CP4AO_PIG
ID CP4AO_PIG Reviewed; 504 AA.
AC Q8SPK1; Q70BW1; Q70BZ6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cytochrome P450 4A24;
DE AltName: Full=CYPIVA24;
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=CYP4A24;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42 AND 83-448.
RX PubMed=14641109; DOI=10.1042/bj20031657;
RA Lundell K.;
RT "The porcine taurochenodeoxycholic acid 6alpha-hydroxylase (CYP4A21) gene:
RT evolution by gene duplication and gene conversion.";
RL Biochem. J. 378:1053-1058(2004).
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; AJ318096; CAC85662.1; -; mRNA.
DR EMBL; AJ586860; CAE52547.1; -; Genomic_DNA.
DR EMBL; AJ586619; CAE52533.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8SPK1; -.
DR SMR; Q8SPK1; -.
DR STRING; 9823.ENSSSCP00000022475; -.
DR PaxDb; Q8SPK1; -.
DR PeptideAtlas; Q8SPK1; -.
DR Ensembl; ENSSSCT00000004304; ENSSSCP00000004204; ENSSSCG00000003891.
DR Ensembl; ENSSSCT00000063601; ENSSSCP00000044191; ENSSSCG00000003891.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000155173; -.
DR InParanoid; Q8SPK1; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000003891; Expressed in adult mammalian kidney and 20 other tissues.
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 4A24"
FT /id="PRO_0000280743"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
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"
FT CONFLICT 202
FT /note="A -> V (in Ref. 2; CAE52533)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="I -> T (in Ref. 2; CAE52533)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="N -> S (in Ref. 2; CAE52533)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="R -> Q (in Ref. 2; CAE52533)"
FT /evidence="ECO:0000305"
FT CONFLICT 382..384
FT /note="GVS -> SVG (in Ref. 2; CAE52533)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="T -> I (in Ref. 2; CAE52533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 57199 MW; DB7F815966DA7D7B CRC64;
MTVPALASAS GLLQVASLLG LLLLLLKAAQ LYLHRQWLLK ALQQFPSPPS HWLYGHSREF
QEESELPPLL KRVEKYPSAC ALWRWGTRAM VLVYDPDYMK VVLARSDPKN SVVYRLLIPW
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 AGITLSLSIY GLHHNPQVWP
NPEEFDPSRF APGSARHSHA FMPFSGGSRN CIGKQFAMNE MKVAVALTLL RFELAPDPSR
KPIATPEVVL NSKNGIHLKL RKLP
