JHD2C_MOUSE
ID JHD2C_MOUSE Reviewed; 2350 AA.
AC Q69ZK6; E9QMM8; Q6NV48; Q8BUF5; Q8C4I5; Q8C5Q9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable JmjC domain-containing histone demethylation protein 2C;
DE EC=1.14.11.-;
DE AltName: Full=Jumonji domain-containing protein 1C;
GN Name=Jmjd1c; Synonyms=Jhdm2c, Kiaa1380;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-141; 1112-1832 AND 1967-2350.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 968-2350.
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
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 [5]
RP PROTEIN SEQUENCE OF 1032-1054, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-138; SER-294 AND
RP SER-471, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, 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).
CC -!- FUNCTION: Probable histone demethylase that specifically demethylates
CC 'Lys-9' of histone H3, thereby playing a central role in histone code.
CC Demethylation of Lys residue generates formaldehyde and succinate. May
CC be involved in hormone-dependent transcriptional activation, by
CC participating in recruitment to androgen-receptor target genes (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68318.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH68318.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAC36783.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC38410.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32440.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK173162; BAD32440.1; ALT_INIT; mRNA.
DR EMBL; AC155712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK077400; BAC36783.1; ALT_SEQ; mRNA.
DR EMBL; AK082106; BAC38410.1; ALT_INIT; mRNA.
DR EMBL; AK085500; BAC39458.1; -; mRNA.
DR EMBL; BC068318; AAH68318.1; ALT_SEQ; mRNA.
DR CCDS; CCDS56708.1; -.
DR RefSeq; NP_001229325.1; NM_001242396.1.
DR RefSeq; XP_006513104.1; XM_006513041.2.
DR RefSeq; XP_006513105.1; XM_006513042.3.
DR AlphaFoldDB; Q69ZK6; -.
DR SMR; Q69ZK6; -.
DR BioGRID; 224438; 7.
DR IntAct; Q69ZK6; 1.
DR STRING; 10090.ENSMUSP00000133700; -.
DR iPTMnet; Q69ZK6; -.
DR PhosphoSitePlus; Q69ZK6; -.
DR EPD; Q69ZK6; -.
DR jPOST; Q69ZK6; -.
DR MaxQB; Q69ZK6; -.
DR PaxDb; Q69ZK6; -.
DR PRIDE; Q69ZK6; -.
DR ProteomicsDB; 269420; -.
DR Antibodypedia; 28318; 143 antibodies from 27 providers.
DR Ensembl; ENSMUST00000173689; ENSMUSP00000133700; ENSMUSG00000037876.
DR GeneID; 108829; -.
DR KEGG; mmu:108829; -.
DR UCSC; uc007fls.2; mouse.
DR CTD; 221037; -.
DR MGI; MGI:1918614; Jmjd1c.
DR VEuPathDB; HostDB:ENSMUSG00000037876; -.
DR eggNOG; KOG1356; Eukaryota.
DR GeneTree; ENSGT00940000158210; -.
DR InParanoid; Q69ZK6; -.
DR TreeFam; TF324723; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 108829; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Jmjd1c; mouse.
DR PRO; PR:Q69ZK6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q69ZK6; protein.
DR Bgee; ENSMUSG00000037876; Expressed in uterus and 73 other tissues.
DR ExpressionAtlas; Q69ZK6; baseline and differential.
DR Genevisible; Q69ZK6; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
DR GO; GO:0098727; P:maintenance of cell number; IMP:MGI.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Direct protein sequencing; Iron;
KW Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2350
FT /note="Probable JmjC domain-containing histone
FT demethylation protein 2C"
FT /id="PRO_0000234375"
FT DOMAIN 2084..2308
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 1657..1682
FT /note="C6-type"
FT /evidence="ECO:0000255"
