ID   DME_ARATH               Reviewed;        1987 AA.
AC   Q8LK56; Q1WEY5; Q84TL4; Q9LZ67; Q9LZ68; Q9LZ69;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Transcriptional activator DEMETER;
DE            EC=3.2.2.-;
DE   AltName: Full=DNA glycosylase-related protein DME;
GN   Name=DME; OrderedLocusNames=At5g04560/At5g04570/At5g04580;
GN   ORFNames=T32M21.160/T32M21.170/T32M21.180;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CHARACTERIZATION.
RC   STRAIN=cv. Columbia; TISSUE=Flower;
RX   PubMed=12150995; DOI=10.1016/s0092-8674(02)00807-3;
RA   Choi Y., Gehring M., Johnson L., Hannon M., Harada J.J., Goldberg R.B.,
RA   Jacobsen S.E., Fischer R.L.;
RT   "DEMETER, a DNA glycosylase domain protein, is required for endosperm gene
RT   imprinting and seed viability in Arabidopsis.";
RL   Cell 110:33-42(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND FUNCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=16624880; DOI=10.1073/pnas.0601109103;
RA   Morales-Ruiz T., Ortega-Galisteo A.P., Ponferrada-Marin M.I.,
RA   Martinez-Macias M.I., Ariza R.R., Roldan-Arjona T.;
RT   "DEMETER and REPRESSOR OF SILENCING 1 encode 5-methylcytosine DNA
RT   glycosylases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6853-6858(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF ASP-1562.
RX   PubMed=15128940; DOI=10.1073/pnas.0402328101;
RA   Choi Y., Harada J.J., Goldberg R.B., Fischer R.L.;
RT   "An invariant aspartic acid in the DNA glycosylase domain of DEMETER is
RT   necessary for transcriptional activation of the imprinted MEDEA gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7481-7486(2004).
CC   -!- FUNCTION: Transcriptional activator involved in gene imprinting.
CC       Catalyzes the release of 5-methylcytosine (5-meC) from DNA by a
CC       glycosylase/lyase mechanism. Allows the expression of the maternal copy
CC       of the imprinted MEA gene before fertilization, possibly by
CC       antagonizing or suppressing DNA methylation on target promoter.
CC       Probably acts by nicking the MEA promoter. Required for stable
CC       reproducible patterns of floral and vegetative development.
CC       {ECO:0000269|PubMed:12150995, ECO:0000269|PubMed:15128940,
CC       ECO:0000269|PubMed:16624880}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a
CC       role in catalysis, but is probably involved in the proper positioning
CC       of the enzyme along the DNA strand. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q8LK56-3; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q8LK56-1; Sequence=VSP_019283;
CC       Name=2;
CC         IsoId=Q8LK56-2; Sequence=VSP_007455;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in immature flower buds, then
CC       decreases as the flower matures. Expressed in the ovule carpels, but
CC       not expressed in pollen stamens. Expressed in developing and mature
CC       ovules (stages 12-14), then strongly decreases after fertilization.
CC   -!- DEVELOPMENTAL STAGE: Maternally expressed. Expressed primarily in the
CC       central cell of gametophyte before fertilization. Not expressed in
CC       endosperm and embryo after fertilization.
CC   -!- DOMAIN: The DEMETER domain, which is present in proteins of the
CC       subfamily, is related to the J-domain, but lacks some important
CC       conserved residues.
CC   -!- MISCELLANEOUS: Although strongly related to DNA glycosylase proteins,
CC       it differs from these proteins because of its large size and its unique
CC       N-terminal basic domain. The DNA repair function has not been proved
CC       and may not exist.
CC   -!- SIMILARITY: Belongs to the DNA glycosylase family. DEMETER subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB85562.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to three different genes At5g04560, At5g04570 and At5g04580.; Evidence={ECO:0000305};
CC       Sequence=CAB85563.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to three different genes At5g04560, At5g04570 and At5g04580.; Evidence={ECO:0000305};
CC       Sequence=CAB85564.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to three different genes At5g04560, At5g04570 and At5g04580.; Evidence={ECO:0000305};
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DR   EMBL; AF521596; AAM77215.1; -; mRNA.
DR   EMBL; DQ335243; ABC61677.1; -; mRNA.
DR   EMBL; AL162875; CAB85562.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL162875; CAB85563.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL162875; CAB85564.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90760.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90761.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69949.1; -; Genomic_DNA.
DR   EMBL; AK117994; BAC42629.1; -; mRNA.
