ID   CP2CN_RAT               Reviewed;         494 AA.
AC   P24470; Q63914; Q64534;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Cytochrome P450 2C23;
DE            EC=1.14.14.- {ECO:0000269|PubMed:14742258, ECO:0000269|PubMed:15766564, ECO:0000269|PubMed:8246128};
DE   AltName: Full=Arachidonic acid epoxygenase;
DE   AltName: Full=CYPIIC23;
GN   Name=Cyp2c23 {ECO:0000303|PubMed:14742258, ECO:0000312|RGD:620370};
GN   Synonyms=Cyp2c-23;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=2263487; DOI=10.1093/nar/18.23.7156;
RA   Cook E.A., Groenewegen W.A., Gloger I.S., Piggott J.R., Suckling K.E.,
RA   Wolf C.R.;
RT   "cDNA and deduced amino acid sequence of a novel cytochrome P-450 from
RT   female rat liver mRNA with high homology to P-450 IIC family.";
RL   Nucleic Acids Res. 18:7156-7156(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=8514789; DOI=10.1016/s0021-9258(19)38686-7;
RA   Karara A., Makita K., Jacobson H.R., Falk J.R., Guengerich P.F.,
RA   Dubois R.N., Capdevila J.H.;
RT   "Molecular cloning, expression, and enzymatic characterization of the rat
RT   kidney cytochrome P-450 arachidonic acid epoxygenase.";
RL   J. Biol. Chem. 268:13565-13570(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-86, FUNCTION, AND PATHWAY.
RC   TISSUE=Kidney;
RX   PubMed=8246128;
RA   Imaoka S., Wedlund P.J., Ogawa H., Kimura S., Gonzalez F.J., Kim H.Y.;
RT   "Identification of CYP2C23 expressed in rat kidney as an arachidonic acid
RT   epoxygenase.";
RL   J. Pharmacol. Exp. Ther. 267:1012-1016(1993).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=10491410; DOI=10.1172/jci7013;
RA   Holla V.R., Makita K., Zaphiropoulos P.G., Capdevila J.H.;
RT   "The kidney cytochrome P-450 2C23 arachidonic acid epoxygenase is
RT   upregulated during dietary salt loading.";
RL   J. Clin. Invest. 104:751-760(1999).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INDUCTION BY FENOFIBRATE.
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   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15766564; DOI=10.1016/j.bbrc.2005.02.103;
RA   Barbosa-Sicard E., Markovic M., Honeck H., Christ B., Muller D.N.,
RA   Schunck W.H.;
RT   "Eicosapentaenoic acid metabolism by cytochrome P450 enzymes of the CYP2C
RT   subfamily.";
RL   Biochem. Biophys. Res. Commun. 329:1275-1281(2005).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in polyunsaturated
CC       fatty acids (PUFAs) metabolism and signaling. Catalyzes preferentially
CC       the epoxidation of double bonds of PUFAs. Converts arachidonic acid
CC       (ARA, C20:4(n-6)) primarily to stereospecific products 8R,9S-,
CC       11R,12S-, and 14S,15R-EET (PubMed:8246128, PubMed:14742258,
CC       PubMed:10491410). Plays a major role in the formation of EETs and
CC       hydroxy-EETs (HEETs) in kidney (PubMed:10491410, PubMed:14742258). Via
CC       EETs may inhibit the epithelial sodium channels (ENaCs) in nephron
CC       segments, preventing excessive sodium absorption during high dietary
CC       salt intake (By similarity). Participates in the formation of anti-
CC       inflammatory hydroxyepoxyeicosatrienoic acids (HEETs) by converting 20-
CC       hydroxyeicosatetraenoic acid (20-HETE) to 20,8,9-HEET, an activator of
CC       PPARA (PubMed:14742258). Metabolizes eicosapentaenoic acid (EPA,
CC       C20:5(n-3)) to epoxyeicosatetraenoic acid (EETeTr) regioisomers, 8,9-,
CC       11,12-, 14,15-, and 17,18-EETeTr, preferentially producing 17R,18S
CC       enantiomer (PubMed:15766564). Mechanistically, uses molecular oxygen
CC       inserting one oxygen atom into a substrate, and reducing the second
CC       into a water molecule, with two electrons provided by NADPH via
CC       cytochrome P450 reductase (NADPH--hemoprotein reductase)
CC       (PubMed:8246128). {ECO:0000250|UniProtKB:E9Q5K4,
CC       ECO:0000269|PubMed:10491410, ECO:0000269|PubMed:14742258,
CC       ECO:0000269|PubMed:15766564, ECO:0000269|PubMed:8246128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49884, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131975; Evidence={ECO:0000269|PubMed:10491410};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49885;
CC         Evidence={ECO:0000305|PubMed:10491410};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49880, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131970; Evidence={ECO:0000269|PubMed:10491410};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881;
CC         Evidence={ECO:0000305|PubMed:10491410};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (11S,12R)-epoxy-(5Z,8Z,14Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49876, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131969; Evidence={ECO:0000269|PubMed:10491410};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49877;
CC         Evidence={ECO:0000305|PubMed:10491410};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131965; Evidence={ECO:0000269|PubMed:10491410};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC         Evidence={ECO:0000305|PubMed:10491410};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131964; Evidence={ECO:0000269|PubMed:10491410};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
CC         Evidence={ECO:0000305|PubMed:10491410};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 8,9-epoxy-(5Z,11Z,14Z,17Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52168, 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:58562,
CC         ChEBI:CHEBI:136439; Evidence={ECO:0000269|PubMed:15766564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52169;
CC         Evidence={ECO:0000305|PubMed:15766564};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 11,12-epoxy-(5Z,8Z,14Z,17Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52172, 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:58562,
