ID   CP4AP_PIG               Reviewed;         504 AA.
AC   Q8SPK0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cytochrome P450 4A25;
DE   AltName: Full=CYPIVA25;
DE   AltName: Full=Fatty acid omega-hydroxylase;
DE   AltName: Full=Long-chain fatty acid omega-monooxygenase;
DE            EC=1.14.14.80 {ECO:0000250|UniProtKB:Q02928};
GN   Name=CYP4A25;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11931657; DOI=10.1042/0264-6021:3630297;
RA   Lundell K.;
RT   "Cloning and expression of two novel pig liver and kidney fatty acid
RT   hydroxylases [cytochrome P450 (CYP)4A24 and CYP4A25].";
RL   Biochem. J. 363:297-303(2002).
CC   -!- FUNCTION: Catalyzes the omega- and (omega-1)-hydroxylation of various
CC       fatty acids such as laurate and palmitate. Has no activity toward
CC       taurochenodeoxycholic acid.
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:Q02928};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P51869};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AJ318097; CAC85663.1; -; mRNA.
DR   AlphaFoldDB; Q8SPK0; -.
DR   SMR; Q8SPK0; -.
DR   PeptideAtlas; Q8SPK0; -.
DR   InParanoid; Q8SPK0; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..504
FT                   /note="Cytochrome P450 4A25"
FT                   /id="PRO_0000280744"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         451
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   504 AA;  57324 MW;  C6FD45CA1EDA97DF CRC64;
     MTVPALASAS GLLQVASLLG LLLLLLKAAQ LYLRRQWLLK ALQQFPSPPS HWLYGHSREF
     QEESELQPLL KRVEKYPSAC ARWLWGTRAM VLVYDPDYMK VVLARSEPKA PVLYRLLIPW
     IGCGLLLLNG QTWFQRRRML TPAFHYDILK PYVGLMAKSV QVMLDKWEQL VAQDPRLEIV
     GPVSLMTLDT IMKCAFSHQG SAQTDGDSHS YIQAIWDLKN LFSIRTKSAF LQNDIIYRLS
     PEGRKNHRAA RIAHQHTDRV IQLRKAQLQK QGEMENVRKK RHLDFLDILL LARMEKGNSL
     SDTDLRAEVD TFMFEGHDTT ASGISWILYA LASHPEHQQR CREEIQGLLG DGTSITWDHL
     DQMPYTTMCI KEALRLYPPV PGVSRELSKP ITFPDGRSLP AGIILSLSVY SLHHNPQVWP
     NPEEFDPSRF APGSARHSHA FMPFSGGSRN CIGKQFAMNE MKVAVALTLL RFELAPDPSR
     KPTVIPEVVL HSKNGIHLKL RKLP