Reviewed, UniProtKB/Swiss-Prot Q9D816 (CP255_MOUSE)

Names and origin

Protein names

Recommended name:
    Cytochrome P450 2C55
    EC=1.14.14.1
Alternative name(s):
    CYPIIC55

Gene names

Name:	Cyp2c55
Synonyms:	Cyp2c-55

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Metabolizes arachidonic acid mainly to 19-hydroxyeicosatetraenoic acid (HETE). Ref.1
Catalytic activity	RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. Ref.1
Cofactor	Heme group By similarity.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Tissue specificity	Highest level in colon. Low levels in liver and small intestine. Ref.1
Induction	P450 can be induced to high levels in liver and other tissues by various foreign compounds, including drugs, pesticides, and carcinogens.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aromatase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 490	490	Cytochrome P450 2C55		PRO_0000282959
Sites
	Metal binding	435	1	Iron (heme axial ligand) By similarity UniProtKB P10632

Sequences

	Sequence		Length	Mass (Da)
	Q9D816-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 5CB0F771C0268FEC	FASTA	490	56,096
	10 20 30 40 50 60 MDPVLVLVLT LSCLLLLSLW RQNSGRGKLP PGPTPFPIIG NILQIDIKNI SKSFNYFSKV 70 80 90 100 110 120 YGPVFTLYFG SKPTVVVHGY EAVKEALDDL GEEFSGRGSF QIFERINNDL GVIFSNGTKW 130 140 150 160 170 180 KELRRFSIMT LRSFGMGKRS IEDRIQEEAS CLVEELRKAN GSLCDPTFIL SCAPSNVICS 190 200 210 220 230 240 VIFHNRFDYK DEKFLNLMER LNENFKILNS PWMQVYNALP TLINYLPGSH NKVIKNFTEI 250 260 270 280 290 300 KSYILGRVKE HQETLDMDNP RDFIDCFLIK MEQEKHNPHS EFTIESLMAT VTDIFVAGTE 310 320 330 340 350 360 TTNITLRYGL LLLLKHTEVT AKVQAEIDHV IGRHRSPCMQ DRTRMPYTDA MVHEIQRYID 370 380 390 400 410 420 LIPNNVPHAA TCNVRFRSYF IPKGTELVTS LTSVLHDDKE FPNPEVFDPG HFLDENGNFK 430 440 450 460 470 480 KSDYFMPFSI GKRMCVGEAL ARTELFLILT TILQNFNLKS LVDTKDIDTT PVANTFGRVP 490 PSYQLYFIPR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and characterization of three new mouse cytochrome p450 enzymes and partial characterization of their fatty acid oxidation activities." Wang H., Zhao Y., Bradbury J.A., Graves J.P., Foley J., Blaisdell J.A., Goldstein J.A., Zeldin D.C. Mol. Pharmacol. 65:1148-1158(2004) [PubMed: 15102943] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Colon.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Small intestine.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY206875 mRNA. Translation: AAO52738.1. AK008580 mRNA. Translation: BAB25759.1. BC010824 mRNA. Translation: AAH10824.1.
IPI	IPI00110673.
RefSeq	NP_082365.1.
UniGene	Mm.142581
3D structure databases
HSSP	HSSP built from PDB template 1R9O based on UniProtKB P11712.
SMR	Q9D816. Positions 44-489.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9D816.
PTM databases
PhosphoSite	Q9D816.
Proteomic databases
PRIDE	Q9D816.
Genome annotation databases
Ensembl	ENSMUST00000025966; ENSMUSP00000025966; ENSMUSG00000025002; Mus musculus. [Genome view]
GeneID	72082.
KEGG	mmu:72082.
UCSC	uc008hju.1. mouse.
Organism-specific databases
CTD	72082.
MGI	MGI:1919332. Cyp2c55.
Phylogenomic databases
HOVERGEN	Q9D816.
OMA	TNDTILA
OrthoDB	EOG9TTK37
Enzyme and pathway databases
BRENDA	1.14.14.1. 244.
Gene expression databases
ArrayExpress	Q9D816.
Bgee	Q9D816.
Genevestigator	Q9D816.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	335388.
SOURCE	Search...

Entry information

Entry name

CP255_MOUSE

Accession

Primary (citable) accession number: Q9D816

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	June 1, 2001
Last modified:	November 24, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)