PPARA_MOUSE
ID PPARA_MOUSE Reviewed; 468 AA.
AC P23204;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Peroxisome proliferator-activated receptor alpha;
DE Short=PPAR-alpha;
DE AltName: Full=Nuclear receptor subfamily 1 group C member 1;
GN Name=Ppara; Synonyms=Nr1c1, Ppar;
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].
RX PubMed=2129546; DOI=10.1038/347645a0;
RA Issemann I., Green S.;
RT "Activation of a member of the steroid hormone receptor superfamily by
RT peroxisome proliferators.";
RL Nature 347:645-650(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8123021; DOI=10.1006/bbrc.1994.1222;
RA Gearing K.L., Crickmore A., Gustafsson J.-A.;
RT "Structure of the mouse peroxisome proliferator activated receptor alpha
RT gene.";
RL Biochem. Biophys. Res. Commun. 199:255-263(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 413-468.
RC STRAIN=Swiss Webster; TISSUE=Liver;
RX PubMed=7588749; DOI=10.1111/j.1432-1033.1995.219_1.x;
RA Jones P.S., Savory R., Barratt P., Bell A.R., Gray T.J.B., Jenkins N.A.,
RA Gilbert D.J., Copeland N.G., Bell D.R.;
RT "Chromosomal localisation, inducibility, tissue-specific expression and
RT strain differences in three murine peroxisome-proliferator-activated-
RT receptor genes.";
RL Eur. J. Biochem. 233:219-226(1995).
RN [5]
RP INTERACTION WITH PPARBP.
RX PubMed=9325263; DOI=10.1074/jbc.272.41.25500;
RA Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.;
RT "Isolation and characterization of PBP, a protein that interacts with
RT peroxisome proliferator-activated receptor.";
RL J. Biol. Chem. 272:25500-25506(1997).
RN [6]
RP INTERACTION WITH AKAP13.
RX PubMed=9627117; DOI=10.1038/sj.onc.1201783;
RA Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K.,
RA Gray K., Gutkind S., Segars J.;
RT "Characterization of Brx, a novel Dbl family member that modulates estrogen
RT receptor action.";
RL Oncogene 16:2513-2526(1998).
RN [7]
RP INTERACTION WITH NCOA6.
RX PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
RA Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.;
RT "Isolation and characterization of peroxisome proliferator-activated
RT receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR.";
RL J. Biol. Chem. 275:13510-13516(2000).
RN [8]
RP IDENTIFICATION AS RECEPTOR FOR OLEYLETHANOLAMIDE, AND FUNCTION.
RX PubMed=12955147; DOI=10.1038/nature01921;
RA Fu J., Gaetani S., Oveisi F., Lo Verme J., Serrano A.,
RA Rodriguez De Fonseca F., Rosengarth A., Luecke H., Di Giacomo B.,
RA Tarzia G., Piomelli D.;
RT "Oleylethanolamide regulates feeding and body weight through activation of
RT the nuclear receptor PPAR-alpha.";
RL Nature 425:90-93(2003).
RN [9]
RP INTERACTION WITH LIPN1.
RX PubMed=16950137; DOI=10.1016/j.cmet.2006.08.005;
RA Finck B.N., Gropler M.C., Chen Z., Leone T.C., Croce M.A., Harris T.E.,
RA Lawrence J.C. Jr., Kelly D.P.;
RT "Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha
RT regulatory pathway.";
RL Cell Metab. 4:199-210(2006).
RN [10]
RP INTERACTION WITH PRDM16.
RX PubMed=18719582; DOI=10.1038/nature07182;
RA Seale P., Bjork B., Yang W., Kajimura S., Chin S., Kuang S., Scime A.,
RA Devarakonda S., Conroe H.M., Erdjument-Bromage H., Tempst P.,
RA Rudnicki M.A., Beier D.R., Spiegelman B.M.;
RT "PRDM16 controls a brown fat/skeletal muscle switch.";
RL Nature 454:961-967(2008).
RN [11]
RP IDENTIFICATION OF 1-PALMITOYL-2-OLEOYL-SN-GLYCEROL-3-PHOSPHOCHOLINE AS A
RP PHYSIOLOGICAL LIGAND, DNA-BINDING, FUNCTION, AND MUTAGENESIS OF CYS-119 AND
RP CYS-122.
RX PubMed=19646743; DOI=10.1016/j.cell.2009.05.036;
RA Chakravarthy M.V., Lodhi I.J., Yin L., Malapaka R.R., Xu H.E., Turk J.,
RA Semenkovich C.F.;
RT "Identification of a physiologically relevant endogenous ligand for
RT PPARalpha in liver.";
RL Cell 138:476-488(2009).
RN [12]
RP FUNCTION IN CIRCADIAN RHYTHMS, INTERACTION WITH PER2, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF LYS-292 AND 459-LEU--TYR-468.
