KDM3A_MOUSE
ID KDM3A_MOUSE Reviewed; 1323 AA.
AC Q6PCM1; Q2MJQ6; Q3TKW8; Q3UML3; Q6ZQ57; Q8K2J6; Q8K2K4; Q8R350;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Lysine-specific demethylase 3A;
DE EC=1.14.11.65 {ECO:0000250|UniProtKB:Q9Y4C1};
DE AltName: Full=JmjC domain-containing histone demethylation protein 2A;
DE AltName: Full=Jumonji domain-containing protein 1A;
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase 3A {ECO:0000305};
GN Name=Kdm3a; Synonyms=Jhdm2a, Jmjd1a, Kiaa0742;
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] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1034 (ISOFORM 2).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-834.
RC TISSUE=Lung;
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 [MRNA] OF 115-1323.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RA Knebel J., De Haro L., Janknecht R.;
RT "Characterization of murine Jmjd1a/TSGA.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17943087; DOI=10.1038/nature06236;
RA Okada Y., Scott G., Ray M.K., Mishina Y., Zhang Y.;
RT "Histone demethylase JHDM2A is critical for Tnp1 and Prm1 transcription and
RT spermatogenesis.";
RL Nature 450:119-123(2007).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19194461; DOI=10.1038/nature07777;
RA Tateishi K., Okada Y., Kallin E.M., Zhang Y.;
RT "Role of Jhdm2a in regulating metabolic gene expression and obesity
RT resistance.";
RL Nature 458:757-761(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code.
CC Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue,
CC with a preference for dimethylated residue, while it has weak or no
CC activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue
CC generates formaldehyde and succinate. Involved in hormone-dependent
CC transcriptional activation, by participating in recruitment to
CC androgen-receptor target genes, resulting in H3 'Lys-9' demethylation
CC and transcriptional activation (By similarity). Involved in
CC spermatogenesis by regulating expression of target genes such as PRM1
CC and TNP1 which are required for packaging and condensation of sperm
CC chromatin (PubMed:17943087). Involved in obesity resistance through
CC regulation of metabolic genes such as PPARA and UCP1. {ECO:0000250,
CC ECO:0000269|PubMed:17943087, ECO:0000269|PubMed:19194461}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4C1};
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: Cytoplasm {ECO:0000269|PubMed:17943087}. Nucleus
CC {ECO:0000269|PubMed:17943087}. Note=Nuclear in round spermatids. When
CC spermatids start to elongate, localizes to the cytoplasm where it forms
CC distinct foci which disappear in mature spermatozoa.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PCM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PCM1-2; Sequence=VSP_018296, VSP_018297;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis (at protein level). Also
CC expressed at high levels in tissues responsive to sympathetic nerve
CC activity such as brown adipose tissue and skeletal muscle.
CC {ECO:0000269|PubMed:17943087}.
CC -!- DEVELOPMENTAL STAGE: Expression increases significantly during
CC spermatogenesis with a 70-fold increase from day 7 testis to day 30
CC testis. First detected in the late pachytene stage, increases in
CC diplotene and secondary spermatocytes and reaches its highest levels in
CC round spermatids. {ECO:0000269|PubMed:17943087}.
CC -!- INDUCTION: By beta-adrenergic stimulation (at protein level).
CC {ECO:0000269|PubMed:19194461}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000250}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Spermatogenesis defects and adult obesity.
CC {ECO:0000269|PubMed:19194461}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98014.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129204; BAC98014.1; ALT_INIT; mRNA.
DR EMBL; BC026605; AAH26605.1; -; mRNA.
DR EMBL; BC031158; AAH31158.1; -; mRNA.
DR EMBL; BC031200; AAH31200.1; -; mRNA.
DR EMBL; BC059264; AAH59264.1; -; mRNA.
DR EMBL; AK144825; BAE26085.1; -; mRNA.
DR EMBL; AK166797; BAE39025.1; -; mRNA.
DR EMBL; DQ323991; ABC54567.1; -; mRNA.
DR CCDS; CCDS20233.1; -. [Q6PCM1-1]
DR RefSeq; NP_001033784.2; NM_001038695.3. [Q6PCM1-1]
DR RefSeq; NP_766589.1; NM_173001.3. [Q6PCM1-1]
DR RefSeq; XP_006505327.1; XM_006505264.3.
DR AlphaFoldDB; Q6PCM1; -.
DR SMR; Q6PCM1; -.
DR BioGRID; 222501; 7.
DR IntAct; Q6PCM1; 1.
DR STRING; 10090.ENSMUSP00000128789; -.
DR iPTMnet; Q6PCM1; -.
DR PhosphoSitePlus; Q6PCM1; -.
DR EPD; Q6PCM1; -.
DR MaxQB; Q6PCM1; -.
DR PaxDb; Q6PCM1; -.
DR PeptideAtlas; Q6PCM1; -.
DR PRIDE; Q6PCM1; -.
DR ProteomicsDB; 269288; -. [Q6PCM1-1]
DR ProteomicsDB; 269289; -. [Q6PCM1-2]
DR Antibodypedia; 32101; 435 antibodies from 35 providers.
DR Ensembl; ENSMUST00000065509; ENSMUSP00000065716; ENSMUSG00000053470. [Q6PCM1-1]
DR Ensembl; ENSMUST00000167220; ENSMUSP00000128789; ENSMUSG00000053470. [Q6PCM1-1]
DR Ensembl; ENSMUST00000207023; ENSMUSP00000145959; ENSMUSG00000053470. [Q6PCM1-1]
DR GeneID; 104263; -.
DR KEGG; mmu:104263; -.
DR UCSC; uc009cgy.3; mouse. [Q6PCM1-1]
DR CTD; 55818; -.
