CUX1_MOUSE
ID CUX1_MOUSE Reviewed; 1515 AA.
AC P53564; O08994; P70301; Q571L6; Q91ZD2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 3.
DT 25-MAY-2022, entry version 179.
DE RecName: Full=Homeobox protein cut-like 1 {ECO:0000305};
DE AltName: Full=CCAAT displacement protein;
DE Short=CDP;
DE AltName: Full=Homeobox protein cux-1;
DE Contains:
DE RecName: Full=CDP/Cux p110 {ECO:0000303|PubMed:15099520};
GN Name=Cux1 {ECO:0000312|MGI:MGI:88568}; Synonyms=Cutl1, Cux, Kiaa4047;
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 [MRNA] (ISOFORM 4).
RC STRAIN=A/J, and BALB/cJ; TISSUE=Brain;
RX PubMed=7910552; DOI=10.1242/dev.119.3.881;
RA Valarche I., Tissier-Seta J.-P., Hirsch M.R., Martinez S., Goridis C.,
RA Brunet J.-F.;
RT "The mouse homeodomain protein Phox2 regulates Ncam promoter activity in
RT concert with Cux/CDP and is a putative determinant of neurotransmitter
RT phenotype.";
RL Development 119:881-896(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=8879483; DOI=10.1095/biolreprod55.4.731;
RA Vanden Heuvel G.B., Quaggin S.E., Igarashi P.;
RT "A unique variant of a homeobox gene related to Drosophila cut is expressed
RT in mouse testis.";
RL Biol. Reprod. 55:731-739(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND FUNCTION.
RX PubMed=11544187; DOI=10.1101/gad.200101;
RA Ellis T., Gambardella L., Horcher M., Tschanz S., Capol J., Bertram P.,
RA Jochum W., Barrandon Y., Busslinger M.;
RT "The transcriptional repressor CDP (Cutl1) is essential for epithelial cell
RT differentiation of the lung and the hair follicle.";
RL Genes Dev. 15:2307-2319(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryonic tail;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 121-1515 (ISOFORM 2), AND FUNCTION.
RC STRAIN=C57BL/6N;
RX PubMed=9858552; DOI=10.1128/mcb.19.1.284;
RA Wang Z., Goldstein A., Zong R.-T., Lin D., Neufeld E.J., Scheuermann R.H.,
RA Tucker P.W.;
RT "Cux/CDP homeoprotein is a component of NF-muNR and represses the
RT immunoglobulin heavy chain intronic enhancer by antagonizing the bright
RT transcription activator.";
RL Mol. Cell. Biol. 19:284-295(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 762-1515 (ISOFORMS 2/3/4/5).
RX PubMed=8840273; DOI=10.1038/ki.1996.336;
RA Vanden Heuvel G.B., Bodmer R., McConnell K.R., Nagami G.T., Igarashi P.;
RT "Expression of a cut-related homeobox gene in developing and polycystic
RT mouse kidney.";
RL Kidney Int. 50:453-461(1996).
RN [7]
RP INTERACTION WITH SATB1.
RX PubMed=10373541; DOI=10.1128/mcb.19.7.4918;
RA Liu J., Barnett A., Neufeld E.J., Dudley J.P.;
RT "Homeoproteins CDP and SATB1 interact: potential for tissue-specific
RT regulation.";
RL Mol. Cell. Biol. 19:4918-4926(1999).
RN [8]
RP FUNCTION, INTERACTION WITH BANP, AND SUBCELLULAR LOCATION.
RX PubMed=15371550; DOI=10.1093/nar/gkh807;
RA Kaul-Ghanekar R., Jalota-Badhwar A., Pavithra L., Tucker P.,
RA Chattopadhyay S.;
RT "SMAR1 and Cux/CDP modulate chromatin and act as negative regulators of the
RT TCRbeta enhancer (Ebeta).";
RL Nucleic Acids Res. 32:4862-4875(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND DNA-BINDING.
