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CP4F_SHEEP
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   03-AUG-2022, entry version 82.
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.ENSOARP00000001262; -.
DR   SwissLipids; SLP:000001701; -.
DR   GeneID; 443099; -.
DR   KEGG; oas:443099; -.
DR   CTD; 443099; -.
DR   OrthoDB; 825914at2759; -.
DR   Proteomes; UP000002356; 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: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   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; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 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
 
 
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