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Cytochrome P450 4F12 (EC 1.14.14.1) (CYPIVF12)

 CP4FC_HUMAN             Reviewed;         524 AA.
Q9HCS2; E7ET51; O60389; Q5JPJ7; Q9HCS1;
10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
23-MAY-2018, entry version 150.
RecName: Full=Cytochrome P450 4F12;
EC=1.14.14.1;
AltName: Full=CYPIVF12;
Name=CYP4F12; ORFNames=UNQ568/PRO1129;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
CHARACTERIZATION, AND VARIANTS MET-16; ASP-76; VAL-90; ARG-188 AND
GLY-522.
TISSUE=Liver;
PubMed=11162607; DOI=10.1006/bbrc.2000.4191;
Bylund J., Bylund M., Oliw E.H.;
"cDNA cloning and expression of CYP4F12, a novel human cytochrome
P450.";
Biochem. Biophys. Res. Commun. 280:892-897(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
CHARACTERIZATION, AND VARIANTS LEU-13; MET-16; ASP-76; VAL-90; ARG-188
AND GLY-522.
TISSUE=Small intestine;
PubMed=11162645; DOI=10.1006/bbrc.2000.4238;
Hashizume T., Imaoka S., Hiroi T., Terauchi Y., Fujii T., Miyazaki H.,
Kamataki T., Funae Y.;
"cDNA cloning and expression of a novel cytochrome p450 (cyp4f12) from
human small intestine.";
Biochem. Biophys. Res. Commun. 280:1135-1141(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
MET-16; ASP-76; VAL-90; ARG-188 AND GLY-522.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
MET-16 AND ASP-76.
TISSUE=Placenta;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
MET-16 AND ASP-76.
TISSUE=Cervix;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS MET-16;
ASP-76; VAL-90; ARG-188 AND GLY-522.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes leukotriene B4 omega-hydroxylation and
arachidonic acid omega-hydroxylation but with an activity much
lower than that of CYP4F2. Catalyzes the hydroxylation of the
antihistamine ebastine.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P51869};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Microsome membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9HCS2-1; Sequence=Displayed;
Name=2;
IsoId=Q9HCS2-2; Sequence=VSP_055581, VSP_055582;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in small intestine, liver, colon and
heart. {ECO:0000269|PubMed:11162607, ECO:0000269|PubMed:11162645}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAW84492.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY008841; AAG33247.1; -; mRNA.
EMBL; AB035130; BAB18269.1; -; mRNA.
EMBL; AB035131; BAB18270.1; -; mRNA.
EMBL; AY358977; AAQ89336.1; -; mRNA.
EMBL; AK075435; BAG52137.1; -; mRNA.
EMBL; AL832171; CAI46131.1; -; mRNA.
EMBL; AC004523; AAC11543.1; -; Genomic_DNA.
EMBL; AC122702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84492.1; ALT_INIT; Genomic_DNA.
EMBL; CH471106; EAW84495.1; -; Genomic_DNA.
CCDS; CCDS42517.1; -. [Q9HCS2-1]
PIR; JC7594; JC7594.
PIR; JC7598; JC7598.
RefSeq; NP_076433.3; NM_023944.3.
UniGene; Hs.131459; -.
ProteinModelPortal; Q9HCS2; -.
SMR; Q9HCS2; -.
BioGrid; 122449; 7.
IntAct; Q9HCS2; 4.
STRING; 9606.ENSP00000321821; -.
ChEMBL; CHEMBL3509589; -.
DrugBank; DB08868; Fingolimod.
SwissLipids; SLP:000001652; -.
iPTMnet; Q9HCS2; -.
PhosphoSitePlus; Q9HCS2; -.
BioMuta; CYP4F12; -.
DMDM; 313104094; -.
MaxQB; Q9HCS2; -.
PaxDb; Q9HCS2; -.
PeptideAtlas; Q9HCS2; -.
PRIDE; Q9HCS2; -.
DNASU; 66002; -.
Ensembl; ENST00000517734; ENSP00000430849; ENSG00000186204. [Q9HCS2-2]
Ensembl; ENST00000548435; ENSP00000449703; ENSG00000186204. [Q9HCS2-2]
GeneID; 66002; -.
KEGG; hsa:66002; -.
UCSC; uc060uvi.1; human. [Q9HCS2-1]
CTD; 66002; -.
EuPathDB; HostDB:ENSG00000186204.14; -.
GeneCards; CYP4F12; -.
HGNC; HGNC:18857; CYP4F12.
HPA; HPA058960; -.
MIM; 611485; gene.
neXtProt; NX_Q9HCS2; -.
OpenTargets; ENSG00000186204; -.
PharmGKB; PA38717; -.
eggNOG; KOG0157; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00900000140829; -.
HOGENOM; HOG000233833; -.
HOVERGEN; HBG000182; -.
InParanoid; Q9HCS2; -.
