CP7A1_MOUSE
ID CP7A1_MOUSE Reviewed; 503 AA.
AC Q64505; Q8BFR7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cytochrome P450 7A1 {ECO:0000250|UniProtKB:P22680};
DE AltName: Full=24-hydroxycholesterol 7-alpha-hydroxylase {ECO:0000250|UniProtKB:P22680};
DE EC=1.14.14.26 {ECO:0000250|UniProtKB:P22680};
DE AltName: Full=CYPVII;
DE AltName: Full=Cholesterol 7-alpha-hydroxylase {ECO:0000303|PubMed:8088795};
DE AltName: Full=Cholesterol 7-alpha-monooxygenase;
DE EC=1.14.14.23 {ECO:0000250|UniProtKB:P18125};
GN Name=Cyp7a1 {ECO:0000303|PubMed:14522988, ECO:0000312|MGI:MGI:106091};
GN Synonyms=Cyp7;
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 [GENOMIC DNA].
RX PubMed=8088795; DOI=10.1006/geno.1994.1250;
RA Tzung K.W., Ishimura-Oka K., Kihara S., Oka K., Chan L.;
RT "Structure of the mouse cholesterol 7 alpha-hydroxylase gene.";
RL Genomics 21:244-247(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, INDUCTION BY FASTING, AND PATHWAY.
RX PubMed=14522988; DOI=10.1074/jbc.m309736200;
RA Shin D.J., Campos J.A., Gil G., Osborne T.F.;
RT "PGC-1alpha activates CYP7A1 and bile acid biosynthesis.";
RL J. Biol. Chem. 278:50047-50052(2003).
RN [5]
RP INDUCTION BY FASTING.
RX PubMed=17636037; DOI=10.1210/me.2007-0196;
RA Ponugoti B., Fang S., Kemper J.K.;
RT "Functional interaction of hepatic nuclear factor-4 and peroxisome
RT proliferator-activated receptor-gamma coactivator 1alpha in CYP7A1
RT regulation is inhibited by a key lipogenic activator, sterol regulatory
RT element-binding protein-1c.";
RL Mol. Endocrinol. 21:2698-2712(2007).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC endogenous cholesterol and its oxygenated derivatives (oxysterols) (By
CC similarity). Mechanistically, uses molecular oxygen inserting one
CC oxygen atom into a substrate, and reducing the second into a water
CC molecule, with two electrons provided by NADPH via cytochrome P450
CC reductase (CPR; NADPH-ferrihemoprotein reductase) (By similarity).
CC Functions as a critical regulatory enzyme of bile acid biosynthesis and
CC cholesterol homeostasis. Catalyzes the hydroxylation of carbon hydrogen
CC bond at 7-alpha position of cholesterol, a rate-limiting step in
CC cholesterol catabolism and bile acid biosynthesis (Probable). 7-alpha
CC hydroxylates several oxysterols, including 4beta-hydroxycholesterol and
CC 24-hydroxycholesterol. Catalyzes the oxidation of the 7,8 double bond
CC of 7-dehydrocholesterol and lathosterol with direct and predominant
CC formation of the 7-keto derivatives (By similarity).
CC {ECO:0000250|UniProtKB:P22680, ECO:0000305|PubMed:14522988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC 7alpha-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:21812, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:17500, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.23;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21813;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4beta-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 4beta,7alpha-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46120,
CC Rhea:RHEA-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:85779;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46121;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lathosterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC 7alpha,8alpha-epoxy-5alpha-cholestan-3beta-ol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53256, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17168,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137063;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53257;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lathosterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC 5alpha-cholestan-7-oxo-3beta-ol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:53252, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17168, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:137062;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53253;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-dehydrocholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 7-oxocholesterol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:53248, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17759, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:64294;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53249;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (24S)-7alpha-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46124,
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:37640, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC EC=1.14.14.26; Evidence={ECO:0000250|UniProtKB:P22680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46125;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24R)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (24R)-7alpha-dihydroxycholesterol + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:16093,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:50516,
CC ChEBI:CHEBI:50518, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16094;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P22680};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000269|PubMed:14522988}.
CC -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC {ECO:0000250|UniProtKB:P22680}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P22680}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P22680}. Microsome membrane
CC {ECO:0000250|UniProtKB:P22680}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P22680}.
CC -!- INDUCTION: Up-regulated by fasting, returns to ground state upon
CC feeding. Up-regulated by experimentally induced diabetes. Down-
CC regulated by insulin treatment. {ECO:0000269|PubMed:14522988,
CC ECO:0000269|PubMed:17636037}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; L23754; AAA68867.1; -; Genomic_DNA.
DR EMBL; AK050020; BAC34033.1; -; mRNA.
DR EMBL; AK050210; BAC34123.1; -; mRNA.