RX PubMed=20159955; DOI=10.1101/gad.564110;
RA Schmutz I., Ripperger J.A., Baeriswyl-Aebischer S., Albrecht U.;
RT "The mammalian clock component PERIOD2 coordinates circadian output by
RT interaction with nuclear receptors.";
RL Genes Dev. 24:345-357(2010).
RN [13]
RP INTERACTION WITH CRY1 AND CRY2.
RX PubMed=28683290; DOI=10.1016/j.cmet.2017.06.002;
RA Jordan S.D., Kriebs A., Vaughan M., Duglan D., Fan W., Henriksson E.,
RA Huber A.L., Papp S.J., Nguyen M., Afetian M., Downes M., Yu R.T.,
RA Kralli A., Evans R.M., Lamia K.A.;
RT "CRY1/2 selectively repress PPARdelta and limit exercise capacity.";
RL Cell Metab. 26:243-255(2017).
CC -!- FUNCTION: Ligand-activated transcription factor. Key regulator of lipid
CC metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-
CC glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by
CC oleylethanolamide, a naturally occurring lipid that regulates satiety.
CC Receptor for peroxisome proliferators such as hypolipidemic drugs and
CC fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty
CC acids. Functions as transcription activator for the ACOX1 and P450
CC genes. Transactivation activity requires heterodimerization with RXRA
CC and is antagonized by NR2C2. May be required for the propagation of
CC clock information to metabolic pathways regulated by PER2.
CC {ECO:0000269|PubMed:12955147, ECO:0000269|PubMed:19646743,
CC ECO:0000269|PubMed:20159955}.
CC -!- SUBUNIT: Heterodimer; with RXRA. This heterodimerization is required
CC for DNA binding and transactivation activity. Interacts with NCOA3
CC coactivator. Interacts with CITED2; the interaction stimulates its
CC transcriptional activity. Also interacts with PPARBP in vitro.
CC Interacts with AKAP13, LPIN1, PRDM16 and coactivator NCOA6. Interacts
CC with ASXL1 and ASXL2. Interacts with PER2. Interacts with SIRT1; the
CC interaction seems to be modulated by NAD(+) levels (By similarity).
CC Interacts with CRY1 and CRY2 (PubMed:28683290).
CC {ECO:0000250|UniProtKB:Q07869, ECO:0000269|PubMed:10788465,
CC ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:18719582,
CC ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:28683290,
CC ECO:0000269|PubMed:9325263, ECO:0000269|PubMed:9627117}.
CC -!- INTERACTION:
CC P23204; O88559: Men1; NbExp=2; IntAct=EBI-5273083, EBI-3990176;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:20159955}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney and heart. Very
CC weakly expressed in brain and testis.
CC -!- DEVELOPMENTAL STAGE: It appears first at 13.5 dpc and increases until
CC birth.
CC -!- DISEASE: Note=Peroxisome proliferators are a diverse group of chemicals
CC that include hypolipidaemic drugs, herbicides and industrial
CC plasticisers. Administration of these chemicals to rodents results in
CC the dramatic proliferation of hepatic peroxisomes as well as liver
CC hyperplasia.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; X57638; CAA40856.1; -; mRNA.
DR EMBL; X75289; CAA53042.1; -; Genomic_DNA.
DR EMBL; X75290; CAA53042.1; JOINED; Genomic_DNA.
DR EMBL; X75291; CAA53042.1; JOINED; Genomic_DNA.
DR EMBL; X75292; CAA53042.1; JOINED; Genomic_DNA.
DR EMBL; X75293; CAA53042.1; JOINED; Genomic_DNA.
DR EMBL; X75294; CAA53042.1; JOINED; Genomic_DNA.
DR EMBL; BC016892; AAH16892.1; -; mRNA.
DR EMBL; X89577; CAA61754.1; -; mRNA.
DR CCDS; CCDS27721.1; -.
DR PIR; JC2085; JC2085.
DR RefSeq; NP_001106889.1; NM_001113418.1.
DR RefSeq; NP_035274.2; NM_011144.6.
DR RefSeq; XP_006520682.1; XM_006520619.1.
DR RefSeq; XP_006520683.1; XM_006520620.3.
DR RefSeq; XP_006520684.1; XM_006520621.3.
DR RefSeq; XP_006520685.1; XM_006520622.3.
DR RefSeq; XP_006520686.1; XM_006520623.3.
DR RefSeq; XP_011243818.1; XM_011245516.2.
DR RefSeq; XP_011243819.1; XM_011245517.2.
DR RefSeq; XP_011243821.1; XM_011245519.2.
DR AlphaFoldDB; P23204; -.
DR SMR; P23204; -.
DR BioGRID; 202317; 18.
DR CORUM; P23204; -.
DR DIP; DIP-5958N; -.
DR IntAct; P23204; 5.
DR MINT; P23204; -.
DR STRING; 10090.ENSMUSP00000105049; -.
