ID   NR1I3_MOUSE             Reviewed;         358 AA.
AC   O35627; O35628; Q3V008;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 196.
DE   RecName: Full=Nuclear receptor subfamily 1 group I member 3;
DE   AltName: Full=Constitutive androstane receptor;
DE            Short=CAR;
DE   AltName: Full=Orphan nuclear receptor MB67;
GN   Name=Nr1i3; Synonyms=Car;
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] (ISOFORMS CAR1 AND CAR2).
RC   TISSUE=Liver;
RX   PubMed=9295294; DOI=10.1074/jbc.272.38.23565;
RA   Choi H.-S., Chung M., Tzameli I., Simha D., Lee Y.-K., Seol W., Moore D.D.;
RT   "Differential transactivation by two isoforms of the orphan nuclear hormone
RT   receptor CAR.";
RL   J. Biol. Chem. 272:23565-23571(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CAR1).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
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].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=10462436; DOI=10.1006/abbi.1999.1351;
RA   Waxman D.J.;
RT   "P450 gene induction by structurally diverse xenochemicals: central role of
RT   nuclear receptors CAR, PXR, and PPAR.";
RL   Arch. Biochem. Biophys. 369:11-23(1999).
RN   [5]
RP   INTERACTION WITH PSMC4.
RX   PubMed=8603043; DOI=10.1016/0960-0760(95)00220-0;
RA   Choi H.S., Seol W., Moore D.D.;
RT   "A component of the 26S proteasome binds on orphan member of the nuclear
RT   hormone receptor superfamily.";
RL   J. Steroid Biochem. Mol. Biol. 56:23-30(1996).
RN   [6]
RP   INTERACTION WITH DNAJC7 AND HSP90, AND SUBCELLULAR LOCATION.
RX   PubMed=14573755; DOI=10.1124/mol.64.5.1069;
RA   Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.;
RT   "Cytoplasmic accumulation of the nuclear receptor CAR by a
RT   tetratricopeptide repeat protein in HepG2 cells.";
RL   Mol. Pharmacol. 64:1069-1075(2003).
RN   [7]
RP   INTERACTION WITH ECT2, AND SUBCELLULAR LOCATION.
RX   PubMed=17904126; DOI=10.1016/j.febslet.2007.09.024;
RA   Hosseinpour F., Timsit Y., Koike C., Matsui K., Yamamoto Y., Moore R.,
RA   Negishi M.;
RT   "Overexpression of the Rho-guanine nucleotide exchange factor ECT2 inhibits
RT   nuclear translocation of nuclear receptor CAR in the mouse liver.";
RL   FEBS Lett. 581:4937-4942(2007).
RN   [8]
RP   INTERACTION WITH CRY1 AND CRY2.
RX   PubMed=28751364; DOI=10.1073/pnas.1704955114;
RA   Kriebs A., Jordan S.D., Soto E., Henriksson E., Sandate C.R., Vaughan M.E.,
RA   Chan A.B., Duglan D., Papp S.J., Huber A.L., Afetian M.E., Yu R.T.,
RA   Zhao X., Downes M., Evans R.M., Lamia K.A.;
RT   "Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors
RT   and modulate transcriptional activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:8776-8781(2017).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 227-458 IN COMPLEX WITH H.SAPIENS
RP   RXRA; R.NORVEGICUS NCOA2 AND AGONIST INSECTICIDE CONTAMINANT TCPOBOP, AND
RP   MUTAGENESIS OF PHE-171; ASN-175; LEU-216; PHE-227; TYR-234; PHE-244;
RP   TYR-336 AND LEU-346.
RX   PubMed=15610733; DOI=10.1016/j.molcel.2004.11.036;
RA   Suino K., Peng L., Reynolds R., Li Y., Cha J.Y., Repa J.J., Kliewer S.A.,
RA   Xu H.E.;
RT   "The nuclear xenobiotic receptor CAR: structural determinants of
RT   constitutive activation and heterodimerization.";
RL   Mol. Cell 16:893-905(2004).
CC   -!- FUNCTION: Binds and transactivates the retinoic acid response elements
CC       that control expression of the retinoic acid receptor beta 2 and
CC       alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital
CC       responsive element module of the human CYP2B6 gene and the CYP3A4
CC       xenobiotic response element (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:10462436}.
CC   -!- SUBUNIT: Heterodimer of NR1I3 and RXR. Interacts with PSMC4. Interacts
CC       with ECT2. Directly interacts with DNAJC7; this complex may also
CC       include HSP90. Interacts with CRY1 (PubMed:28751364). Interacts with
CC       CRY2 in a ligand-dependent manner (PubMed:28751364).