KO; K17730; -.
PhylomeDB; Q9HCS2; -.
TreeFam; TF105088; -.
Reactome; R-HSA-211935; Fatty acids.
Reactome; R-HSA-211979; Eicosanoids.
GeneWiki; CYP4F12; -.
GenomeRNAi; 66002; -.
PRO; PR:Q9HCS2; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000186204; -.
CleanEx; HS_CYP4F12; -.
ExpressionAtlas; Q9HCS2; baseline and differential.
Genevisible; Q9HCS2; HS.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0018685; F:alkane 1-monooxygenase activity; ISS:UniProtKB.
GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISS:UniProtKB.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; ISS:UniProtKB.
GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
GO; GO:0017144; P:drug metabolic process; ISS:UniProtKB.
GO; GO:0019373; P:epoxygenase P450 pathway; ISS:UniProtKB.
GO; GO:0036101; P:leukotriene B4 catabolic process; ISS:UniProtKB.
GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; ISS:UniProtKB.
GO; GO:0003095; P:pressure natriuresis; ISS:UniProtKB.
GO; GO:0003091; P:renal water homeostasis; ISS:UniProtKB.
GO; GO:0055078; P:sodium ion homeostasis; ISS:UniProtKB.
GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS:UniProtKB.
GO; GO:0042360; P:vitamin E metabolic process; ISS:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endoplasmic reticulum; Heme;
Iron; Membrane; Metal-binding; Microsome; Monooxygenase;
Oxidoreductase; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 524 Cytochrome P450 4F12.
/FTId=PRO_0000051857.
TRANSMEM 19 39 Helical. {ECO:0000255}.
TRANSMEM 87 107 Helical. {ECO:0000255}.
METAL 468 468 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P51869}.
VAR_SEQ 90 102 IWLGPIIPFIVLC -> LPLHPRIISSSGS (in
isoform 2). {ECO:0000303|PubMed:16303743,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_055581.
VAR_SEQ 103 524 Missing (in isoform 2).
{ECO:0000303|PubMed:16303743,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_055582.
VARIANT 13 13 P -> L (in dbSNP:rs16995376).
{ECO:0000269|PubMed:11162645}.
/FTId=VAR_013244.
VARIANT 16 16 T -> M (in dbSNP:rs16995378).
{ECO:0000269|PubMed:11162607,
ECO:0000269|PubMed:11162645,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:16303743,
ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.7}.
/FTId=VAR_048459.
VARIANT 76 76 N -> D (in dbSNP:rs609636).
{ECO:0000269|PubMed:11162607,
ECO:0000269|PubMed:11162645,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:16303743,
ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.7}.
/FTId=VAR_013245.
VARIANT 90 90 I -> V (in dbSNP:rs609290).
{ECO:0000269|PubMed:11162607,
ECO:0000269|PubMed:11162645,
ECO:0000269|PubMed:12975309,
ECO:0000269|Ref.7}.
/FTId=VAR_013246.
VARIANT 188 188 C -> R (in dbSNP:rs2285888).
{ECO:0000269|PubMed:11162607,
ECO:0000269|PubMed:11162645,
ECO:0000269|PubMed:12975309,
ECO:0000269|Ref.7}.
/FTId=VAR_013247.
VARIANT 522 522 S -> G (in dbSNP:rs593818).
{ECO:0000269|PubMed:11162607,
ECO:0000269|PubMed:11162645,
ECO:0000269|PubMed:12975309,
ECO:0000269|Ref.7}.
/FTId=VAR_048460.
SEQUENCE 524 AA; 60270 MW; F29C29BA8DB880FE CRC64;
MSLLSLPWLG LRPVATSPWL LLLLVVGSWL LARILAWTYA FYNNCRRLQC FPQPPKRNWF
WGHLGLITPT EEGLKNSTQM SATYSQGFTI WLGPIIPFIV LCHPDTIRSI TNASAAIAPK
DNLFIRFLKP WLGEGILLSG GDKWSRHRRM LTPAFHFNIL KSYITIFNKS ANIMLDKWQH
LASEGSSCLD MFEHISLMTL DSLQKCIFSF DSHCQERPSE YIATILELSA LVEKRSQHIL
QHMDFLYYLS HDGRRFHRAC RLVHDFTDAV IRERRRTLPT QGIDDFFKDK AKSKTLDFID
VLLLSKDEDG KALSDEDIRA EADTFMFGGH DTTASGLSWV LYNLARHPEY QERCRQEVQE
LLKDRDPKEI EWDDLAQLPF LTMCVKESLR LHPPAPFISR CCTQDIVLPD GRVIPKGITC
LIDIIGVHHN PTVWPDPEVY DPFRFDPENS KGRSPLAFIP FSAGPRNCIG QAFAMAEMKV
VLALMLLHFR FLPDHTEPRR KLELIMRAEG GLWLRVEPLN VSLQ


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