DPF3_MOUSE
ID DPF3_MOUSE Reviewed; 378 AA.
AC P58269; Q80W78; Q8CAD8;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger protein DPF3;
DE AltName: Full=BRG1-associated factor 45C;
DE Short=BAF45C;
DE AltName: Full=Zinc finger protein cer-d4;
GN Name=Dpf3; Synonyms=Baf45c, Cerd4;
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 2).
RC STRAIN=CD-1; TISSUE=Trigeminal ganglion;
RX PubMed=11845289; DOI=10.1007/s00335-001-3039-1;
RA Ninkina N.N., Mertsalov I.B., Kulikova D.A., Alimova-Kost M.V.,
RA Simonova O.B., Korochkin L.I., Kiselev S.L., Buchman V.L.;
RT "Cerd4, third member of the d4 gene family: expression and organization of
RT genomic locus.";
RL Mamm. Genome 12:862-866(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=8812431; DOI=10.1006/geno.1996.0440;
RA Chestkov A.V., Baka I.D., Kost M.V., Georgiev G.P., Buchman V.L.;
RT "The d4 gene family in the human genome.";
RL Genomics 36:174-177(1996).
RN [5]
RP FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE NBAF COMPLEX, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA Aebersold R., Graef I.A., Crabtree G.R.;
RT "An essential switch in subunit composition of a chromatin remodeling
RT complex during neural development.";
RL Neuron 55:201-215(2007).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18765789; DOI=10.1101/gad.471408;
RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
RT "Regulation of muscle development by DPF3, a novel histone acetylation and
RT methylation reader of the BAF chromatin remodeling complex.";
RL Genes Dev. 22:2370-2384(2008).
RN [7]
RP FUNCTION (ISOFORM 2), AND INTERACTION WITH HDGFL2 (ISOFORM 2).
RX PubMed=32459350; DOI=10.1093/nar/gkaa441;
RA Zhu X., Lan B., Yi X., He C., Dang L., Zhou X., Lu Y., Sun Y., Liu Z.,
RA Bai X., Zhang K., Li B., Li M.J., Chen Y., Zhang L.;
RT "HRP2-DPF3a-BAF complex coordinates histone modification and chromatin
RT remodeling to regulate myogenic gene transcription.";
RL Nucleic Acids Res. 48:6563-6582(2020).
CC -!- FUNCTION: Muscle-specific component of the BAF complex, a multiprotein
CC complex involved in transcriptional activation and repression of select
CC genes by chromatin remodeling (alteration of DNA-nucleosome topology).
CC Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac,
CC H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a
CC tissue-specific anchor between histone acetylations and methylations
CC and chromatin remodeling. It thereby probably plays an essential role
CC in heart and skeletal muscle development (By similarity). Belongs to
CC the neuron-specific chromatin remodeling complex (nBAF complex). During
CC neural development a switch from a stem/progenitor to a post-mitotic
CC chromatin remodeling mechanism occurs as neurons exit the cell cycle
CC and become committed to their adult state. The transition from
CC proliferating neural stem/progenitor cells to post-mitotic neurons
CC requires a switch in subunit composition of the npBAF and nBAF
CC complexes. As neural progenitors exit mitosis and differentiate into
CC neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A,
CC are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
CC or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF
CC complex is essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth.
CC {ECO:0000250, ECO:0000269|PubMed:17640523}.
CC -!- FUNCTION: [Isoform 2]: Acts as a regulator of myogenesis in cooperation
CC with HDGFL2 (PubMed:32459350). Mediates the interaction of HDGFL2 with
CC the BAF complex (PubMed:32459350). HDGFL2-DPF3a activate myogenic genes
CC by increasing chromatin accessibility through recruitment of
CC SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic
CC gene promoters (PubMed:32459350). {ECO:0000269|PubMed:32459350}.
CC -!- SUBUNIT: Component of the BAF complex, which includes at least actin
CC (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A,
CC ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
CC SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A,
CC SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In muscle cells, the
CC BAF complex also contains DPF3 (By similarity). Interacts with
CC acetylated histones H3 and H4 (By similarity). Component of neuron-
CC specific chromatin remodeling complex (nBAF complex) composed of at
CC least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523).
CC {ECO:0000250|UniProtKB:Q92784, ECO:0000269|PubMed:17640523}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with HDGFL2 (PubMed:32459350).
CC Interacts with SMARCA4/BRG1/BAF190A, SMARCC1/BAF155 and SMARCD1/BAF60A
CC (By similarity). {ECO:0000250|UniProtKB:Q92784,
CC ECO:0000269|PubMed:32459350}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92784}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=DPF3b;
CC IsoId=P58269-1; Sequence=Displayed;
CC Name=2; Synonyms=DPF3a;
CC IsoId=P58269-2; Sequence=VSP_035887;
CC Name=3;
CC IsoId=P58269-3; Sequence=VSP_035886, VSP_035887;
CC Name=4;
CC IsoId=P58269-4; Sequence=VSP_035885, VSP_035887;
CC -!- TISSUE SPECIFICITY: Expressed in the heart and somites. Expressed in
CC cerebellum and spinal cord, but not in cerebral cortex. Expressed
CC specifically in post-mitotic neurons (at protein level).
CC {ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:18765789,
CC ECO:0000269|PubMed:8812431}.
