ID CP4F_SHEEP Reviewed; 528 AA.
AC Q9GLL1;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Prostaglandin E2 omega-hydroxylase CYP4F21 {ECO:0000303|PubMed:11370662};
DE EC=1.14.14.- {ECO:0000269|PubMed:11370662};
DE AltName: Full=Cytochrome P450 4F21;
DE Flags: Precursor;
GN Name=CYP4F21 {ECO:0000303|PubMed:11370662};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC TISSUE=Seminal vesicle;
RX PubMed=11370662; DOI=10.1006/abbi.2001.2322;
RA Bylund J., Oliw E.H.;
RT "Cloning and characterization of CYP4F21: a prostaglandin E2 20-hydroxylase
RT of ram seminal vesicles.";
RL Arch. Biochem. Biophys. 389:123-129(2001).
CC -!- FUNCTION: A cytochrome P450 monooxygenase that catalyzes the omega-
CC hydroxylation of prostaglandin E2. 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).
CC {ECO:0000269|PubMed:11370662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + prostaglandin E2 + reduced [NADPH--hemoprotein reductase]
CC = 20-hydroxy prostaglandin E2 + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:52488, 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:136653, ChEBI:CHEBI:606564;
CC Evidence={ECO:0000269|PubMed:11370662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52489;
CC Evidence={ECO:0000305|PubMed:11370662};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P51869};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for prostaglandin E2 {ECO:0000269|PubMed:11370662};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:11370662}; Single-pass type I membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000305|PubMed:11370662};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF246236; AAG09778.1; -; mRNA.
DR RefSeq; NP_001009743.1; NM_001009743.1.
DR AlphaFoldDB; Q9GLL1; -.
DR SMR; Q9GLL1; -.
DR STRING; 9940.ENSOARP00000001538; -.
DR SwissLipids; SLP:000001701; -.
DR PaxDb; 9940-ENSOARP00000001262; -.
DR GeneID; 443099; -.
DR KEGG; oas:443099; -.
DR CTD; 443099; -.
DR OrthoDB; 3592258at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum 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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd20679; CYP4F; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24291:SF112; CYTOCHROME P450 4F2; 1.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 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; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..528
FT /note="Prostaglandin E2 omega-hydroxylase CYP4F21"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448979"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 332
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P51869"
FT BINDING 472
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:P51869"
SQ SEQUENCE 528 AA; 61113 MW; 582F5210213AC32D CRC64;
MLELSVSRLG FGLVAASPWL LLLVVGASWL LARVLAWTYT FYNNCRLLQC FPQPPKQNWF
FAHLYLVPPT EQGLRKSTQL AANYSHGYLI WFGPITPMIV FCHPDMLRSI ANASAAVAPK
NMDFYKFLKP WLGDGLLLSA GDKWSRHRHL LTPTFHFNIL KPYMKIFTKS TDIMHTKWER
LITQGHTRLD MFEHLSLLTL DSLQKCVFSF DSNCQELSSC RKPSKYITAI LELSELVAKR
NRQIFLHADF LYFLTLDGWR FLRACRLVHD FTDAVIQERC RTLPENVDDF LKAKAKTKTL
DFIDVLLLTK DEDGKRLSDE DIRAEADTFM FEGHDTTASG LSWILYNLAK HPEYQERCRQ
EVQELLRDRE SKEIEWDNLA QLPFLTMCIK ESLRLHPPVT IISRCCTQDI VLPNGWVIPK
GVICIIDIFG THHNQSVWPD PEVYDPFRFD QENIKGRSPL AFIPFSAGPR NCIGQTFAMT
EMKVVLALTL LRFRFLPDKE EPRRKRELIL RAEGGLWLQV EPLSASPQ
//