CC         ChEBI:CHEBI:136441; Evidence={ECO:0000269|PubMed:15766564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52173;
CC         Evidence={ECO:0000305|PubMed:15766564};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 14,15-epoxy-(5Z,8Z,11Z,17Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52176, 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:58562,
CC         ChEBI:CHEBI:136443; Evidence={ECO:0000269|PubMed:15766564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52177;
CC         Evidence={ECO:0000305|PubMed:15766564};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39779, 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:58562,
CC         ChEBI:CHEBI:76634; Evidence={ECO:0000269|PubMed:15766564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC         Evidence={ECO:0000305|PubMed:15766564};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (17S,18R)-epoxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39783, 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:58562,
CC         ChEBI:CHEBI:76635; Evidence={ECO:0000269|PubMed:15766564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39784;
CC         Evidence={ECO:0000305|PubMed:15766564};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:64980, 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:76624,
CC         ChEBI:CHEBI:137474; Evidence={ECO:0000269|PubMed:14742258};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64981;
CC         Evidence={ECO:0000305|PubMed:14742258};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P33261};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.1 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (total epoxygenase
CC         activity) {ECO:0000269|PubMed:15766564};
CC         KM=14.7 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate (total
CC         epoxygenase activity) {ECO:0000269|PubMed:15766564};
CC         Vmax=14.1 nmol/min/nmol enzyme toward
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate (total epoxygenase activity)
CC         {ECO:0000269|PubMed:15766564};
CC         Vmax=22 nmol/min/nmol enzyme toward
CC         (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate (total epoxygenase activity)
CC         {ECO:0000269|PubMed:15766564};
CC   -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC       {ECO:0000269|PubMed:10491410, ECO:0000305|PubMed:8246128}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14742258}. Microsome membrane
CC       {ECO:0000269|PubMed:14742258}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney and liver. Expressed in
CC       cortical tubules of kidney (at protein level).
CC       {ECO:0000269|PubMed:14742258, ECO:0000269|PubMed:2263487,
CC       ECO:0000269|PubMed:8514789}.
CC   -!- INDUCTION: Constitutively expressed. Up-regulated by fenofibrate.
CC       {ECO:0000269|PubMed:14742258}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X55446; CAA39087.1; -; mRNA.
DR   EMBL; U04733; AAA03716.1; -; mRNA.
DR   EMBL; S67064; AAB29022.1; -; mRNA.
DR   PIR; A46588; A46588.
DR   PIR; S13101; S13101.
DR   AlphaFoldDB; P24470; -.
DR   SMR; P24470; -.
DR   IntAct; P24470; 2.
DR   STRING; 10116.ENSRNOP00000017840; -.
DR   BindingDB; P24470; -.
DR   ChEMBL; CHEMBL2772; -.
DR   SwissLipids; SLP:000001688; -.
DR   iPTMnet; P24470; -.
DR   PhosphoSitePlus; P24470; -.
DR   PaxDb; 10116-ENSRNOP00000017840; -.
DR   UCSC; RGD:620370; rat.
DR   AGR; RGD:620370; -.
DR   RGD; 620370; Cyp2c23.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P24470; -.
DR   PhylomeDB; P24470; -.
DR   UniPathway; UPA00383; -.
DR   PRO; PR:P24470; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0008405; F:arachidonic acid 11,12-epoxygenase activity; IDA:UniProtKB.
DR   GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; IDA:UniProtKB.
DR   GO; GO:0008392; F:arachidonic acid epoxygenase activity; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; NAS:RGD.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; IDA:UniProtKB.
DR   GO; GO:0046456; P:icosanoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20665; CYP2C-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24300:SF392; CYTOCHROME P450 2C44; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endoplasmic reticulum; Fatty acid metabolism; Heme; Iron;
KW   Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW   Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..494
FT                   /note="Cytochrome P450 2C23"
FT                   /id="PRO_0000051711"
FT   BINDING         439
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:P33261"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00176"
FT   MOD_RES         253
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64458"
FT   MOD_RES         379
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64458"
FT   CONFLICT        38..54
FT                   /note="TPLPIIGNLLQLNLKDI -> HPPSHYWESTATEPQGH (in Ref. 1;
FT                   CAA39087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="R -> W (in Ref. 1; CAA39087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366..367
FT                   /note="LP -> VG (in Ref. 1; CAA39087)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  56433 MW;  BB6529F9953B540E CRC64;
     MELLGFTTLA LVVSVTCLSL LSVWTKLRTR GRLPPGPTPL PIIGNLLQLN LKDIPASLSK
     LAKEYGPVYT LYFGTSPTVV LHGYDVVKEA LLQQGDEFLG RGPLPIIEDT HKGYGLIFSN
     GERWKVMRRF SLMTLRNFGM GKRSLEERVQ EEARCLVEEL QKTKAQPFDP TFILACAPCN
     VICSILFNDR FQYNDKTFLN LMDLLNKNFQ QVNSVWCQMY NLWPTIIKYL PGKHIEFAKR
     IDDVKNFILE KVKEHQKSLD PANPRDYIDC FLSKIEEEKD NLKSEFHLEN LAVCGSNLFT
     AGTETTSTTL RFGLLLLMKY PEVQAKVHEE LDRVIGRHQP PSMKDKMKLP YTDAVLHEIQ
     RYITLLPSSL PHAVVQDTKF RDYVIPKGTT VLPMLSSVML DQKEFANPEK FDPGHFLDKN
     GCFKKTDYFV PFSLGKRACV GESLARMELF LFFTTLLQKF SLKTLVEPKD LDIKPITTGI
     INLPPPYKLC LVPR
//