CC       {ECO:0000269|PubMed:14573755, ECO:0000269|PubMed:15610733,
CC       ECO:0000269|PubMed:17904126, ECO:0000269|PubMed:28751364,
CC       ECO:0000269|PubMed:8603043}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Note=Recruited to the cytoplasm by DNAJC7.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=CAR1;
CC         IsoId=O35627-1; Sequence=Displayed;
CC       Name=CAR2;
CC         IsoId=O35627-2; Sequence=VSP_003671, VSP_003672;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in liver.
CC   -!- DOMAIN: Composed by a short N-terminal domain followed by the DNA
CC       binding, hinge, and ligand binding/dimerization domains.
CC   -!- PTM: Phosphorylated at Thr-48 by PKC, dephosphorylation of Thr-48 is
CC       required for nuclear translocation and activation. {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform CAR2]: Does not seem to act as a
CC       transactivator. Lacks the C-terminal portion of the ligand
CC       binding/dimerization domain. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF009327; AAC53349.1; -; mRNA.
DR   EMBL; AF009328; AAC53350.1; -; mRNA.
DR   EMBL; AK133515; BAE21697.1; -; mRNA.
DR   EMBL; CH466520; EDL39126.1; -; Genomic_DNA.
DR   CCDS; CCDS15480.1; -. [O35627-1]
DR   CCDS; CCDS56654.1; -. [O35627-2]
DR   RefSeq; NP_001229991.1; NM_001243062.1. [O35627-2]
DR   RefSeq; NP_001229992.1; NM_001243063.1.
DR   RefSeq; NP_033933.2; NM_009803.5. [O35627-1]
DR   PDB; 1XLS; X-ray; 2.96 A; E/F/G/H=117-358.
DR   PDB; 1XNX; X-ray; 2.90 A; A/B=109-358.
DR   PDBsum; 1XLS; -.
DR   PDBsum; 1XNX; -.
DR   AlphaFoldDB; O35627; -.
DR   SMR; O35627; -.
DR   BioGRID; 198489; 13.
DR   IntAct; O35627; 1.
DR   STRING; 10090.ENSMUSP00000005820; -.
DR   BindingDB; O35627; -.
DR   ChEMBL; CHEMBL3069; -.
DR   DrugCentral; O35627; -.
DR   GuidetoPHARMACOLOGY; 607; -.
DR   iPTMnet; O35627; -.
DR   PhosphoSitePlus; O35627; -.
DR   PaxDb; 10090-ENSMUSP00000005820; -.
DR   ProteomicsDB; 295523; -. [O35627-1]
DR   ProteomicsDB; 295524; -. [O35627-2]
DR   Antibodypedia; 20508; 531 antibodies from 32 providers.
DR   DNASU; 12355; -.
DR   Ensembl; ENSMUST00000005820.11; ENSMUSP00000005820.5; ENSMUSG00000005677.15. [O35627-1]
DR   Ensembl; ENSMUST00000075469.12; ENSMUSP00000074915.6; ENSMUSG00000005677.15. [O35627-2]
DR   GeneID; 12355; -.
DR   KEGG; mmu:12355; -.
DR   UCSC; uc007dnf.2; mouse. [O35627-1]
DR   UCSC; uc007dng.2; mouse. [O35627-2]
DR   AGR; MGI:1346307; -.
DR   CTD; 9970; -.
DR   MGI; MGI:1346307; Nr1i3.
DR   VEuPathDB; HostDB:ENSMUSG00000005677; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000160641; -.
DR   HOGENOM; CLU_007368_12_0_1; -.
DR   InParanoid; O35627; -.
DR   OMA; VHAGFQE; -.
DR   OrthoDB; 5359733at2759; -.
DR   PhylomeDB; O35627; -.
DR   TreeFam; TF316304; -.
DR   Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR   BioGRID-ORCS; 12355; 3 hits in 81 CRISPR screens.
DR   ChiTaRS; Nr1i3; mouse.
DR   EvolutionaryTrace; O35627; -.
DR   PRO; PR:O35627; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; O35627; Protein.
DR   Bgee; ENSMUSG00000005677; Expressed in left lobe of liver and 61 other cell types or tissues.
