CP4AA_RAT
ID CP4AA_RAT Reviewed; 509 AA.
AC P08516; Q5EBD8;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Cytochrome P450 4A10;
DE AltName: Full=CYPIVA10;
DE AltName: Full=Cytochrome P450-LA-omega 1;
DE AltName: Full=Cytochrome P452;
DE AltName: Full=Lauric acid omega-hydroxylase;
DE AltName: Full=Long-chain fatty acid omega-monooxygenase;
DE EC=1.14.14.80 {ECO:0000269|PubMed:10362749, ECO:0000269|PubMed:10620324};
GN Name=Cyp4a10; Synonyms=Cyp4a-1, Cyp4a1 {ECO:0000303|PubMed:10362749};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY CLOFIBRATE.
RC TISSUE=Liver;
RX PubMed=3027069; DOI=10.1016/s0021-9258(19)75857-8;
RA Hardwick J.P., Song B.-J., Huberman E., Gonzalez F.J.;
RT "Isolation, complementary DNA sequence, and regulation of rat hepatic
RT lauric acid omega-hydroxylase (cytochrome P-450LA omega). Identification of
RT a new cytochrome P-450 gene family.";
RL J. Biol. Chem. 262:801-810(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=3410047; DOI=10.1016/0014-5793(88)80055-3;
RA Earnshaw D., Dale J.W., Goldfarb P.S., Gibson G.G.;
RT "Differential splicing in the 3' non-coding region of rat cytochrome P-452
RT (P450 IVA1) mRNA.";
RL FEBS Lett. 236:357-361(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=2766932; DOI=10.1089/dna.1.1989.8.503;
RA Kimura S., Hanioka N., Matsunaga E., Gonzalez F.J.;
RT "The rat clofibrate-inducible CYP4A gene subfamily. I. Complete intron and
RT exon sequence of the CYP4A1 and CYP4A2 genes, unique exon organization, and
RT identification of a conserved 19-bp upstream element.";
RL DNA 8:503-516(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-22.
RX PubMed=1567203; DOI=10.1016/0003-9861(92)90714-8;
RA Okita R.T., Okita J.R.;
RT "Characterization of a cytochrome P450 from di(2-ethylhexyl) phthalate-
RT treated rats which hydroxylates fatty acids.";
RL Arch. Biochem. Biophys. 294:475-481(1992).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10362749; DOI=10.1152/ajpregu.1999.276.6.r1691;
RA Nguyen X., Wang M.H., Reddy K.M., Falck J.R., Schwartzman M.L.;
RT "Kinetic profile of the rat CYP4A isoforms: arachidonic acid metabolism and
RT isoform-specific inhibitors.";
RL Am. J. Physiol. 276:R1691-R1700(1999).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10620324; DOI=10.1006/abbi.1999.1504;
RA Hoch U., Zhang Z., Kroetz D.L., Ortiz de Montellano P.R.;
RT "Structural determination of the substrate specificities and
RT regioselectivities of the rat and human fatty acid omega-hydroxylases.";
RL Arch. Biochem. Biophys. 373:63-71(2000).
RN [8]
RP COVALENT HEME ATTACHMENT.
RX PubMed=11139583; DOI=10.1074/jbc.m009969200;
RA Hoch U., Ortiz de Montellano P.R.;
RT "Covalently linked heme in cytochrome P4504A fatty acid hydroxylases.";
RL J. Biol. Chem. 276:11339-11346(2001).
RN [9]
RP COVALENT HEME ATTACHMENT, AND MUTAGENESIS OF GLU-320.
