000025966; -.
DR iPTMnet; Q9D816; -.
DR PhosphoSitePlus; Q9D816; -.
DR jPOST; Q9D816; -.
DR MaxQB; Q9D816; -.
DR PaxDb; Q9D816; -.
DR PeptideAtlas; Q9D816; -.
DR PRIDE; Q9D816; -.
DR ProteomicsDB; 284109; -.
DR DNASU; 72082; -.
DR Ensembl; ENSMUST00000025966; ENSMUSP00000025966; ENSMUSG00000025002.
DR GeneID; 72082; -.
DR KEGG; mmu:72082; -.
DR UCSC; uc008hju.1; mouse.
DR CTD; 72082; -.
DR MGI; MGI:1919332; Cyp2c55.
DR VEuPathDB; HostDB:ENSMUSG00000025002; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000162913; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; Q9D816; -.
DR OMA; VVAKPHF; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9D816; -.
DR TreeFam; TF352043; -.
DR Reactome; R-MMU-211981; Xenobiotics.
DR BioGRID-ORCS; 72082; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9D816; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9D816; protein.
DR Bgee; ENSMUSG00000025002; Expressed in right colon and 22 other tissues.
DR Genevisible; Q9D816; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IDA:MGI.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0071614; F:linoleic acid epoxygenase activity; IDA:MGI.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; ISO:MGI.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:MGI.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:MGI.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISO:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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 InterPro; IPR036396; Cyt_P450_sf.
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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..490
FT /note="Cytochrome P450 2C55"
FT /id="PRO_0000282959"
FT BINDING 435
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P10632"
SQ SEQUENCE 490 AA; 56096 MW; 5CB0F771C0268FEC CRC64;
MDPVLVLVLT LSCLLLLSLW RQNSGRGKLP PGPTPFPIIG NILQIDIKNI SKSFNYFSKV
YGPVFTLYFG SKPTVVVHGY EAVKEALDDL GEEFSGRGSF QIFERINNDL GVIFSNGTKW
KELRRFSIMT LRSFGMGKRS IEDRIQEEAS CLVEELRKAN GSLCDPTFIL SCAPSNVICS
VIFHNRFDYK DEKFLNLMER LNENFKILNS PWMQVYNALP TLINYLPGSH NKVIKNFTEI
KSYILGRVKE HQETLDMDNP RDFIDCFLIK MEQEKHNPHS EFTIESLMAT VTDIFVAGTE
TTNITLRYGL LLLLKHTEVT AKVQAEIDHV IGRHRSPCMQ DRTRMPYTDA MVHEIQRYID
LIPNNVPHAA TCNVRFRSYF IPKGTELVTS LTSVLHDDKE FPNPEVFDPG HFLDENGNFK
KSDYFMPFSI GKRMCVGEAL ARTELFLILT TILQNFNLKS LVDTKDIDTT PVANTFGRVP
PSYQLYFIPR