DR   EMBL; BT005357; AAO63421.1; -; mRNA.
DR   PIR; T48452; T48452.
DR   PIR; T48453; T48453.
DR   PIR; T48454; T48454.
DR   RefSeq; NP_001078527.1; NM_001085058.2. [Q8LK56-3]
DR   RefSeq; NP_001331593.1; NM_001342781.1. [Q8LK56-1]
DR   RefSeq; NP_196076.2; NM_120538.2. [Q8LK56-1]
DR   AlphaFoldDB; Q8LK56; -.
DR   SMR; Q8LK56; -.
DR   BioGRID; 15614; 7.
DR   STRING; 3702.Q8LK56; -.
DR   PaxDb; 3702-AT5G04560-2; -.
DR   ProteomicsDB; 222002; -. [Q8LK56-3]
DR   EnsemblPlants; AT5G04560.1; AT5G04560.1; AT5G04560. [Q8LK56-1]
DR   EnsemblPlants; AT5G04560.2; AT5G04560.2; AT5G04560. [Q8LK56-3]
DR   EnsemblPlants; AT5G04560.3; AT5G04560.3; AT5G04560. [Q8LK56-1]
DR   GeneID; 830335; -.
DR   Gramene; AT5G04560.1; AT5G04560.1; AT5G04560. [Q8LK56-1]
DR   Gramene; AT5G04560.2; AT5G04560.2; AT5G04560. [Q8LK56-3]
DR   Gramene; AT5G04560.3; AT5G04560.3; AT5G04560. [Q8LK56-1]
DR   KEGG; ath:AT5G04560; -.
DR   Araport; AT5G04560; -.
DR   TAIR; AT5G04560; DME.
DR   eggNOG; ENOG502QQKH; Eukaryota.
DR   InParanoid; Q8LK56; -.
DR   OMA; MYLMGTQ; -.
DR   OrthoDB; 1216739at2759; -.
DR   PhylomeDB; Q8LK56; -.
DR   PRO; PR:Q8LK56; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8LK56; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISS:TAIR.
DR   GO; GO:0043078; C:polar nucleus; IDA:TAIR.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0035514; F:DNA demethylase activity; IEA:InterPro.
DR   GO; GO:0019104; F:DNA N-glycosylase activity; IDA:TAIR.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032183; F:SUMO binding; IPI:TAIR.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0080111; P:DNA demethylation; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IDA:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR   InterPro; IPR044811; DME/ROS1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR028924; Perm-CXXC.
DR   InterPro; IPR028925; RRM_DME.
DR   PANTHER; PTHR46213; TRANSCRIPTIONAL ACTIVATOR DEMETER; 1.
DR   PANTHER; PTHR46213:SF31; TRANSCRIPTIONAL ACTIVATOR DEMETER; 1.
DR   Pfam; PF15629; Perm-CXXC; 1.
DR   Pfam; PF15628; RRM_DME; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   Genevisible; Q8LK56; AT.
PE   1: Evidence at protein level;
KW   4Fe-4S; Activator; Alternative splicing; DNA-binding; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1987
FT                   /note="Transcriptional activator DEMETER"
FT                   /id="PRO_0000102245"
FT   REGION          246..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1054
FT                   /note="DEMETER"
FT   REGION          1324..1351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1439..1471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..843
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1326..1341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1448..1471
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1629
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         1636
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         1639
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         1645
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..258
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:12150995"
FT                   /id="VSP_019283"
FT   VAR_SEQ         259..1571
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11910074,
FT                   ECO:0000303|PubMed:14593172"
FT                   /id="VSP_007455"
FT   MUTAGEN         1562
FT                   /note="D->N: Loss of activity and abnormal MEA imprinting."