RX PubMed=15099520; DOI=10.1016/s1097-2765(04)00209-6;
RA Goulet B., Baruch A., Moon N.S., Poirier M., Sansregret L.L., Erickson A.,
RA Bogyo M., Nepveu A.;
RT "A cathepsin L isoform that is devoid of a signal peptide localizes to the
RT nucleus in S phase and processes the CDP/Cux transcription factor.";
RL Mol. Cell 14:207-219(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427; SER-1332 AND SER-1506,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20510857; DOI=10.1016/j.neuron.2010.04.038;
RA Cubelos B., Sebastian-Serrano A., Beccari L., Calcagnotto M.E.,
RA Cisneros E., Kim S., Dopazo A., Alvarez-Dolado M., Redondo J.M.,
RA Bovolenta P., Walsh C.A., Nieto M.;
RT "Cux1 and Cux2 regulate dendritic branching, spine morphology, and synapses
RT of the upper layer neurons of the cortex.";
RL Neuron 66:523-535(2010).
CC -!- FUNCTION: Transcription factor involved in the control of neuronal
CC differentiation in the brain. Regulates dendrite development and
CC branching, and dendritic spine formation in cortical layers II-III
CC (PubMed:20510857). Also involved in the control of synaptogenesis
CC (Probable). In addition, it has probably a broad role in mammalian
CC development as a repressor of developmentally regulated gene
CC expression. May act by preventing binding of positively-activing CCAAT
CC factors to promoters. Component of nf-munr repressor; binds to the
CC matrix attachment regions (MARs) (5' and 3') of the immunoglobulin
CC heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer
CC function by binding to MARbeta, an ATC-rich DNA sequence located
CC upstream of the TCR beta enhancer. Binds to the TH enhancer; may
CC require the basic helix-loop-helix protein TCF4 as a coactivator.
CC {ECO:0000269|PubMed:11544187, ECO:0000269|PubMed:15371550,
CC ECO:0000269|PubMed:20510857, ECO:0000269|PubMed:9858552,
CC ECO:0000305|PubMed:20510857}.
CC -!- FUNCTION: [CDP/Cux p110]: Plays a role in cell cycle progression, in
CC particular at the G1/S transition. As cells progress into S phase, a
CC fraction of CUX1 molecules is proteolytically processed into N-
CC terminally truncated proteins of 110 kDa. While CUX1 only transiently
CC binds to DNA and carries the CCAAT-displacement activity, CDP/Cux p110
CC makes a stable interaction with DNA and stimulates expression of genes
CC such as POLA1. {ECO:0000269|PubMed:15099520}.
CC -!- SUBUNIT: Interacts with BANP. Interacts with SATB1 (via DNA-binding
CC domains); the interaction inhibits the attachment of both proteins to
CC DNA. {ECO:0000269|PubMed:10373541, ECO:0000269|PubMed:15371550}.
CC -!- INTERACTION:
CC P53564; Q8VI24: Satb2; NbExp=3; IntAct=EBI-642309, EBI-5737999;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000255|PROSITE-ProRule:PRU00374, ECO:0000269|PubMed:15371550}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=5;
CC IsoId=P53564-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53564-2; Sequence=VSP_002311;
CC Name=3;
CC IsoId=P53564-3; Sequence=VSP_015749, VSP_015750;
CC Name=4;
CC IsoId=P53564-4; Sequence=VSP_015748;
CC Name=6;
CC IsoId=P53564-5; Sequence=VSP_017360;
CC Name=1; Synonyms=CASP;
CC IsoId=P70403-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: [Isoform 6]: Testis-specific where it is expressed
CC in germ cells. {ECO:0000269|PubMed:8879483}.
CC -!- DEVELOPMENTAL STAGE: In postpubertal testis, isoform 6 is expressed
CC from stages IV-V of spermatogenesis in the outer layer of round
CC spermatids. Expression continues through stages VI-VII but no
CC expression is detected in stages IX-XI. In prepubertal testis, isoform
CC 6 is expressed in post-meiotic germ cells at the round spermatid stage.
CC {ECO:0000269|PubMed:8879483}.
CC -!- PTM: Phosphorylated by PKA. {ECO:0000250|UniProtKB:P53565}.