DR EMBL; AK050220; BAC34131.1; -; mRNA.
DR EMBL; AK050260; BAC34150.1; -; mRNA.
DR EMBL; AL772306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17950.1; -.
DR PIR; A54779; A54779.
DR RefSeq; NP_031850.2; NM_007824.2.
DR RefSeq; XP_006537666.1; XM_006537603.1.
DR AlphaFoldDB; Q64505; -.
DR SMR; Q64505; -.
DR STRING; 10090.ENSMUSP00000029905; -.
DR ChEMBL; CHEMBL2212; -.
DR iPTMnet; Q64505; -.
DR PhosphoSitePlus; Q64505; -.
DR jPOST; Q64505; -.
DR MaxQB; Q64505; -.
DR PaxDb; Q64505; -.
DR PRIDE; Q64505; -.
DR ProteomicsDB; 284110; -.
DR Antibodypedia; 2602; 160 antibodies from 30 providers.
DR DNASU; 13122; -.
DR Ensembl; ENSMUST00000029905; ENSMUSP00000029905; ENSMUSG00000028240.
DR GeneID; 13122; -.
DR KEGG; mmu:13122; -.
DR UCSC; uc008rxk.1; mouse.
DR CTD; 1581; -.
DR MGI; MGI:106091; Cyp7a1.
DR VEuPathDB; HostDB:ENSMUSG00000028240; -.
DR eggNOG; KOG0684; Eukaryota.
DR GeneTree; ENSGT00940000153141; -.
DR HOGENOM; CLU_018012_1_3_1; -.
DR InParanoid; Q64505; -.
DR OMA; VCCCLWL; -.
DR OrthoDB; 864748at2759; -.
DR PhylomeDB; Q64505; -.
DR TreeFam; TF105090; -.
DR BRENDA; 1.14.14.23; 3474.
DR Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-MMU-211976; Endogenous sterols.
DR UniPathway; UPA00221; -.
DR UniPathway; UPA01058; -.
DR BioGRID-ORCS; 13122; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Cyp7a1; mouse.
DR PRO; PR:Q64505; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q64505; protein.
DR Bgee; ENSMUSG00000028240; Expressed in liver and 18 other tissues.
DR Genevisible; Q64505; MM.
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:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0033782; F:24-hydroxycholesterol 7alpha-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008123; F:cholesterol 7-alpha-monooxygenase activity; IDA:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IEA:Ensembl.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0038183; P:bile acid signaling pathway; IEA:Ensembl.
DR GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0006707; P:cholesterol catabolic process; IDA:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0070859; P:positive regulation of bile acid biosynthetic process; TAS:BHF-UCL.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISO:MGI.
DR GO; GO:0070857; P:regulation of bile acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR030681; Cholesterol_7a_monooxygenase.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR024204; Cyt_P450_CYP7A1-type.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24304:SF1; PTHR24304:SF1; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF500625; Cytochrome_CYP7A1; 1.
DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Cholesterol metabolism; Endoplasmic reticulum; Heme; Iron;
KW Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW Oxidoreductase; Reference proteome; Steroid metabolism; Sterol metabolism;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..503
FT /note="Cytochrome P450 7A1"
FT /id="PRO_0000051902"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 444
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:P22680"
FT CONFLICT 197
FT /note="S -> T (in Ref. 1; AAA68867)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="F -> L (in Ref. 1; AAA68867)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="A -> S (in Ref. 1; AAA68867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57262 MW; F7F8BC2CDD2C43D1 CRC64;
MMSISLIWGI AVVVSCCIWF IIGIRRRKVG EPPLDNGLIP YLGCALKFGS NPLEFLRAKQ
RKHGHVFTCK LMGKYVHFIT NSLSYHKVLC HGKYFDWKKF HYTTSAKAFG HRSIDPSDGN
TTENINKTFN KTLQGDALCS LSEAMMQNLQ SVMRPPGLPK SKSAVWVTEG MYAFCYRVMF
EAGYLTLFGK DISKTDSQRA FIQNNLDSFK QFDQVFPALV AGVPIHLFKT AHKARERLAE
SLKHKNLYMR DQVSELIRLR MFLNDTLSTF DDMEKAKTHL VILWASQANT IPATFWSLFQ
MIRSPEAMKA ASEEVNGALQ SAGQELSSGG NAIYLDQEQL NNLPVLDSII KEALRLSSAS
LNIRTAKEDF TLHLEDGSYN IRKDDIIALY PQLMHLDPEI YPDPLTFKYD RYLDESGKAK
TTFYRNGNKL KYFYMPFGSG ATICPGRLFA VQEIKQFLIL MLSYFELELV ESHTKCPPLD
QSRAGLGILP PLNDIEFKYK LKH
