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Lysine-specific demethylase 5A (EC 1.14.11.-) (Histone demethylase JARID1A) (Jumonji/ARID domain-containing protein 1A) (Retinoblastoma-binding protein 2) (RBBP-2)

 KDM5A_MOUSE             Reviewed;        1690 AA.
Q3UXZ9; Q3TM94; Q3UMI5; Q66JZ3;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
28-MAR-2018, entry version 115.
RecName: Full=Lysine-specific demethylase 5A;
EC=1.14.11.-;
AltName: Full=Histone demethylase JARID1A;
AltName: Full=Jumonji/ARID domain-containing protein 1A;
AltName: Full=Retinoblastoma-binding protein 2;
Short=RBBP-2;
Name=Kdm5a; Synonyms=Jarid1a, Rbp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1552.
STRAIN=C57BL/6J; TISSUE=Lung, and Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1099.
STRAIN=C57BL/6J; TISSUE=Germ cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 1538-1546, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17320163; DOI=10.1016/j.cell.2007.02.013;
Klose R.J., Yan Q., Tothova Z., Yamane K., Erdjument-Bromage H.,
Tempst P., Gilliland D.G., Zhang Y., Kaelin W.G. Jr.;
"The retinoblastoma binding protein RBP2 is an H3K4 demethylase.";
Cell 128:889-900(2007).
[6]
FUNCTION.
PubMed=17320161; DOI=10.1016/j.cell.2007.02.003;
Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S.,
Sennels L., Rappsilber J., Hansen K.H., Salcini A.E., Helin K.;
"RBP2 belongs to a family of demethylases, specific for tri-and
dimethylated lysine 4 on histone 3.";
Cell 128:1063-1076(2007).
[7]
SUBCELLULAR LOCATION, DOMAIN GSGFP MOTIF, AND INTERACTION WITH SUZ12.
PubMed=20064375; DOI=10.1016/j.cell.2009.12.002;
Peng J.C., Valouev A., Swigut T., Zhang J., Zhao Y., Sidow A.,
Wysocka J.;
"Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and
target gene occupancy in pluripotent cells.";
Cell 139:1290-1302(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111; THR-1343;
SER-1345; TYR-1595; SER-1598; SER-1603 AND SER-1666, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, AND INTERACTION WITH ARNTL; CLOCK AND HDAC1.
PubMed=21960634; DOI=10.1126/science.1206022;
DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J.,
Panda S.;
"Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and
influences the circadian clock.";
Science 333:1881-1885(2011).
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
4' of histone H3, thereby playing a central role in histone code.
Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36',
H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and
dimethylated but not monomethylated H3 'Lys-4' (PubMed:17320161,
PubMed:17320163). Regulates specific gene transcription through
DNA-binding on 5'-CCGCCC-3' motif. May stimulate transcription
mediated by nuclear receptors. Involved in transcriptional
regulation of Hox proteins during cell differentiation (By
similarity). May participate in transcriptional repression of
cytokines such as CXCL12. Plays a role in the regulation of the
circadian rhythm and in maintaining the normal periodicity of the
circadian clock. In a histone demethylase-independent manner, acts
as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional
activation of PER1/2 and other clock-controlled genes and
increases histone acetylation at PER1/2 promoters by inhibiting
the activity of HDAC1 (PubMed:21960634). Seems to act as a
transcriptional corepressor for some genes such as MT1F and to
favor the proliferation of cancer cells (By similarity).
{ECO:0000250|UniProtKB:P29375, ECO:0000269|PubMed:17320161,
ECO:0000269|PubMed:17320163, ECO:0000269|PubMed:21960634}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with RB1, ESR1, MYC, MYCN and LMO2 (By
similarity). Interacts with SUZ12; the interaction is direct
(PubMed:20064375). Interacts with HDAC1, ARNTL/BMAL1 and CLOCK
(PubMed:21960634). Interacts (via PHD-type 1 zinc finger) with
histone H3 unmodified at 'Lys-4' and (via PHD-type 3 zinc finger)
with histone H3 di- and trimethylated at 'Lys-4' (By similarity).
{ECO:0000250|UniProtKB:P29375, ECO:0000269|PubMed:20064375,
ECO:0000269|PubMed:21960634}.
-!- INTERACTION:
Q80U70:Suz12; NbExp=2; IntAct=EBI-2531441, EBI-2526494;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:P29375}. Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537,
ECO:0000269|PubMed:20064375}. Note=Occupies promoters of genes
involved in RNA metabolism and mitochondrial function.
{ECO:0000269|PubMed:20064375}.
