CP46A_MOUSE
ID CP46A_MOUSE Reviewed; 500 AA.
AC Q9WVK8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cholesterol 24-hydroxylase {ECO:0000305|PubMed:10377398};
DE Short=CH24H;
DE EC=1.14.14.25 {ECO:0000269|PubMed:10377398};
DE AltName: Full=Cholesterol 24-monooxygenase;
DE AltName: Full=Cholesterol 24S-hydroxylase {ECO:0000303|PubMed:10377398};
DE AltName: Full=Cytochrome P450 46A1 {ECO:0000303|PubMed:28190002};
GN Name=Cyp46a1 {ECO:0000303|PubMed:28190002, ECO:0000312|MGI:MGI:1341877};
GN Synonyms=Cyp46;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Liver;
RX PubMed=10377398; DOI=10.1073/pnas.96.13.7238;
RA Lund E.G., Guileyardo J.M., Russell D.W.;
RT "cDNA cloning of cholesterol 24-hydroxylase, a mediator of cholesterol
RT homeostasis in the brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7238-7243(1999).
RN [2]
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=16505352; DOI=10.1073/pnas.0600316103;
RA Kotti T.J., Ramirez D.M., Pfeiffer B.E., Huber K.M., Russell D.W.;
RT "Brain cholesterol turnover required for geranylgeraniol production and
RT learning in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3869-3874(2006).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18241055; DOI=10.1002/cne.21605;
RA Ramirez D.M., Andersson S., Russell D.W.;
RT "Neuronal expression and subcellular localization of cholesterol 24-
RT hydroxylase in the mouse brain.";
RL J. Comp. Neurol. 507:1676-1693(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY.
RX PubMed=28190002; DOI=10.1074/jbc.m116.774760;
RA Mast N., Anderson K.W., Lin J.B., Li Y., Turko I.V., Tatsuoka C.,
RA Bjorkhem I., Pikuleva I.A.;
RT "Cytochrome P450 27A1 Deficiency and Regional Differences in Brain Sterol
RT Metabolism Cause Preferential Cholestanol Accumulation in the Cerebellum.";
RL J. Biol. Chem. 292:4913-4924(2017).
CC -!- FUNCTION: P450 monooxygenase that plays a major role in cholesterol
CC homeostasis in the brain. Primarily catalyzes the hydroxylation (with S
CC stereochemistry) at C-24 of cholesterol side chain, triggering
CC cholesterol diffusion out of neurons and its further degradation
CC (PubMed:10377398, PubMed:16505352, PubMed:28190002). By promoting
CC constant cholesterol elimination in neurons, may activate the
CC mevalonate pathway and coordinate the synthesis of new cholesterol and
CC nonsterol isoprenoids involved in synaptic activity and learning
CC (PubMed:16505352). Further hydroxylates cholesterol derivatives and
CC hormone steroids on both the ring and side chain of these molecules,
CC converting them into active oxysterols involved in lipid signaling and
CC biosynthesis (By similarity). Acts as an epoxidase converting cholesta-
CC 5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, an
CC abundant lipid ligand of nuclear NR1H2 and NR1H3 receptors shown to
CC promote neurogenesis in developing brain (By similarity). May also
CC catalyze the oxidative metabolism of xenobiotics, such as clotrimazole
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y6A2,
CC ECO:0000269|PubMed:10377398, ECO:0000269|PubMed:16505352,
CC ECO:0000269|PubMed:28190002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (24S)-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:22716, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:34310, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.25;
CC Evidence={ECO:0000269|PubMed:10377398};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22717;
CC Evidence={ECO:0000305|PubMed:28190002};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholestanol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (24S)-hydroxycholestanol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53808, 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:86570,
CC ChEBI:CHEBI:137687; Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53809;
CC Evidence={ECO:0000305|PubMed:28190002};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-dehydrocholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = cholesta-5,7-dien-3beta,24S-diol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53244, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17759,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137061;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53245;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-dehydrocholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = cholesta-5,7-dien-3beta,25-diol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53240, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17759,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137057;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53241;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=desmosterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (24Z),26-hydroxydesmosterol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:53236, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17737, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:137053;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53237;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=desmosterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (24S)-25-epoxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53232, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17737, ChEBI:CHEBI:41633, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53233;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4beta-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 4beta,24S-dihydroxycholesterol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46392, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:85778, ChEBI:CHEBI:86087;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46393;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (24S,25R)-24,26-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46388,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:86165;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46389;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 24S,25-dihydroxycholesterol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46384, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:86074;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46385;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7alpha-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (24S)-7alpha-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46380,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17500,
CC ChEBI:CHEBI:37640, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46381;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] =
CC 17alpha-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:46308, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17026, ChEBI:CHEBI:17252,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46309;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + testosterone =
CC 16beta,17beta-dihydroxyandrost-4-en-3-one + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46304, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17347,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:83027;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46305;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + testosterone =
CC 2-hydroxytestosterone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:46300, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:86013; Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46301;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + testosterone =
CC 6beta,17beta-dihydroxyandrost-4-en-3-one + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46296, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17347,
CC ChEBI:CHEBI:34477, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46297;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC {ECO:0000305|PubMed:28190002}.
