TRXR3_MOUSE
ID TRXR3_MOUSE Reviewed; 652 AA.
AC Q99MD6; Q9CZE5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Thioredoxin reductase 3;
DE EC=1.8.1.9;
DE AltName: Full=Thioredoxin and glutathione reductase;
DE AltName: Full=Thioredoxin reductase TR2;
GN Name=Txnrd3 {ECO:0000312|MGI:MGI:2386711};
GN Synonyms=Tgr {ECO:0000312|EMBL:AAK31172.1}, Trxr3;
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] {ECO:0000305, ECO:0000312|EMBL:AAK31172.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, DOMAIN, 3D-STRUCTURE MODELING, AND SELENOCYSTEINE AT
RP SEC-651.
RX PubMed=11259642; DOI=10.1073/pnas.051454398;
RA Sun Q.-A., Kirnarsky L., Sherman S., Gladyshev V.N.;
RT "Selenoprotein oxidoreductase with specificity for thioredoxin and
RT glutathione systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3673-3678(2001).
RN [2] {ECO:0000312|EMBL:BAB28419.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB28419.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB28419.1}, and
RC Thymus {ECO:0000312|EMBL:BAC37890.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAH76605.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH76605.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH76605.1};
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 191-202 AND 550-561, AND TISSUE SPECIFICITY.
RX PubMed=10455115; DOI=10.1074/jbc.274.35.24522;
RA Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Redox regulation of cell signaling by selenocysteine in mammalian
RT thioredoxin reductases.";
RL J. Biol. Chem. 274:24522-24530(1999).
RN [5] {ECO:0000305}
RP DOMAIN, AND MUTAGENESIS OF SEC-651 AND 651-SEC-GLY-652.
RX PubMed=16262253; DOI=10.1021/bi051321w;
RA Sun Q.-A., Su D., Novoselov S.V., Carlson B.A., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Reaction mechanism and regulation of mammalian thioredoxin/glutathione
RT reductase.";
RL Biochemistry 44:14528-14537(2005).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15901730; DOI=10.1074/jbc.m503638200;
RA Su D., Novoselov S.V., Sun Q.-A., Moustafa M.E., Zhou Y., Oko R.,
RA Hatfield D.L., Gladyshev V.N.;
RT "Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in
RT disulfide bond formation and sperm maturation.";
RL J. Biol. Chem. 280:26491-26498(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP NON-AUG INITIATOR START CODON, AND TISSUE SPECIFICITY.
RX PubMed=20018845; DOI=10.1074/jbc.m109.070532;
RA Gerashchenko M.V., Su D., Gladyshev V.N.;
RT "CUG start codon generates thioredoxin/glutathione reductase isoforms in
RT mouse testes.";
RL J. Biol. Chem. 285:4595-4602(2010).
RN [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-388, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-34, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Displays thioredoxin reductase, glutaredoxin and glutathione
CC reductase activities. Catalyzes disulfide bond isomerization. Promotes
CC disulfide bond formation between GPX4 and various sperm proteins and
CC may play a role in sperm maturation by promoting formation of sperm
CC structural components. {ECO:0000269|PubMed:11259642,
CC ECO:0000269|PubMed:15901730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000269|PubMed:11259642};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O89049};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O89049};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.7 uM for 5,5'-dithiobis(2-nitrobenzoic acid)
CC {ECO:0000269|PubMed:11259642};
CC KM=10.7 uM for NADPH {ECO:0000269|PubMed:11259642};
CC KM=3.0 uM for thioredoxin {ECO:0000269|PubMed:11259642};
CC KM=8.84 uM for oxidized glutathione {ECO:0000269|PubMed:11259642};
CC KM=45.2 uM for beta-hydroxyethyl disulfide
CC {ECO:0000269|PubMed:11259642};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O89049}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11259642,
CC ECO:0000269|PubMed:15901730}. Nucleus {ECO:0000269|PubMed:11259642,
CC ECO:0000269|PubMed:15901730}. Microsome {ECO:0000269|PubMed:11259642,
CC ECO:0000269|PubMed:15901730}. Endoplasmic reticulum. Note=Detected in
CC cytoplasm and nucleus in late spermatids. {ECO:0000269|PubMed:11259642,
CC ECO:0000269|PubMed:15901730}.
CC -!- TISSUE SPECIFICITY: Expressed preferentially in testis where it is
CC found in spermatids and spermatocytes but not in sperm. In elongating
CC spermatids, expressed at the site of mitochondrial sheath formation.
CC Low levels in other tissues including heart, lung, liver, kidney,
CC brain, muscle and prostate. {ECO:0000269|PubMed:10455115,
CC ECO:0000269|PubMed:15901730, ECO:0000269|PubMed:20018845}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in the testis after puberty. Not
CC detected in 20-day-old mice but highly expressed in testes of 7-month-
CC old mice. {ECO:0000269|PubMed:15901730}.
CC -!- DOMAIN: The N-terminal glutaredoxin domain does not contain the C-X-X-C
CC redox-active motif normally found in glutaredoxins but activity may be
CC mediated through a single cysteine. The C-terminal Cys-Sec motif of one
CC subunit of the homodimer may transfer electrons from the thiol-
CC disulfide center to the glutaredoxin domain of the other subunit.
CC {ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:16262253}.
CC -!- MISCELLANEOUS: The thioredoxin reductase active site is a redox-active
CC disulfide bond. The selenocysteine residue is also essential for
CC catalytic activity (By similarity). {ECO:0000250|UniProtKB:Q16881}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- CAUTION: This sequence initiates at a CTG codon.