CC -!- PTM: As cells progress into S phase, a fraction of CUX1 molecules is
CC proteolytically processed into N-terminally truncated proteins of 110
CC kDa by CTSL. Cell cycle-dependent processing of CUX1 serves to generate
CC a CDP/Cux p110 with distinct DNA binding and transcriptional
CC properties. {ECO:0000269|PubMed:15099520}.
CC -!- DISRUPTION PHENOTYPE: Brains from knockout mice show neurons in layer
CC II-III with a significant decrease in the dendritic length and the
CC number of branches, as well as a severe reduction of dendritic spines
CC density. {ECO:0000269|PubMed:20510857}.
CC -!- MISCELLANEOUS: Asn-1285 may participate in regulating DNA-binding
CC activity by promoting homo- and heterodimerization.
CC -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90358.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X75013; CAA52922.1; -; mRNA.
DR EMBL; U46684; AAB41146.1; -; mRNA.
DR EMBL; AY037807; AAK59986.1; -; mRNA.
DR EMBL; AK220173; BAD90358.1; ALT_INIT; mRNA.
DR EMBL; AF004225; AAD12485.1; -; mRNA.
DR EMBL; U46683; AAC52775.1; -; mRNA.
DR CCDS; CCDS71684.1; -. [P53564-3]
DR PIR; I48314; I48314.
DR RefSeq; NP_001278162.1; NM_001291233.1.
DR RefSeq; NP_001278163.1; NM_001291234.1.
DR RefSeq; NP_034116.3; NM_009986.4.
DR AlphaFoldDB; P53564; -.
DR SMR; P53564; -.
DR BioGRID; 198981; 6.
DR IntAct; P53564; 5.
DR MINT; P53564; -.
DR STRING; 10090.ENSMUSP00000004097; -.
DR iPTMnet; P53564; -.
DR PhosphoSitePlus; P53564; -.
DR EPD; P53564; -.
DR jPOST; P53564; -.
DR MaxQB; P53564; -.
DR PeptideAtlas; P53564; -.
DR PRIDE; P53564; -.
DR ProteomicsDB; 284063; -. [P53564-1]
DR ProteomicsDB; 284064; -. [P53564-2]
DR ProteomicsDB; 284065; -. [P53564-3]
DR ProteomicsDB; 284066; -. [P53564-4]
DR ProteomicsDB; 284067; -. [P53564-5]
DR DNASU; 13047; -.
DR GeneID; 13047; -.
DR KEGG; mmu:13047; -.
DR CTD; 1523; -.
DR MGI; MGI:88568; Cux1.
DR InParanoid; P53564; -.
DR OrthoDB; 181575at2759; -.
DR PhylomeDB; P53564; -.
DR BioGRID-ORCS; 13047; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Cux1; mouse.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P53564; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; 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:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IGI:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; ISO:MGI.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 3.
DR InterPro; IPR003350; CUT_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR Pfam; PF02376; CUT; 3.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM01109; CUT; 3.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 3.
DR PROSITE; PS51042; CUT; 3.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein; DNA-binding;
KW Homeobox; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1515
FT /note="Homeobox protein cut-like 1"
FT /id="PRO_0000202394"
FT CHAIN 754..1515
FT /note="CDP/Cux p110"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT /id="PRO_0000450798"
FT DNA_BIND 540..627
FT /note="CUT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 929..1016
FT /note="CUT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 1112..1199
FT /note="CUT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 1239..1298
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 393..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..361
FT /evidence="ECO:0000255"
