CP2U1_BOVIN
ID CP2U1_BOVIN Reviewed; 543 AA.
AC Q0IIF9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Cytochrome P450 2U1;
DE AltName: Full=Long-chain fatty acid omega-monooxygenase;
DE EC=1.14.14.80 {ECO:0000250|UniProtKB:Q7Z449};
GN Name=CYP2U1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC arachidonic acid and its conjugates. Mechanistically, uses molecular
CC oxygen inserting one oxygen atom into a substrate, and reducing the
CC second into a water molecule, with two electrons provided by NADPH via
CC cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Acts
CC as an omega and omega-1 hydroxylase for arachidonic acid and possibly
CC for other long chain fatty acids. May modulate the arachidonic acid
CC signaling pathway and play a role in other fatty acid signaling
CC processes. May down-regulate the biological activities of N-
CC arachidonoyl-serotonin, an endocannabinoid that has anti-nociceptive
CC effects through inhibition of fatty acid amide hydrolase FAAH, TRPV1
CC receptor and T-type calcium channels. Catalyzes C-2 oxidation of the
CC indole ring of N-arachidonoyl-serotonin forming a less active product
CC 2-oxo-N-arachidonoyl-serotonin. {ECO:0000250|UniProtKB:Q7Z449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--
CC hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991,
CC ChEBI:CHEBI:140992; EC=1.14.14.80;
CC Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56749;
CC Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76627; Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
CC Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76624; Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756;
CC Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-[(5Z,8Z,11Z,14Z)-eicosatetraenoyl]-serotonin + O2 + reduced
CC [NADPH--hemoprotein reductase] = 2-oxo-N-[(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl]-serotonin + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:50296, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:132255, ChEBI:CHEBI:132256;
CC Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50297;
CC Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q7Z449};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q7Z449}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q7Z449};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q7Z449}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; BC122663; AAI22664.1; -; mRNA.
DR RefSeq; NP_001069518.1; NM_001076050.2.
DR AlphaFoldDB; Q0IIF9; -.
DR SMR; Q0IIF9; -.
DR STRING; 9913.ENSBTAP00000017246; -.
DR PaxDb; Q0IIF9; -.
DR GeneID; 535227; -.
DR KEGG; bta:535227; -.
DR CTD; 113612; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; Q0IIF9; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01686; EP450ICYP2D.
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; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..543
FT /note="Cytochrome P450 2U1"
FT /id="PRO_0000291755"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 490
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"
SQ SEQUENCE 543 AA; 61997 MW; 00DEC2B84EC1D93C CRC64;
MASPGLPQPP TEDAAWPLRL LHAPPGLLRL DPTGGALLLL VLAALLGWSW LWRLPERGIP
PGPAPWPVVG NFGFVLLPRF LRRKSWPYRR ARNGGMNASG QGVQLLLADL GRVYGNIFSF
LIGHYLVVVL NDFHSVREAL VQQAEVFSDR PRVPLTSIMT KGKGIVFAHY GPVWRQQRKF
SHSTLRHFGL GKLSLEPKII EEFRYVKEEM QKHGDAPFNP FPIVNNAVSN IICSLCFGRR
FDYTNSEFKQ MLNFMSRALE VCLNTQLLLV NICSWLYYLP FGPFKELRQI EKDLTLFLKK
IIKDHRESLD VENPQDFIDM YLLHVEEEKK NNSNSGFDED YLFYIIGDLF IAGTDTTTNS
LLWCLLYMSL HPNIQEKIHE EIARVIGADR APSLTDKAQM PYTEATIMEV QRLSTVVPLS
IPHMTSEKTV LQGFTIPKGT IILPNLWSVH RDPAIWEKPN DFYPDRFLDD QGQLIKKETF
IPFGIGKRVC MGEQLAKMEL FLMFVSLMQS FTFVLPKDSK PILTGKYGLT LAPHPFNIII
SKR