-!- DOMAIN: The GSGFP motif is required for the interaction with SUZ12
(PubMed:20064375). The ARID domain specifically binds to the
CCGCCC motif and is required for the lysine-specific histone
demethylase activity. The PHD-type 3 zinc finger is required for
the interaction with histone H3 di- and trimethylated at 'Lys-4'
(By similarity). {ECO:0000250|UniProtKB:P29375,
ECO:0000269|PubMed:20064375}.
-!- DISRUPTION PHENOTYPE: Mice are grossly normal, except that they
exhibit behavioral abnormalities when held upside down by the
tail, and slight hematological defects.
{ECO:0000269|PubMed:17320163}.
-!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE22414.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AC155720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC078896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK135085; BAE22414.1; ALT_INIT; mRNA.
EMBL; AK144877; BAE26113.1; -; mRNA.
EMBL; AK166055; BAE38548.1; -; mRNA.
EMBL; BC080691; AAH80691.1; ALT_TERM; mRNA.
CCDS; CCDS51889.1; -.
RefSeq; NP_666109.2; NM_145997.2.
UniGene; Mm.404761; -.
UniGene; Mm.463658; -.
ProteinModelPortal; Q3UXZ9; -.
SMR; Q3UXZ9; -.
BioGrid; 229572; 8.
IntAct; Q3UXZ9; 7.
STRING; 10090.ENSMUSP00000098558; -.
BindingDB; Q3UXZ9; -.
ChEMBL; CHEMBL3707461; -.
iPTMnet; Q3UXZ9; -.
PhosphoSitePlus; Q3UXZ9; -.
EPD; Q3UXZ9; -.
MaxQB; Q3UXZ9; -.
PaxDb; Q3UXZ9; -.
PeptideAtlas; Q3UXZ9; -.
PRIDE; Q3UXZ9; -.
Ensembl; ENSMUST00000005108; ENSMUSP00000005108; ENSMUSG00000030180.
GeneID; 214899; -.
KEGG; mmu:214899; -.
UCSC; uc009dne.2; mouse.
CTD; 5927; -.
MGI; MGI:2136980; Kdm5a.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410XR9J; LUCA.
GeneTree; ENSGT00530000063118; -.
HOGENOM; HOG000290719; -.
InParanoid; Q3UXZ9; -.
KO; K11446; -.
OMA; CHEWYHG; -.
PhylomeDB; Q3UXZ9; -.
TreeFam; TF106476; -.
BRENDA; 1.14.11.B2; 3474.
Reactome; R-MMU-3214842; HDMs demethylate histones.
ChiTaRS; Kdm5a; mouse.
PRO; PR:Q3UXZ9; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030180; -.
CleanEx; MM_RBP2; -.
ExpressionAtlas; Q3UXZ9; baseline and differential.
Genevisible; Q3UXZ9; MM.
GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032993; C:protein-DNA complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; ISO:MGI.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0034648; F:histone demethylase activity (H3-dimethyl-K4 specific); ISO:MGI.
GO; GO:0034647; F:histone demethylase activity (H3-trimethyl-K4 specific); ISO:MGI.
GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0034720; P:histone H3-K4 demethylation; IMP:MGI.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:1901726; P:negative regulation of histone deacetylase activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0051090; P:regulation of DNA binding transcription factor activity; ISO:MGI.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.150.60; -; 1.
Gene3D; 3.30.40.10; -; 3.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR003349; JmjN.
InterPro; IPR013637; Lys_sp_deMease-like_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR004198; Znf_C5HC2.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF01388; ARID; 1.
Pfam; PF02373; JmjC; 1.
Pfam; PF02375; JmjN; 1.
Pfam; PF00628; PHD; 2.
Pfam; PF08429; PLU-1; 1.
Pfam; PF02928; zf-C5HC2; 1.
SMART; SM00501; BRIGHT; 1.
SMART; SM00558; JmjC; 1.
SMART; SM00545; JmjN; 1.
SMART; SM00249; PHD; 3.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF57903; SSF57903; 3.
PROSITE; PS51011; ARID; 1.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS51183; JMJN; 1.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 3.
1: Evidence at protein level;
Activator; Biological rhythms; Chromatin regulator; Complete proteome;
Developmental protein; Dioxygenase; Direct protein sequencing; Iron;
Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1690 Lysine-specific demethylase 5A.
/FTId=PRO_0000292411.
DOMAIN 19 60 JmjN. {ECO:0000255|PROSITE-
ProRule:PRU00537}.
DOMAIN 84 174 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
DOMAIN 437 603 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 293 343 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 676 728 C5HC2. {ECO:0000250|UniProtKB:P29375}.