FT COMPBIAS 433..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..923
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 641..642
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT SITE 745..753
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53565"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53565"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 1332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT MOD_RES 1506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 783
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 809
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 840
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT CROSSLNK 1279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39880"
FT VAR_SEQ 1..1055
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:8879483"
FT /id="VSP_017360"
FT VAR_SEQ 1..183
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:7910552"
FT /id="VSP_015748"
FT VAR_SEQ 1..10
FT /note="MLCVAGAKLK -> MAANVGSMFQYWKRFDLQQLQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015749"
FT VAR_SEQ 406..507
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9858552"
FT /id="VSP_002311"
FT VAR_SEQ 630..651
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015750"
FT CONFLICT 276
FT /note="V -> VEQ (in Ref. 3; AAK59986)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="R -> G (in Ref. 1; CAA52922 and 5; AAD12485)"
FT /evidence="ECO:0000305"
FT CONFLICT 1480
FT /note="G -> A (in Ref. 1; CAA52922)"
FT /evidence="ECO:0000305"
FT CONFLICT 1485
FT /note="P -> L (in Ref. 5; AAD12485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1515 AA; 165596 MW; 72BC6E8D8ECD78DE CRC64;
MLCVAGAKLK RELDATATVL ANRQDESEQS RKRLIEQSRE FKKNTPEDLR KQVAPLLKSF
QGEIDALSKR SKEAEAAFLT VYKRLIDVPD PVPALDVGQQ LEIKVQRLHD IETENQKLRE
TLEEYNKEFA EVKNQEVTIK ALKEKIREYE QTLKSQAETI ALEKEQKLQN DFAEKERKLQ
ETQMSTTSKL EEAEHKLQTL QTALEKTRTE LFDLKTKYDE ETTAKADEIE MIMTDLERAN
QRAEVAQREA ETLREQLSSA NHSLQLASQI QKAPDVAIEV LTRSSLEVEL AAKEREIAQL
VEDVQRLQAS LTKLRENSAS QISQLEQQLN AKNSTLKQLE EKLKGQADYE EVKKELNTLK
SMEFAPSEGA GTQDSTKPLE VLLLEKNRSL QSENATLRIS NSDLSGSARR KGRDQPESRR
PGPLPASPPP QLPRNTGEQV SNTNGTHHFS PAGLSQDFFS SNLASPSLPL ASTGKFALNS
LLQRQLMQSF YSKAMQEAGS TSTIFSTGPY STNSISSPSP LQQSPDVNGM APSPSQSESA
GSISEGEEID TAEIARQVKE QLIKHNIGQR IFGHYVLGLS QGSVSEILAR PKPWNKLTVR
GKEPFHKMKQ FLSDEQNILA LRSIQGRQRE NPGQSLNRLF QEVPKRRNRS EGNITTRIRA
SETGSDEAIK SILEQAKREL QVQKTAEPVQ TSSTSSSGNS DDAIRSILQQ ARREMEAQQA
ALDPALKPAP LSQPDLTILT PKHLSASPMS TVSTYPPLAI SLKKTPAAPE TSTAALPSAP
ALKKEAQDVP TLDPPGSADA AQGVLRPMKS ELVRGSTWKD PWWSPIQPER RNLTSSEETK
ADETTASGKE RAGSSQPRAE RSQLQGPSAS AEYWKEWPSA ESPYSQSSEL SLTGASRSET
PQNSPLPSSP IVPMAKPAKP SVPPLTPEQY EVYMYQEVDT IELTRQVKEK LAKNGICQRI
FGEKVLGLSQ GSVSDMLSRP KPWSKLTQKG REPFIRMQLW LNGELGQGVL PVQGQQQGPV
LHSVASLQDP LQQGCVSSES TPKTSASCSP APESPMSSSE SVKSLTELVQ QPCPAIETSK
EGKPPEPSDP PASDSQPTTP LPLSGHSALS IQELVAMSPE LDTYGITKRV KEVLTDNNLG
QRLFGETILG LTQGSVSDLL ARPKPWHKLS LKGREPFVRM QLWLNDPNNV EKLMDMKRME
KKAYMKRRHS SVSDSQPCEP PSVGIDYSQG ASPQPQHQLK KPRVVLAPEE KEALKRAYQQ
KPYPSPKTIE ELATQLNLKT STVINWFHNY RSRIRRELFI EEIQAGSQGQ AGASDSPSAR
SSRAAPSSEG DSCDGVEATD AEEPGGNIVA TKSQGGLAEV AAAPADREEA TQPAEKAKAQ
PLCSGTPGQD DGEDASRPRP LPEGLADAPA PVPSLAAPAA GEDAATSATA PATATEAPGA
ARAGPAERSS ALPSTSAPAN APARRPSSLQ SLFGLPEAAG ARDNPVRKKK AANLNSIIHR
LEKAASREEP IEWEF