FT REGION 96..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1933..1962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1876..1880
FT /note="LXXLL motif"
FT COMPBIAS 96..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1941..1955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2146
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 2148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 2276
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT MOD_RES 1800
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT CROSSLNK 1942
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15652"
FT CONFLICT 1506
FT /note="P -> S (in Ref. 4; AAH68318)"
FT /evidence="ECO:0000305"
FT CONFLICT 1715
FT /note="L -> P (in Ref. 1; BAD32440)"
FT /evidence="ECO:0000305"
FT CONFLICT 2189
FT /note="R -> I (in Ref. 1; BAD32440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2350 AA; 260639 MW; B17F6FAEB48FBE73 CRC64;
MQGPYSLNGY RVRVYRQDSA TQWFTGIITH HDLFTRTMIV MNDQVLEPQN VDPSMVQMTF
LDDVVHSLLK GENIGITSRR RSRASQNIST VHGHYTRAQA NSPRPAMNSQ AAVPKQNTHQ
QQQQRSIRPN KRKGSDSSIP DEEKMKEDKY DCVSRGENPK GKNKHVVTKR RKPEEAEKRL
SMKRLRTDNA SDASESSDAE SSSKRVTETS SSEPMPEYEP KNKVTSKVNG EEGQSQAAEE
AGEETLIDTR PPWDQMQEDK NHNEGEKPKS TDSHLQDKMT LRSSEQATVA DHNSNDSVLQ
ECNVENQRTV ELLPKDRLVS RTPTPKCVTD IKNDTHSERA AQENLNTFGL QTPENMDPNV
SDSKHSNAKY LETAKQDCDQ SWVSDVVKVD LTQSSVTNAP SGSDKRDTEK ERNHYVSYMS
SLSAVSVTED QLHKRSPPPE TIKAKLTTSV DTQKAKSSSS PEVVKPKITH SPDSVKSKAA
YGNSQAVGER RLANKIEHEL SRGSFHPVPT RGSALETTKS PLIIDKNEHF TVYRDPALIG
SETGANHISP FLSQHPFSLH SSSHRTCLNP GTHHPALTPG PHLLAGSTSQ TPLPTINTHP
LTSGPHHPVH HPHLLPTVLP GVPTASLLGG HPRLESAHAS SLSHLALAHQ QQQQLLQHQS
PHLLGQAHPS ASYNQLGLYP IIWQYPNGTH AYSGLGLPSS KWVHPENAVN AEASLRRNSP
SPWLHQPTPV TSADGIGLLS HIPVRPSSAE PHRPHKITVH SSPPLTKTLA DHHKEELERK
AFMEPLRSNA STSVKGDLDL NRSQAGKDCH LHRHFVGPRP PQETGERLNK YKEEHRRILQ
ESIDVAPFTT KIKGHEVERE NYSRVVPSSS SPKSHAIKQD KDVDRSVSEI YKMKHSVPQS
LPQSNYFTTL SNSVVNEPPR SYPSKEVSNI YTEKQNNNLS ATANPQTHSF ISSLSKPPPL
IKHQPESESL VGKIPDHLPH QSASHSVTTF RSDCRSPTHL TVSSTNALRS MPALHRAPVF
HPPIHHSLER KESSYSSLSP PTLTPVMPVN AGGKVQESQK PPTLIPEPKD SQSNFKNSSD
QSLTEMWRSN NNLNREKAEW PVEKSSGKSQ AAVASVIVRP PSSTKVDSVP SVPLASKDRV
CERSSSGANK TDYLKPEAGE TGRIILPNVN LESAHVKSEK NFEAVSQGNV PVSVMSAVNV
VSTTKADVFT SAATTTSVSS LSSAETSYSL SNTISASTPF ECTSSKSVVS QAVAQAKDCT
VSTAVPGTLA CSKTGSAVQP GSGFSGTTDF IHLKKHKAAL AAAQFKNSSV SEAELNTVRN
QTVAASLPLD STMTCTASNK AISVGNGPAA QSSQPNYHTK LKKAWLTRHS EEDKNTNKME
NSGNSVSEII KPCSVNLIAS TSNDIENRAD GRVAVDKYGR DEKVSRRKAK RTYESGSESG
DSDESESKSE QRTKRQPKPT YKKKQNDLQK RKGEVEEDSK PNGVLSRSAK DKSKLKLQNS
NSAGVPRSVL KDWRKVKKLK QTGESFLQDD SCCEIGPNLQ KCRECRLIRS KKGEESTHSP
VFCRFYYFRR LSFSKNGVVR IDGFSSPDQY DDEAMSLWTH ENYEDDEVDV ETSKYILDII
GDKFCQLVTS EKTALSWVKK DAKIAWKRAV RGVREMCDAC EATLFNVHWV CRKCGFVACL
DCYKAKERKS SRDKELYAWM KCVKGQPHDH KHLMLTQIIP GSVLTDLLDA MHILREKYGI
KSHCHCTNRQ NLQGGNVPTM NGVSQVLQNV LHHSNKTSVS LPESQQQNSP QKSQTNGNSS
PGSASTDSRL TPPESQSPLH WLADLAEQKS REEKQENKEF TLEREIKEDG DQDASDSPNG
STSPPASQSN EQGSTLRDLL TTTAGKLRVG STDAGIAFAP VYSMGTSSGK GGRTMPNILD
DIIASVVENK IPPNKTSKIN IKSEPNEEPK ESSLPATDES NKSYRDIPHS WICDQHILWL
KDYKNSNNWK LFKECWKQGQ PAVVSGVHKK MNISLWKAES ISLDFGDHQA DLLNCKDSIV
SNANVKEFWD GFEEVSKRQK NKGGETVVLK LKDCPSGEDF KAMMPTRYED FLRCLPLPEY
CNPEGKFNLA SHLPGFFVRP DLGPRLCSAY GVAAAKDHDI GTTNLHIEAS DVVNVLVYVG
IAKGNGVLSK AGILKKFEEE ELDDVLRKRL KDSSEIPGAL WHIYAGKDVD KIREFLQKIS
KEQGLEVLPE HDPIRDQSWY VNRKLRQRLL EEYGVRACTL IQFLGDAIVL PAGTLHQVQN
FHSCVQVTED FVSPEHLVQS FHLTQELRLL KEEINYDDKL QVKNILYHAV KEMVRALKMH
EDEVEDMEDT
