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CP2J6_MOUSE
ID   CP2J6_MOUSE             Reviewed;         501 AA.
AC   O54750; Q8BR78;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Cytochrome P450 2J6;
DE            EC=1.14.14.1;
DE   AltName: Full=Arachidonic acid epoxygenase;
DE   AltName: Full=CYPIIJ6;
GN   Name=Cyp2j6;
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].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   PubMed=9570962; DOI=10.1006/geno.1998.5235;
RA   Ma J., Ramachandran S., Fiedorek F.T. Jr., Zeldin D.C.;
RT   "Mapping of the CYP2J cytochrome P450 genes to human chromosome 1 and mouse
RT   chromosome 4.";
RL   Genomics 49:152-155(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
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   -!- 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   -!- 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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U62295; AAB87636.1; -; mRNA.
DR   EMBL; AK045421; BAC32356.1; -; mRNA.
DR   EMBL; AK165663; BAE38325.1; -; mRNA.
DR   EMBL; AL683816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466527; EDL30913.1; -; Genomic_DNA.
DR   EMBL; BC050832; AAH50832.1; -; mRNA.
DR   CCDS; CCDS18369.1; -.
DR   RefSeq; NP_034138.3; NM_010008.4.
DR   AlphaFoldDB; O54750; -.
DR   SMR; O54750; -.
DR   STRING; 10090.ENSMUSP00000030303; -.
DR   iPTMnet; O54750; -.
DR   PhosphoSitePlus; O54750; -.
DR   jPOST; O54750; -.
DR   MaxQB; O54750; -.
DR   PaxDb; O54750; -.
DR   PeptideAtlas; O54750; -.
DR   PRIDE; O54750; -.
DR   ProteomicsDB; 283444; -.
DR   DNASU; 13110; -.
DR   Ensembl; ENSMUST00000030303; ENSMUSP00000030303; ENSMUSG00000052914.
DR   GeneID; 13110; -.
DR   KEGG; mmu:13110; -.
DR   UCSC; uc008tti.2; mouse.
DR   CTD; 13110; -.
DR   MGI; MGI:1270148; Cyp2j6.
DR   VEuPathDB; HostDB:ENSMUSG00000052914; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00950000182879; -.
DR   HOGENOM; CLU_001570_22_0_1; -.
DR   InParanoid; O54750; -.
DR   OMA; AEPRDFI; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; O54750; -.
DR   TreeFam; TF352043; -.
DR   Reactome; R-MMU-211935; Fatty acids.
DR   Reactome; R-MMU-211981; Xenobiotics.
DR   Reactome; R-MMU-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
DR   BioGRID-ORCS; 13110; 6 hits in 74 CRISPR screens.
DR   ChiTaRS; Cyp2j6; mouse.
DR   PRO; PR:O54750; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; O54750; protein.
DR   Bgee; ENSMUSG00000052914; Expressed in saccule of membranous labyrinth and 224 other tissues.
DR   Genevisible; O54750; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0008405; F:arachidonic acid 11,12-epoxygenase activity; ISO:MGI.
DR   GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; ISO:MGI.
DR   GO; GO:0008392; F:arachidonic acid epoxygenase activity; IMP:MGI.
DR   GO; GO:0008391; F:arachidonic acid monooxygenase activity; ISO: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:0016853; F:isomerase activity; ISO:MGI.
DR   GO; GO:0071614; F:linoleic acid epoxygenase activity; ISO:MGI.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; ISO: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:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; ISO:MGI.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; ISO:MGI.
DR   GO; GO:0006690; P:icosanoid metabolic process; ISO:MGI.
DR   GO; GO:0043651; P:linoleic acid metabolic process; ISO:MGI.
DR   GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR   GO; GO:0035359; P:negative regulation of peroxisome proliferator activated receptor signaling pathway; ISO:MGI.
DR   GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR   GO; GO:1903055; P:positive regulation of extracellular matrix organization; ISO:MGI.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; ISO:MGI.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR   GO; GO:0001523; P:retinoid 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; IPR008071; Cyt_P450_E_grp-I_CYP2J-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01688; EP450ICYP2J.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..501
FT                   /note="Cytochrome P450 2J6"
FT                   /id="PRO_0000051772"
FT   BINDING         447
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"
FT   CONFLICT        369
FT                   /note="Q -> R (in Ref. 1; AAB87636)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  57792 MW;  4E5A257C5C9C1CE7 CRC64;
     MLAATGSLLA TIWAALHPRT LLVAAVTFLL LADYFKNRRP KNYPPGPWGL PFVGNIFQLD
     FGQPHLSIQP LVKKYGNIFS LNLGDITSVV ITGLPLIKEA LTQMEQNIMN RPLSVMQERI
     SNKNGLIFSS GQIWKEQRRF ALMTLRNFGL GKKSLEERMQ EEASHLVEAI REEEGKPFNP
     HFSINNAVSN IICSVTFGER FDYHDSRFQE MLRLLDEVMY LETTMISQLY NIFPWIMKYI
     PGSHQKVFRN WEKLKLFVSC MIDDHRKDWN PDEPRDFIDA FLKEMTKYPE KTTSFNEENL
     ICSTLDLFFA GTETTSTTLR WALLYMALYP EVQEKVQAEI DRVIGQKRAA RLADRESMPY
     TNAVIHEVQR MGNIIPLNVP REVAMDTNLN GFHLPKGTMV LTNLTALHRD PKEWATPDVF
     NPEHFLENGQ FKKRESFLPF SMGKRACLGE QLARSELFIF FTSLMQKFTF NPPINEKLSP
     KFRNGLTLSP VSHRICAVPR Q
 
 
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