DR MGI; MGI:98847; Kdm3a.
DR VEuPathDB; HostDB:ENSMUSG00000053470; -.
DR eggNOG; KOG1356; Eukaryota.
DR GeneTree; ENSGT00940000160135; -.
DR HOGENOM; CLU_002991_0_0_1; -.
DR InParanoid; Q6PCM1; -.
DR OMA; SPQVTTH; -.
DR OrthoDB; 1185631at2759; -.
DR PhylomeDB; Q6PCM1; -.
DR TreeFam; TF324723; -.
DR BRENDA; 1.14.11.65; 3474.
DR BRENDA; 1.14.11.66; 3474.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 104263; 0 hits in 78 CRISPR screens.
DR ChiTaRS; Kdm3a; mouse.
DR PRO; PR:Q6PCM1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6PCM1; protein.
DR Bgee; ENSMUSG00000053470; Expressed in spermatocyte and 262 other tissues.
DR ExpressionAtlas; Q6PCM1; baseline and differential.
DR Genevisible; Q6PCM1; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; ISO:MGI.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:MGI.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0046293; P:formaldehyde biosynthetic process; ISO:MGI.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IMP:MGI.
DR GO; GO:0036123; P:histone H3-K9 dimethylation; IDA:MGI.
DR GO; GO:0051567; P:histone H3-K9 methylation; IMP:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:MGI.
DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0010628; P:positive regulation of gene expression; 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; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IMP:MGI.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007290; P:spermatid nucleus elongation; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; 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 Acetylation; Activator; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Differentiation; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Spermatogenesis;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1323
FT /note="Lysine-specific demethylase 3A"
FT /id="PRO_0000084286"
FT DOMAIN 1060..1283
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 662..687
FT /note="C6-type"
FT /evidence="ECO:0000255"
FT REGION 255..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 885..889
FT /note="LXXLL motif"
FT COMPBIAS 309..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C1"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C1"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C1"
FT MOD_RES 895
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C1"
FT VAR_SEQ 1..492
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018296"
FT VAR_SEQ 493..507
FT /note="NESCCTRSSNKTQTP -> MFWGDWKNIMEGAPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018297"
FT CONFLICT 144
FT /note="K -> Q (in Ref. 4; ABC54567)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="P -> L (in Ref. 4; ABC54567)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="A -> T (in Ref. 4; ABC54567)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="V -> F (in Ref. 2; AAH31200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1323 AA; 147847 MW; 6D9C4A7779076AED CRC64;
MVLTLGESWP VLVGKRFLSL SAAEGNEGGQ DNWDLERVAE WPWLSGTIRA VSHTDVTKKD
LKVCVEFDGE SWRKRRWIDV YSLQRKAFLV EHNLVLAERK SPEVPEQVIQ WPAIMYKSLL
DKAGLGAITS VRFLGDQQSV FVSKDLLKPI QDVNSLRLSL TDNQTVSKEF QALIVKHLDE
SHLLQGDKNL VGSEVKIYSL DPSTQWFSAT VVHGNPSSKT LQVNCEEIPA LKIVDPALIH
VEVVHDNFVT CGNSTRTGAV KRKSSENNGS SVSKQAKSCS EASPSMCPVQ SVPTTVFKEI
LLGCTAATPS SKDPRQQNTP QAANSPPNIG AKLPQGCHKQ NLPEELSSCL NTKPEVPRTK
PDVCKEGLLS SKSSQVGAGD LKILSEPKGS CIQPKTNTDQ ESRLESAPQP VTGLPKECLP
AKTSSKAELD IATTPELQKH LEHAASTSDD LSDKPEVKAG VTSLNSCAEK KVEPSHLGSQ
SQNLKETSVK VDNESCCTRS SNKTQTPPAR KSVLTDPDKV RKLQQSGEAF VQDDSCVNIV
AQLPKCRECR LDSLRKDKDQ QKDSPVFCRF FHFRRLQFNK HGVLRVEGFL TPNKYDSEAI
GLWLPLTKNV VGTDLDTAKY ILANIGDHFC QMVISEKEAM STIEPHRQVA WKRAVKGVRE
MCDVCDTTIF NLHWVCPRCG FGVCVDCYRM KRKNCQQGAA YKTFSWIRCV KSQIHEPENL
MPTQIIPGKA LYDVGDIVHS VRAKWGIKAN CPCSNRQFKL FSKPALKEDL KQTSLSGEKP
TLGTMVQQSS PVLEPVAVCG EAASKPASSV KPTCPTSTSP LNWLADLTSG NVNKENKEKQ
LTMPILKNEI KCLPPLPPLN KPSTVLHTFN STILTPVSNN NSGFLRNLLN SSTAKTENGL
KNTPKILDDI FASLVQNKTS SDSSKRPQGL TIKPSILGFD TPHYWLCDNR LLCLQDPNNK
SNWNVFRECW KQGQPVMVSG VHHKLNTELW KPESFRKEFG EQEVDLVNCR TNEIITGATV
GDFWDGFEDV PNRLKNDKEK EPMVLKLKDW PPGEDFRDMM PSRFDDLMAN IPLPEYTRRD
GKLNLASRLP NYFVRPDLGP KMYNAYGLIT PEDRKYGTTN LHLDVSDAAN VMVYVGIPKG
QCEQEEEVLR TIQDGDSDEL TIKRFIEGKE KPGALWHIYA AKDTEKIREF LKKVSEEQGQ
DNPADHDPIH DQSWYLDRSL RKRLYQEYGV QGWAIVQFLG DVVFIPAGAP HQVHNLYSCI
KVAEDFVSPE HVKHCFWLTQ EFRYLSQTHT NHEDKLQVKN VIYHAVKDAV AMLKASESSL
GKP