CC -!- DEVELOPMENTAL STAGE: First expressed in the first differentiating
CC cardiomyocytes of the cardiac crescent at 7.5 dpc and in the first
CC somites at 8.0 dpc. In the heart, expression is restricted to the
CC myocardial compartment. In the developing forebrain and cerebellar
CC primordium, strictly expressed in post-mitotic neurons.
CC {ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:18765789}.
CC -!- DOMAIN: The PHD-type zinc fingers mediate the binding to acetylated
CC histones. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}.
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DR EMBL; AF362750; AAK54538.1; -; mRNA.
DR EMBL; AK039011; BAC30204.1; -; mRNA.
DR EMBL; BC048572; AAH48572.1; -; mRNA.
DR CCDS; CCDS56846.1; -. [P58269-3]
DR CCDS; CCDS59574.1; -. [P58269-1]
DR RefSeq; NP_001254554.1; NM_001267625.1. [P58269-1]
DR RefSeq; NP_478119.1; NM_058212.2. [P58269-3]
DR AlphaFoldDB; P58269; -.
DR BMRB; P58269; -.
DR SMR; P58269; -.
DR ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1244; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1246; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1256; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1258; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR STRING; 10090.ENSMUSP00000136280; -.
DR iPTMnet; P58269; -.
DR PhosphoSitePlus; P58269; -.
DR MaxQB; P58269; -.
DR PaxDb; P58269; -.
DR PeptideAtlas; P58269; -.
DR PRIDE; P58269; -.
DR ProteomicsDB; 277377; -. [P58269-1]
DR ProteomicsDB; 277378; -. [P58269-2]
DR ProteomicsDB; 277379; -. [P58269-3]
DR ProteomicsDB; 277380; -. [P58269-4]
DR Antibodypedia; 25263; 134 antibodies from 23 providers.
DR DNASU; 70127; -.
DR Ensembl; ENSMUST00000177801; ENSMUSP00000136740; ENSMUSG00000021221. [P58269-4]
DR Ensembl; ENSMUST00000177959; ENSMUSP00000137477; ENSMUSG00000021221. [P58269-3]
DR Ensembl; ENSMUST00000178756; ENSMUSP00000136280; ENSMUSG00000021221. [P58269-1]
DR GeneID; 70127; -.
DR KEGG; mmu:70127; -.
DR UCSC; uc007odc.2; mouse. [P58269-1]
DR UCSC; uc007odd.2; mouse. [P58269-3]
DR CTD; 8110; -.
DR MGI; MGI:1917377; Dpf3.
DR VEuPathDB; HostDB:ENSMUSG00000021221; -.
DR eggNOG; KOG1244; Eukaryota.
DR GeneTree; ENSGT00940000159153; -.
DR HOGENOM; CLU_038980_0_1_1; -.
DR InParanoid; P58269; -.
DR OMA; HYTHFHN; -.
DR OrthoDB; 708781at2759; -.
DR PhylomeDB; P58269; -.
DR TreeFam; TF318971; -.
DR BioGRID-ORCS; 70127; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Dpf3; mouse.
DR PRO; PR:P58269; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P58269; protein.
DR Bgee; ENSMUSG00000021221; Expressed in retinal neural layer and 122 other tissues.
DR ExpressionAtlas; P58269; baseline and differential.
DR Genevisible; P58269; MM.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016514; C:SWI/SNF complex; IC:ComplexPortal.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025750; DPF1-3_N.
DR InterPro; IPR038047; DPF3.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615:SF120; PTHR10615:SF120; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF14051; Requiem_N; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator; Isopeptide bond;
KW Metal-binding; Myogenesis; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..378
FT /note="Zinc finger protein DPF3"
FT /id="PRO_0000168155"
FT ZN_FING 198..221
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 259..319
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 316..366
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 146..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92784"
FT VAR_SEQ 1..55
FT /note="MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNN
FT CYI -> MGCLPKGHNRPGA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035885"
FT VAR_SEQ 101
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_035886"
FT VAR_SEQ 291..378
FT /note="GHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYH
FT MYCLNPPVAEPPEGSWSCHLCWELLKEKASAFGCQA -> AHLGGEGRKEKEAAAAART
FT TEDLFGSTSESDTSTFYGFDEDDLEEPRSCRGRRSGRGSPTADKKGSC (in
FT isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11845289,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035887"
FT REGION P58269-2:317..332
FT /note="Interaction with HDGFL2"
FT /evidence="ECO:0000250|UniProtKB:Q92784"
FT MOD_RES P58269-2:323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92784"
SQ SEQUENCE 378 AA; 43070 MW; 0B0B93651BF72233 CRC64;
MATVIHNPLK ALGDQFYKEA IEHCRSYNSR LCAERSVRLP FLDSQTGVAQ NNCYIWMEKR
HRGPGLAPGQ LYTYPARCWR KKRRLHPPED PKLRLLEIKP EVELPLKKDG FTSESTTLEA
LLRGEGVEKK VDAREEESIQ EIQRVLENDE NVEEGNEEED LEEDVPKRKN RTRGRARGSA
GGRRRHDAAS QEDHDKPYVC DICGKRYKNR PGLSYHYAHT HLASEEGDEA QDQETRSPPN
HRNENHRPQK GPDGTVIPNN YCDFCLGGSN MNKKSGRPEE LVSCADCGRS GHPTCLQFTL
NMTEAVKTYK WQCIECKSCI LCGTSENDDQ LLFCDDCDRG YHMYCLNPPV AEPPEGSWSC
HLCWELLKEK ASAFGCQA