CC -!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism.
CC {ECO:0000250|UniProtKB:Q9Y6A2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18241055}; Single-pass membrane protein. Microsome
CC membrane; Single-pass membrane protein. Postsynapse
CC {ECO:0000269|PubMed:16505352}. Presynapse
CC {ECO:0000269|PubMed:16505352}. Cell projection, dendrite
CC {ECO:0000269|PubMed:18241055}.
CC -!- TISSUE SPECIFICITY: Expressed in high level in the pyramidal cells of
CC the hippocampus, Purkinje cells of the cerebellum, and neuronal cell
CC bodies in layers II/III, V, and VI of the cortex. Expressed in
CC hippocampal and cerebellar interneurons, in retinal ganglion cells, and
CC in a subset of retinal cells localized to the inner nuclear layer (at
CC protein level). {ECO:0000269|PubMed:10377398,
CC ECO:0000269|PubMed:18241055}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are deficient in spatial, associative
CC and motor learning. {ECO:0000269|PubMed:16505352}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF094479; AAD41243.1; -; mRNA.
DR EMBL; BC018307; AAH18307.1; -; mRNA.
DR CCDS; CCDS26160.1; -.
DR RefSeq; NP_034140.1; NM_010010.1.
DR AlphaFoldDB; Q9WVK8; -.
DR SMR; Q9WVK8; -.
DR BioGRID; 199032; 1.
DR STRING; 10090.ENSMUSP00000021684; -.
DR iPTMnet; Q9WVK8; -.
DR PhosphoSitePlus; Q9WVK8; -.
DR SwissPalm; Q9WVK8; -.
DR MaxQB; Q9WVK8; -.
DR PaxDb; Q9WVK8; -.
DR PRIDE; Q9WVK8; -.
DR ProteomicsDB; 285280; -.
DR Antibodypedia; 14316; 304 antibodies from 31 providers.
DR DNASU; 13116; -.
DR Ensembl; ENSMUST00000021684; ENSMUSP00000021684; ENSMUSG00000021259.
DR GeneID; 13116; -.
DR KEGG; mmu:13116; -.
DR UCSC; uc007ozo.1; mouse.
DR CTD; 10858; -.
DR MGI; MGI:1341877; Cyp46a1.
DR VEuPathDB; HostDB:ENSMUSG00000021259; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000156927; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q9WVK8; -.
DR OMA; IAGRTMF; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q9WVK8; -.
DR TreeFam; TF352037; -.
DR BRENDA; 1.14.14.25; 3474.
DR Reactome; R-MMU-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR Reactome; R-MMU-211976; Endogenous sterols.
DR UniPathway; UPA00229; -.
DR UniPathway; UPA01058; -.
DR BioGRID-ORCS; 13116; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q9WVK8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9WVK8; protein.
DR Bgee; ENSMUSG00000021259; Expressed in visual cortex and 119 other tissues.
DR ExpressionAtlas; Q9WVK8; baseline and differential.
DR Genevisible; Q9WVK8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0033781; F:cholesterol 24-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008395; F:steroid hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0062184; F:testosterone 16-beta-hydroxylase activity; IEA:RHEA.
DR GO; GO:0006707; P:cholesterol catabolic process; IDA:UniProtKB.
DR GO; GO:0042448; P:progesterone metabolic process; ISS:UniProtKB.
DR GO; GO:1903044; P:protein localization to membrane raft; IDA:ARUK-UCL.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR039983; CYP46A1.
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; PTHR24293; PTHR24293; 1.
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 Cell projection; Cholesterol metabolism; Endoplasmic reticulum; Heme; Iron;
KW Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW Oxidoreductase; Reference proteome; Steroid metabolism; Sterol metabolism;
KW Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..500
FT /note="Cholesterol 24-hydroxylase"
FT /id="PRO_0000051995"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 437
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:Q9Y6A2"
SQ SEQUENCE 500 AA; 56814 MW; F0F178FA65820FF2 CRC64;
MSPGLLLLGS AVLLAFGLCC TFVHRARSRY EHIPGPPRPS FLLGHLPYFW KKDEDCGRVL
QDVFLDWAKK YGPVVRVNVF YKTSVIVTSP ESVKKFLMST KYNKDSKMYR ALQTVFGERL
FGQGLVSECD YGRWYKQRKV MDLAFSRSSL VSLMETFNEK AEQLVEILEA KADGQTPVSM
QDMLTCATID ILAKAAFGME TSMLLGAQKP LSQAVKVMLE GISASRNTLA KFMPGKRKQL
REIRESIRLL RQVGKDWVQR RREALKRGED MPADILTQIL KAEEGAQDDE VLLDNFVTFF
IAGHETSANH LAFTVMELSR QPEIVARLQA EVDEVVGSKR HLDYEDLGRL QYLSQVLKES
LRLYPPAWGT FRLLEEETLI DGVRVPGNTP LLFSTYVMGR MDTYFEDPLT FNPDRFGPGA
PKPRFTYFPF SLGHRSCIGQ QFAQMEVKVV MAKLLQRIEF RLVPGQRFGL QEQATLKPLD
PVLCTLRPRG WQPAPPPPPC
