CP2CN_RAT
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 03-AUG-2022, entry version 151.
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 [NADPH--
CC hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49884, 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: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 [NADPH--
CC hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49880, 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: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 [NADPH--
CC hemoprotein reductase] = (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49876, 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: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 [NADPH--
CC hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49860, 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: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 [NADPH--
CC hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49856, 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: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 [NADPH--
CC hemoprotein reductase] = 8,9-epoxy-(5Z,11Z,14Z,17Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:52168, 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: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 [NADPH--
CC 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 [NADPH--
CC 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 [NADPH--
CC 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 [NADPH--
CC 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 (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate (total epoxygenase activity)
CC {ECO:0000269|PubMed:15766564};
CC Vmax=22 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z,17Z)-
CC 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; P24470; -.
DR PRIDE; P24470; -.
DR UCSC; RGD:620370; rat.
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; IDA:RGD.
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:0008395; F:steroid hydroxylase activity; 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:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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 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