CC {ECO:0000305|PubMed:20018845}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH76605.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH76605.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=AAK31172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB28419.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB28419.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB28419.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=BAC37890.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC37890.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR EMBL; AF349659; AAK31172.1; ALT_INIT; mRNA.
DR EMBL; AK012699; BAB28419.1; ALT_SEQ; mRNA.
DR EMBL; AK080362; BAC37890.1; ALT_SEQ; mRNA.
DR EMBL; BC076605; AAH76605.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001171529.1; NM_001178058.1.
DR RefSeq; NP_694802.2; NM_153162.3.
DR PDB; 2LV3; NMR; -; A=44-161.
DR PDBsum; 2LV3; -.
DR BMRB; Q99MD6; -.
DR SMR; Q99MD6; -.
DR STRING; 10090.ENSMUSP00000000828; -.
DR iPTMnet; Q99MD6; -.
DR PhosphoSitePlus; Q99MD6; -.
DR jPOST; Q99MD6; -.
DR MaxQB; Q99MD6; -.
DR PaxDb; Q99MD6; -.
DR PeptideAtlas; Q99MD6; -.
DR PRIDE; Q99MD6; -.
DR ProteomicsDB; 297530; -.
DR DNASU; 232223; -.
DR GeneID; 232223; -.
DR KEGG; mmu:232223; -.
DR UCSC; uc009cwj.1; mouse.
DR CTD; 114112; -.
DR MGI; MGI:2386711; Txnrd3.
DR eggNOG; KOG1752; Eukaryota.
DR eggNOG; KOG4716; Eukaryota.
DR InParanoid; Q99MD6; -.
DR OrthoDB; 581771at2759; -.
DR BRENDA; 1.8.1.B1; 3474.
DR SABIO-RK; Q99MD6; -.
DR BioGRID-ORCS; 232223; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q99MD6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99MD6; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR TIGRFAMs; TIGR01438; TGR; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Electron transport;
KW Endoplasmic reticulum; FAD; Flavoprotein; Methylation; Microsome; NADP;
KW Nucleus; Oxidoreductase; Phosphoprotein; Redox-active center;
KW Reference proteome; Selenocysteine; Spermatogenesis; Transport.
FT CHAIN 1..652
FT /note="Thioredoxin reductase 3"
FT /id="PRO_0000320696"
FT DOMAIN 65..165
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 625
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 167..196
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT NON_STD 651
FT /note="Selenocysteine"
FT MOD_RES 34
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 34
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VQ6"
FT MOD_RES 388
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT DISULFID 212..217
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 650..651
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000250"
FT MUTAGEN 651..652
FT /note="Missing: Abolishes thioredoxin reductase,
FT glutaredoxin and gluthioine reductase activities."
FT /evidence="ECO:0000269|PubMed:16262253"
FT MUTAGEN 651
FT /note="U->C: Thioredoxin reductase activity reduced to 21%.
FT Glutaredoxin activity reduced to 14%. Glutathione reductase
FT activity reduced to 18%."
FT /evidence="ECO:0000269|PubMed:16262253"
FT MUTAGEN 651
FT /note="U->S: Abolishes thioredoxin reductase, glutaredoxin
FT and gluthioine reductase activities."
FT /evidence="ECO:0000269|PubMed:16262253"
FT CONFLICT 8
FT /note="P -> R (in Ref. 2; BAB28419)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="S -> W (in Ref. 2; BAB28419)"
FT /evidence="ECO:0000305"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:2LV3"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:2LV3"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:2LV3"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2LV3"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2LV3"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:2LV3"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:2LV3"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2LV3"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2LV3"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:2LV3"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:2LV3"
SQ SEQUENCE 652 AA; 71319 MW; AC6342C64DDEC1BC CRC64;
MEKPPSPPPP PRAQTSPGLG KVGVLPNRRL GAVRGGLMSS PPGRRARLAS PGTSRPSSEA
REELRRRLRD LIEGNRVMIF SKSYCPHSTR VKELFSSLGV VYNILELDQV DDGASVQEVL
TEISNQKTVP NIFVNKVHVG GCDRTFQAHQ NGLLQKLLQD DSAHDYDLII IGGGSGGLSC
AKEAANLGKK VMVLDFVVPS PQGTTWGLGG TCVNVGCIPK KLMHQAALLG HALQDAKKYG
WEYNQQVKHN WEAMTEAIQS HIGSLNWGYR VTLREKGVTY VNSFGEFVDL HKIKATNKKG
QETFYTASKF VIATGERPRY LGIQGDKEYC ITSDDLFSLP YCPGCTLVVG ASYVGLECAG
FLAGLGLDVT VMVRSVLLRG FDQEMAEKVG SYLEQQGVKF QRKFTPILVQ QLEKGLPGKL
KVVAKSTEGP ETVEGIYNTV LLAIGRDSCT RKIGLEKIGV KINEKNGKIP VNDVEQTNVP
HVYAIGDILD GKPELTPVAI QAGKLLARRL FGVSLEKCDY INIPTTVFTP LEYGCCGLSE
EKAIEMYKKE NLEVYHTLFW PLEWTVAGRD NNTCYAKIIC NKFDNERVVG FHLLGPNAGE
ITQGFAAAMK CGLTKQLLDD TIGIHPTCGE VFTTLEITKS SGLDITQKGC UG