RX PubMed=11821421; DOI=10.1074/jbc.m112155200;
RA LeBrun L.A., Hoch U., Ortiz de Montellano P.R.;
RT "Autocatalytic mechanism and consequences of covalent heme attachment in
RT the cytochrome P4504A family.";
RL J. Biol. Chem. 277:12755-12761(2002).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14742258; DOI=10.1016/s0002-9440(10)63142-2;
RA Muller D.N., Theuer J., Shagdarsuren E., Kaergel E., Honeck H., Park J.K.,
RA Markovic M., Barbosa-Sicard E., Dechend R., Wellner M., Kirsch T.,
RA Fiebeler A., Rothe M., Haller H., Luft F.C., Schunck W.H.;
RT "A peroxisome proliferator-activated receptor-alpha activator induces renal
RT CYP2C23 activity and protects from angiotensin II-induced renal injury.";
RL Am. J. Pathol. 164:521-532(2004).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16212878; DOI=10.1038/sj.cr.7290341;
RA Zhang F., Chen C.L., Qian J.Q., Yan J.T., Cianflone K., Xiao X., Wang D.W.;
RT "Long-term modifications of blood pressure in normotensive and
RT spontaneously hypertensive rats by gene delivery of rAAV-mediated
RT cytochrome P450 arachidonic acid hydroxylase.";
RL Cell Res. 15:717-724(2005).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC fatty acids. Catalyzes predominantly the oxidation of the terminal
CC carbon (omega-oxidation) of long-chain fatty acids (PubMed:10620324,
CC PubMed:3027069, PubMed:10362749). Acts as a major omega-hydroxylase for
CC dodecanoic (lauric) acid in liver (PubMed:3027069). In kidney, may play
CC an important role in omega-hydroxylation of (5Z,8Z,11Z,14Z)-
CC eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid
CC (20-HETE), a signaling molecule acting both as vasoconstrictive and
CC natriuretic with overall effect on arterial blood pressure
CC (PubMed:10362749, PubMed:10620324, PubMed:16212878). Also participates
CC in the formation of anti-inflammatory hydroxyepoxyeicosatrienoic acids
CC (HEETs) in kidney by converting 8,9-epoxyeicosatrienoic acid (EET) to
CC 20,8,9-HEET, an activator of PPARA (PubMed:14742258). Displays
CC substantially lower fatty acid omega-1 hydroxylase activity
CC (PubMed:10362749, PubMed:10620324). 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 (PubMed:10620324, PubMed:3027069, PubMed:10362749).
CC {ECO:0000269|PubMed:10362749, ECO:0000269|PubMed:10620324,
CC ECO:0000269|PubMed:14742258, ECO:0000269|PubMed:16212878,
CC ECO:0000269|PubMed:3027069}.
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:0000269|PubMed:10362749, ECO:0000269|PubMed:10620324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56749;
CC Evidence={ECO:0000305|PubMed:10362749, ECO:0000305|PubMed:10620324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:38947, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:36204, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10362749,
CC ECO:0000269|PubMed:10620324, ECO:0000269|PubMed:3027069};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38948;
CC Evidence={ECO:0000305|PubMed:10362749, ECO:0000305|PubMed:10620324,
CC ECO:0000305|PubMed:3027069};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76628; Evidence={ECO:0000250|UniProtKB:O88833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39752;
CC Evidence={ECO:0000250|UniProtKB:O88833};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate =
CC 14-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40203, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:77033; Evidence={ECO:0000269|PubMed:10620324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40204;
CC Evidence={ECO:0000305|PubMed:10620324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40199, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:55329, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.80;
CC Evidence={ECO:0000269|PubMed:10620324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40200;
CC Evidence={ECO:0000305|PubMed:10620324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41728, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78424;
CC EC=1.14.14.80; Evidence={ECO:0000269|PubMed:10620324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41729;
CC Evidence={ECO:0000305|PubMed:10620324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60580,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132029;
CC Evidence={ECO:0000269|PubMed:10362749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60581;
CC Evidence={ECO:0000305|PubMed:10362749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 17-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60932,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144041;
CC Evidence={ECO:0000269|PubMed:10362749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60933;
CC Evidence={ECO:0000305|PubMed:10362749};
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:0000269|PubMed:10362749,
CC ECO:0000269|PubMed:10620324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756;
CC Evidence={ECO:0000305|PubMed:10620324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)-
CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53572, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84025,
CC ChEBI:CHEBI:137474; Evidence={ECO:0000269|PubMed:14742258};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53573;
CC Evidence={ECO:0000305|PubMed:14742258};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:11139583, ECO:0000269|PubMed:11821421};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate
CC {ECO:0000269|PubMed:10362749};
CC Note=kcat is 649 min-1 for dodecanoate. kcat is 230 min-1 for
CC tetradecanoate. kcat is 60 min-1 for hexadecanoate. kcat is 1.4 min-1
CC for (9Z)-octadecenoate. kcat is 6 min-1 for (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate. {ECO:0000269|PubMed:10620324};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:3027069}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:3027069}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level) and kidney
CC (at protein level). {ECO:0000269|PubMed:16212878,
CC ECO:0000269|PubMed:3027069}.