ZN_FING 1153 1210 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1599 1653 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 1622 1690 Interaction with LMO2.
{ECO:0000250|UniProtKB:P29375}.
MOTIF 419 423 GSGFP motif.
{ECO:0000269|PubMed:20064375}.
COMPBIAS 1484 1579 Lys-rich.
METAL 483 483 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 485 485 Iron; catalytic.
{ECO:0000250|UniProtKB:P29375}.
METAL 571 571 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
BINDING 409 409 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 491 491 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 493 493 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 501 501 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000250|UniProtKB:P29375}.
MOD_RES 1111 1111 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1330 1330 Phosphoserine.
{ECO:0000250|UniProtKB:P29375}.
MOD_RES 1331 1331 Phosphoserine.
{ECO:0000250|UniProtKB:P29375}.
MOD_RES 1343 1343 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1345 1345 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1438 1438 Phosphoserine.
{ECO:0000250|UniProtKB:P29375}.
MOD_RES 1488 1488 Phosphoserine.
{ECO:0000250|UniProtKB:P29375}.
MOD_RES 1595 1595 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1598 1598 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1603 1603 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1666 1666 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 191 191 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P29375}.
CROSSLNK 1007 1007 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P29375}.
CONFLICT 10 10 A -> S (in Ref. 2; BAE38548).
{ECO:0000305}.
CONFLICT 14 14 V -> R (in Ref. 2; BAE38548).
{ECO:0000305}.
CONFLICT 17 17 P -> A (in Ref. 2; BAE38548).
{ECO:0000305}.
CONFLICT 24 24 P -> A (in Ref. 2; BAE38548).
{ECO:0000305}.
CONFLICT 544 544 V -> A (in Ref. 2; BAE38548).
{ECO:0000305}.
CONFLICT 1272 1272 A -> P (in Ref. 2; BAE22414).
{ECO:0000305}.
SEQUENCE 1690 AA; 192216 MW; EFCF56AAAA51F0FC CRC64;
MASVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PFAEKTGICK IRPPKDWQPP
FACEVKTFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL QGSTLKIPVV ERKILDLYAL
SKIVASKGGF EIVTKEKKWS KVGSRLGYLP GKGTGSLLKS HYERILYPYE LFQSGVSLMG
VQMPDLDLKE KVEAEVLSTD IQPSPERGTR MNIPPKRTRR VKSQSDSGEV NRNTELKKLQ
IFGAGPKVVG LAVGAKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
RGNNEDKLLL CDGCDDSYHT FCLLPPLPDV PKGDWRCPKC VAEECNKPRE AFGFEQAVRE
YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS IEEDVIVEYG ADISSKDFGS
GFPKKDGQRK MLPEEEEYAL SGWNLNNMPV LEQSVLAHIN VDISGMKVPW LYVGMCFSSF
CWHIEDHWSY SINYLHWGEP KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM
NPNVLMEHGV PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR ESVVQMGVVM
SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL YHPTDLCSCP MQNKCLRYRY
PLEDLPSLLY GVKVRAQSYD TWVNRVTEAL SASFNHKKDL IELRVMLEDA EDRKYPENDL
FRKLRDAVKE AETCGSVAQL LLSKKQKHRQ SSDSGKTRTK LTVEELKAFV QQLVSLPCVI
SQTRQVKNLL DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT VSERWEEKAK
VCLQARPRHS MANLENIVNE AKNIPAFLPN VLSLKEALQK AREWTAKVEA IQSGNNYAYL
EQLESLSAKG RPIPVRLDAL PQVESQVAAA RAWRERTGRT FLKKNSSHTL LQVLSPRTDI
GVYGSGKNRR KKVKEIIEKE KEKDLDLEPL SDLEEGLEES RDTAMVVAVF KEREQKEIEA
MHSLRAANLA KMTIVERIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
SSWQAKDVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT ERAMSWQDKA
RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL QKAAANPDLQ GHLPSFQQSA
FNRVVSSVSS SPHQTMDYDD EETDSDEDIR ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP
IKSEEVVTHM WTAPSFCAEH AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG
AKAQLEELMM VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSIE EKPLKMKGKD
SSEKKRKRKL EKVEQLFGEG KQKTKELKKI DKPKKKKLKL NVDKSKELNK LAKKLAKEEE
RKKKKEKAAA AKVELVKEST EKKRERKVLD IPSKYDWSGA EESDDENAVC AAQNCQRPCK
DKVDWVQCDG GCDEWFHQVC VGVSAEMAEN EDYICINCAK KQGPDSPGQA PPPPFLMSYK
LPMEDLKETS


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