DR   ExpressionAtlas; O35627; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0004879; F:nuclear receptor activity; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR   CDD; cd07156; NR_DBD_VDR_like; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   IDEAL; IID50248; -.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR001728; ThyrH_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24082:SF231; NUCLEAR RECEPTOR SUBFAMILY 1 GROUP I MEMBER 3; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   PRINTS; PR00546; THYROIDHORMR.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   Genevisible; O35627; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Receptor;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..358
FT                   /note="Nuclear receptor subfamily 1 group I member 3"
FT                   /id="PRO_0000053554"
FT   DOMAIN          119..358
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        18..93
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         21..41
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         57..81
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   SITE            171
FT                   /note="Important for TCPOBOP recognition"
FT   SITE            175
FT                   /note="Important for TCPOBOP recognition"
FT   SITE            216
FT                   /note="Important for TCPOBOP recognition"
FT   SITE            227
FT                   /note="Important for TCPOBOP recognition"
FT   SITE            244
FT                   /note="Important for TCPOBOP recognition"
FT   SITE            336
FT                   /note="Important for TCPOBOP recognition"
FT   MOD_RES         48
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:Q14994"
FT   VAR_SEQ         281..286
FT                   /note="DRPGVT -> GFCMQS (in isoform CAR2)"
FT                   /evidence="ECO:0000303|PubMed:9295294"
FT                   /id="VSP_003671"
FT   VAR_SEQ         287..358
FT                   /note="Missing (in isoform CAR2)"
FT                   /evidence="ECO:0000303|PubMed:9295294"
FT                   /id="VSP_003672"
FT   MUTAGEN         171
FT                   /note="F->W: Diminished binding of coactivator NCOA2 in the
FT                   presence of TCPOBOP."
FT                   /evidence="ECO:0000269|PubMed:15610733"
FT   MUTAGEN         175
FT                   /note="N->F: Diminished binding of coactivator NCOA2 in the
FT                   presence of TCPOBOP."
FT                   /evidence="ECO:0000269|PubMed:15610733"
FT   MUTAGEN         216
FT                   /note="L->F: Diminished binding of coactivator NCOA2 in the
FT                   presence of TCPOBOP."
FT                   /evidence="ECO:0000269|PubMed:15610733"
FT   MUTAGEN         227
FT                   /note="F->W: Diminished binding of coactivator NCOA2 in the
FT                   presence of TCPOBOP."
FT                   /evidence="ECO:0000269|PubMed:15610733"
FT   MUTAGEN         234
FT                   /note="Y->A: No effect on binding of coactivator NCOA2 in
FT                   the presence of TCPOBOP."
FT                   /evidence="ECO:0000269|PubMed:15610733"
FT   MUTAGEN         244
FT                   /note="F->A: Diminished binding of coactivator NCOA2 in the
FT                   presence of TCPOBOP."
FT                   /evidence="ECO:0000269|PubMed:15610733"
FT   MUTAGEN         336
FT                   /note="Y->A: Diminished binding of coactivator NCOA2 in the
FT                   presence of TCPOBOP."
FT                   /evidence="ECO:0000269|PubMed:15610733"
FT   MUTAGEN         346
FT                   /note="L->F: Dramatic increase in binding NCOA2. Little
FT                   effect on binding of coactivator NCOA2 in the presence of
FT                   TCPOBOP."
FT                   /evidence="ECO:0000269|PubMed:15610733"
FT   CONFLICT        138
FT                   /note="M -> L (in Ref. 1; AAC53349/AAC53350)"
FT                   /evidence="ECO:0000305"
FT   HELIX           118..134
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           138..144
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:1XLS"
FT   HELIX           164..187
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           190..193
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           197..216
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           217..219
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   TURN            222..225
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   STRAND          226..229
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           236..241
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           246..260
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           266..277
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           288..308
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   TURN            309..312
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           318..335
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           337..343
FT                   /evidence="ECO:0007829|PDB:1XNX"
FT   HELIX           345..349
FT                   /evidence="ECO:0007829|PDB:1XLS"
FT   HELIX           351..357
FT                   /evidence="ECO:0007829|PDB:1XLS"
SQ   SEQUENCE   358 AA;  40913 MW;  A11C92B1EC2C06A7 CRC64;
     MTAMLTLETM ASEEEYGPRN CVVCGDRATG YHFHALTCEG CKGFFRRTVS KTIGPICPFA
     GRCEVSKAQR RHCPACRLQK CLNVGMRKDM ILSAEALALR RARQAQRRAE KASLQLNQQQ
     KELVQILLGA HTRHVGPMFD QFVQFKPPAY LFMHHRPFQP RGPVLPLLTH FADINTFMVQ
     QIIKFTKDLP LFRSLTMEDQ ISLLKGAAVE ILHISLNTTF CLQTENFFCG PLCYKMEDAV
     HAGFQYEFLE SILHFHKNLK GLHLQEPEYV LMAATALFSP DRPGVTQREE IDQLQEEMAL
     ILNNHIMEQQ SRLQSRFLYA KLMGLLADLR SINNAYSYEL QRLEELSAMT PLLGEICS
//