DR BindingDB; P23204; -.
DR ChEMBL; CHEMBL2128; -.
DR DrugCentral; P23204; -.
DR GuidetoPHARMACOLOGY; 593; -.
DR iPTMnet; P23204; -.
DR PhosphoSitePlus; P23204; -.
DR PaxDb; P23204; -.
DR PRIDE; P23204; -.
DR ProteomicsDB; 289733; -.
DR Antibodypedia; 13823; 811 antibodies from 39 providers.
DR DNASU; 19013; -.
DR Ensembl; ENSMUST00000057979; ENSMUSP00000059719; ENSMUSG00000022383.
DR Ensembl; ENSMUST00000109422; ENSMUSP00000105049; ENSMUSG00000022383.
DR Ensembl; ENSMUST00000109423; ENSMUSP00000105050; ENSMUSG00000022383.
DR GeneID; 19013; -.
DR KEGG; mmu:19013; -.
DR UCSC; uc007xdj.2; mouse.
DR CTD; 5465; -.
DR MGI; MGI:104740; Ppara.
DR VEuPathDB; HostDB:ENSMUSG00000022383; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000157097; -.
DR HOGENOM; CLU_007368_4_1_1; -.
DR InParanoid; P23204; -.
DR OMA; EMGSIQE; -.
DR OrthoDB; 1240230at2759; -.
DR PhylomeDB; P23204; -.
DR TreeFam; TF316304; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 19013; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Ppara; mouse.
DR PRO; PR:P23204; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P23204; protein.
DR Bgee; ENSMUSG00000022383; Expressed in left lobe of liver and 110 other tissues.
DR ExpressionAtlas; P23204; baseline and differential.
DR Genevisible; P23204; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
DR GO; GO:0051525; F:NFAT protein binding; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:MGI.
DR GO; GO:0003707; F:nuclear steroid receptor activity; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035095; P:behavioral response to nicotine; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IMP:ARUK-UCL.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0070166; P:enamel mineralization; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IMP:MGI.
DR GO; GO:0006006; P:glucose metabolic process; TAS:MGI.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010876; P:lipid localization; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; ISO:MGI.
DR GO; GO:0032099; P:negative regulation of appetite; IMP:UniProtKB.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; ISO:MGI.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:MGI.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISO:MGI.
DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; ISO:MGI.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; IMP:BHF-UCL.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:MGI.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0010565; P:regulation of cellular ketone metabolic process; ISO:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IDA:UniProtKB.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR003074; 1Cnucl_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003076; PPAR-alpha.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01288; PROXISOMEPAR.
DR PRINTS; PR01289; PROXISOMPAAR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; DNA-binding; Lipid-binding; Metal-binding;
KW Nucleus; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..468
FT /note="Peroxisome proliferator-activated receptor alpha"
FT /id="PRO_0000053482"
FT DOMAIN 239..466
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 99..173
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 102..122
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..161
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 304..433
FT /note="Required for heterodimerization with RXRA"
FT /evidence="ECO:0000250"
FT SITE 433
FT /note="Essential for heterodimerization with RXRA"
FT /evidence="ECO:0000250"
FT MUTAGEN 119
FT /note="C->A: Reduces DNA binding and strongly decreases
FT transcriptional activation; when associated with A-122."
FT /evidence="ECO:0000269|PubMed:19646743"
FT MUTAGEN 122
FT /note="C->A: Reduces DNA binding and strongly decreases
FT transcriptional activation; when associated with A-119."
FT /evidence="ECO:0000269|PubMed:19646743"
FT MUTAGEN 292
FT /note="K->A: No effect on interaction with PER2."
FT /evidence="ECO:0000269|PubMed:20159955"
FT MUTAGEN 459..468
FT /note="Missing: Slightly reduces interaction with PER2."
FT /evidence="ECO:0000269|PubMed:20159955"
FT CONFLICT 75
FT /note="A -> R (in Ref. 1; CAA40856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 52347 MW; 2930A5191C610B6B CRC64;
MVDTESPICP LSPLEADDLE SPLSEEFLQE MGNIQEISQS IGEESSGSFG FADYQYLGSC
PGSEGSVITD TLSPASSPSS VSCPVIPAST DESPGSALNI ECRICGDKAS GYHYGVHACE
GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE
KAKLKAEILT CEHDLKDSET ADLKSLGKRI HEAYLKNFNM NKVKARVILA GKTSNNPPFV
IHDMETLCMA EKTLVAKMVA NGVEDKEAEV RFFHCCQCMS VETVTELTEF AKAIPGFANL
DLNDQVTLLK YGVYEAIFTM LSSLMNKDGM LIAYGNGFIT REFLKNLRKP FCDIMEPKFD
FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNIGYIEKL QEGIVHVLKL HLQSNHPDDT
FLFPKLLQKM VDLRQLVTEH AQLVQVIKKT ESDAALHPLL QEIYRDMY