FT                   /evidence="ECO:0000269|PubMed:15128940"
FT   CONFLICT        1679
FT                   /note="Y -> F (in Ref. 1; AAM77215)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1987 AA;  221147 MW;  4035C0D344DCF375 CRC64;
     MNSRADPGDR YFRVPLENQT QQEFMGSWIP FTPKKPRSSL MVDERVINQD LNGFPGGEFV
     DRGFCNTGVD HNGVFDHGAH QGVTNLSMMI NSLAGSHAQA WSNSERDLLG RSEVTSPLAP
     VIRNTTGNVE PVNGNFTSDV GMVNGPFTQS GTSQAGYNEF ELDDLLNPDQ MPFSFTSLLS
     GGDSLFKVRQ YGPPACNKPL YNLNSPIRRE AVGSVCESSF QYVPSTPSLF RTGEKTGFLE
     QIVTTTGHEI PEPKSDKSMQ SIMDSSAVNA TEATEQNDGS RQDVLEFDLN KTPQQKPSKR
     KRKFMPKVVV EGKPKRKPRK PAELPKVVVE GKPKRKPRKA ATQEKVKSKE TGSAKKKNLK
     ESATKKPANV GDMSNKSPEV TLKSCRKALN FDLENPGDAR QGDSESEIVQ NSSGANSFSE
     IRDAIGGTNG SFLDSVSQID KTNGLGAMNQ PLEVSMGNQP DKLSTGAKLA RDQQPDLLTR
     NQQCQFPVAT QNTQFPMENQ QAWLQMKNQL IGFPFGNQQP RMTIRNQQPC LAMGNQQPMY
     LIGTPRPALV SGNQQLGGPQ GNKRPIFLNH QTCLPAGNQL YGSPTDMHQL VMSTGGQQHG
     LLIKNQQPGS LIRGQQPCVP LIDQQPATPK GFTHLNQMVA TSMSSPGLRP HSQSQVPTTY
     LHVESVSRIL NGTTGTCQRS RAPAYDSLQQ DIHQGNKYIL SHEISNGNGC KKALPQNSSL
     PTPIMAKLEE ARGSKRQYHR AMGQTEKHDL NLAQQIAQSQ DVERHNSSTC VEYLDAAKKT
     KIQKVVQENL HGMPPEVIEI EDDPTDGARK GKNTASISKG ASKGNSSPVK KTAEKEKCIV
     PKTPAKKGRA GRKKSVPPPA HASEIQLWQP TPPKTPLSRS KPKGKGRKSI QDSGKARGPS
     GELLCQDSIA EIIYRMQNLY LGDKEREQEQ NAMVLYKGDG ALVPYESKKR KPRPKVDIDD
     ETTRIWNLLM GKGDEKEGDE EKDKKKEKWW EEERRVFRGR ADSFIARMHL VQGDRRFSPW
     KGSVVDSVIG VFLTQNVSDH LSSSAFMSLA ARFPPKLSSS REDERNVRSV VVEDPEGCIL
     NLNEIPSWQE KVQHPSDMEV SGVDSGSKEQ LRDCSNSGIE RFNFLEKSIQ NLEEEVLSSQ
     DSFDPAIFQS CGRVGSCSCS KSDAEFPTTR CETKTVSGTS QSVQTGSPNL SDEICLQGNE
     RPHLYEGSGD VQKQETTNVA QKKPDLEKTM NWKDSVCFGQ PRNDTNWQTT PSSSYEQCAT
     RQPHVLDIED FGMQGEGLGY SWMSISPRVD RVKNKNVPRR FFRQGGSVPR EFTGQIIPST
     PHELPGMGLS GSSSAVQEHQ DDTQHNQQDE MNKASHLQKT FLDLLNSSEE CLTRQSSTKQ
     NITDGCLPRD RTAEDVVDPL SNNSSLQNIL VESNSSNKEQ TAVEYKETNA TILREMKGTL
     ADGKKPTSQW DSLRKDVEGN EGRQERNKNN MDSIDYEAIR RASISEISEA IKERGMNNML
     AVRIKDFLER IVKDHGGIDL EWLRESPPDK AKDYLLSIRG LGLKSVECVR LLTLHNLAFP
     VDTNVGRIAV RMGWVPLQPL PESLQLHLLE LYPVLESIQK FLWPRLCKLD QRTLYELHYQ
     LITFGKVFCT KSRPNCNACP MRGECRHFAS AYASARLALP APEERSLTSA TIPVPPESYP
     PVAIPMIELP LPLEKSLASG APSNRENCEP IIEEPASPGQ ECTEITESDI EDAYYNEDPD
     EIPTIKLNIE QFGMTLREHM ERNMELQEGD MSKALVALHP TTTSIPTPKL KNISRLRTEH
     QVYELPDSHR LLDGMDKREP DDPSPYLLAI WTPGETANSA QPPEQKCGGK ASGKMCFDET
     CSECNSLREA NSQTVRGTLL IPCRTAMRGS FPLNGTYFQV NELFADHESS LKPIDVPRDW
     IWDLPRRTVY FGTSVTSIFR GLSTEQIQFC FWKGFVCVRG FEQKTRAPRP LMARLHFPAS
     KLKNNKT
//