CC -!- INDUCTION: By clofibrate. {ECO:0000269|PubMed:3027069}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M14972; AAA41061.1; -; mRNA.
DR EMBL; X07259; CAA30245.1; -; mRNA.
DR EMBL; M57718; AAA41038.1; -; Genomic_DNA.
DR EMBL; BC089761; AAH89761.1; -; mRNA.
DR PIR; S01336; O4RTLO.
DR RefSeq; NP_787031.1; NM_175837.1.
DR RefSeq; XP_006238774.1; XM_006238712.3.
DR AlphaFoldDB; P08516; -.
DR SMR; P08516; -.
DR STRING; 10116.ENSRNOP00000041025; -.
DR SwissLipids; SLP:000000747; -.
DR iPTMnet; P08516; -.
DR PhosphoSitePlus; P08516; -.
DR PaxDb; P08516; -.
DR PRIDE; P08516; -.
DR Ensembl; ENSRNOT00000012888; ENSRNOP00000012888; ENSRNOG00000009597.
DR GeneID; 50549; -.
DR KEGG; rno:50549; -.
DR CTD; 50549; -.
DR RGD; 68945; Cyp4a1.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000163570; -.
DR InParanoid; P08516; -.
DR OMA; YGVQVCM; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; P08516; -.
DR BRENDA; 1.14.14.80; 5301.
DR Reactome; R-RNO-211935; Fatty acids.
DR Reactome; R-RNO-211958; Miscellaneous substrates.
DR Reactome; R-RNO-211979; Eicosanoids.
DR Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR PRO; PR:P08516; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009597; Expressed in liver and 6 other tissues.
DR ExpressionAtlas; P08516; baseline and differential.
DR Genevisible; P08516; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0103002; F:16-hydroxypalmitate dehydrogenase activity; ISO:RGD.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IMP:RGD.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IDA:RGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102116; F:laurate hydroxylase activity; ISO:RGD.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IMP:RGD.
DR GO; GO:0046456; P:icosanoid biosynthetic process; IMP:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0048252; P:lauric acid metabolic process; IDA:RGD.
DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:RGD.
DR GO; GO:0002933; P:lipid hydroxylation; ISO:RGD.
DR GO; GO:0001890; P:placenta development; IEP:RGD.
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 Direct protein sequencing; Endoplasmic reticulum; Fatty acid metabolism;
KW Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Microsome;
KW Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Cytochrome P450 4A10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000051816"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 320
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11139583,
FT ECO:0000269|PubMed:11821421"
FT BINDING 456
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:0000269|PubMed:11139583,
FT ECO:0000269|PubMed:11821421"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20816"
FT MUTAGEN 320
FT /note="E->A: Loss of heme binding."
FT /evidence="ECO:0000269|PubMed:11821421"
FT CONFLICT 341
FT /note="E -> K (in Ref. 1; AAA41061 and 2; CAA30245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 58215 MW; E622FAB351BC40AF CRC64;
MSVSALSSTR FTGSISGFLQ VASVLGLLLL LVKAVQFYLQ RQWLLKAFQQ FPSPPFHWFF
GHKQFQGDKE LQQIMTCVEN FPSAFPRWFW GSKAYLIVYD PDYMKVILGR SDPKANGVYR
LLAPWIGYGL LLLNGQPWFQ HRRMLTPAFH YDILKPYVKN MADSIRLMLD KWEQLAGQDS
SIEIFQHISL MTLDTVMKCA FSHNGSVQVD GNYKSYIQAI GNLNDLFHSR VRNIFHQNDT
IYNFSSNGHL FNRACQLAHD HTDGVIKLRK DQLQNAGELE KVKKKRRLDF LDILLLARME
NGDSLSDKDL RAEVDTFMFE GHDTTASGVS WIFYALATHP EHQQRCREEV QSVLGDGSSI
TWDHLDQIPY TTMCIKEALR LYPPVPGIVR ELSTSVTFPD GRSLPKGIQV TLSIYGLHHN
PKVWPNPEVF DPSRFAPDSP RHSHSFLPFS GGARNCIGKQ FAMSEMKVIV ALTLLRFELL
PDPTKVPIPL PRLVLKSKNG IYLYLKKLH
