ID   CHD1_MOUSE              Reviewed;        1711 AA.
AC   P40201; Q14BJ0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 1;
DE            Short=CHD-1;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD1;
GN   Name=Chd1; Synonyms=Chd-1;
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].
RX   PubMed=8460153; DOI=10.1073/pnas.90.6.2414;
RA   Delmas V., Stokes D.G., Perry R.P.;
RT   "A mammalian DNA-binding protein that contains a chromodomain and an
RT   SNF2/SWI2-like helicase domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:2414-2418(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   SUBCELLULAR LOCATION, AND DNA-BINDING.
RX   PubMed=7739555; DOI=10.1128/mcb.15.5.2745;
RA   Stokes D.G., Perry R.P.;
RT   "DNA-binding and chromatin localization properties of CHD1.";
RL   Mol. Cell. Biol. 15:2745-2753(1995).
RN   [5]
RP   SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH SSRP1.
RX   PubMed=10199952; DOI=10.1007/s004120050347;
RA   Kelley D.E., Stokes D.G., Perry R.P.;
RT   "CHD1 interacts with SSRP1 and depends on both its chromodomain and its
RT   ATPase/helicase-like domain for proper association with chromatin.";
RL   Chromosoma 108:10-25(1999).
RN   [6]
RP   INTERACTION WITH BCLAF1; NCOR; SRP20 AND SAF-B, AND FUNCTION.
RX   PubMed=12890497; DOI=10.1016/s0006-291x(03)01354-8;
RA   Tai H.H., Geisterfer M., Bell J.C., Moniwa M., Davie J.R., Boucher L.,
RA   McBurney M.W.;
RT   "CHD1 associates with NCoR and histone deacetylase as well as with RNA
RT   splicing proteins.";
RL   Biochem. Biophys. Res. Commun. 308:170-176(2003).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH CHROMATIN.
RX   PubMed=19587682; DOI=10.1038/nature08212;
RA   Gaspar-Maia A., Alajem A., Polesso F., Sridharan R., Mason M.J.,
RA   Heidersbach A., Ramalho-Santos J., McManus M.T., Plath K., Meshorer E.,
RA   Ramalho-Santos M.;
RT   "Chd1 regulates open chromatin and pluripotency of embryonic stem cells.";
RL   Nature 460:863-868(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-215, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, 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: ATP-dependent chromatin-remodeling factor which functions as
CC       substrate recognition component of the transcription regulatory histone
CC       acetylation (HAT) complex SAGA. Regulates polymerase II transcription.
CC       Also required for efficient transcription by RNA polymerase I, and more
CC       specifically the polymerase I transcription termination step. Regulates
CC       negatively DNA replication. Not only involved in transcription-related
CC       chromatin-remodeling, but also required to maintain a specific
CC       chromatin configuration across the genome. Required for the bridging of
CC       SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex
CC       to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing
CC       in part through physical bridging of spliceosomal components to H3K4me3
CC       (By similarity). Required for maintaining open chromatin and
CC       pluripotency in embryonic stem cells (PubMed:19587682). Is also
CC       associated with histone deacetylase (HDAC) activity (PubMed:12890497).
CC       {ECO:0000250|UniProtKB:O14646, ECO:0000269|PubMed:12890497,
CC       ECO:0000269|PubMed:19587682}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Component of the SAGA complex (By similarity). Specifically
CC       interacts with methylated H3K4me2 and H3K4me3. Interacts with the FACT
CC       complex, the PAF complex and the U2 snRNP. Interacts directly with
CC       PAF1, SFA3A1, SFA3A2, SFA3A3, SNF2 and SSRP1 (By similarity). Interacts
CC       with BCLAF1, NCoR, SRP20 and SAFB. {ECO:0000250,
CC       ECO:0000269|PubMed:10199952, ECO:0000269|PubMed:12890497,
CC       ECO:0000269|PubMed:19587682}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10199952,
CC       ECO:0000269|PubMed:7739555}. Cytoplasm {ECO:0000269|PubMed:7739555}.
CC       Note=Is released into the cytoplasm when cells enter mitosis and is
CC       reincorporated into chromatin during telophase-cytokinesis
CC       (PubMed:7739555).
CC   -!- TISSUE SPECIFICITY: Abundance is higher in cells representing early
CC       stages of the B-lymphoid lineage such as pre-B and B-cells, than in
CC       cells representing mature plasmacytes or other cell lineages such as
CC       fibroblasts.
CC   -!- DOMAIN: The 2 chromodomains are involved in the binding to the histone
CC       H3 methyllysine at position 4 (H3K4me3).
CC       {ECO:0000250|UniProtKB:O14646}.
CC   -!- DOMAIN: The CHD1 helical C-terminal domain (CHCT) binds DNA and
CC       nucleosomes. {ECO:0000250|UniProtKB:O14646}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; L10410; AAB08486.1; -; mRNA.
DR   EMBL; CH466630; EDL20454.1; -; Genomic_DNA.
DR   EMBL; BC115822; AAI15823.1; -; mRNA.
DR   CCDS; CCDS28416.1; -.
DR   PIR; A47392; A47392.
DR   RefSeq; NP_031716.2; NM_007690.3.
DR   AlphaFoldDB; P40201; -.
DR   SMR; P40201; -.
DR   BioGRID; 198693; 4.
DR   IntAct; P40201; 1.
DR   STRING; 10090.ENSMUSP00000024627; -.
DR   iPTMnet; P40201; -.
DR   PhosphoSitePlus; P40201; -.
DR   SwissPalm; P40201; -.
DR   EPD; P40201; -.
DR   jPOST; P40201; -.
DR   MaxQB; P40201; -.
DR   PaxDb; 10090-ENSMUSP00000024627; -.
DR   PeptideAtlas; P40201; -.
DR   ProteomicsDB; 279072; -.
DR   Pumba; P40201; -.
DR   Antibodypedia; 25129; 238 antibodies from 35 providers.
DR   DNASU; 12648; -.
DR   Ensembl; ENSMUST00000024627.14; ENSMUSP00000024627.8; ENSMUSG00000023852.15.
DR   GeneID; 12648; -.
DR   KEGG; mmu:12648; -.
DR   UCSC; uc008aou.2; mouse.
DR   AGR; MGI:88393; -.
DR   CTD; 1105; -.
DR   MGI; MGI:88393; Chd1.
DR   VEuPathDB; HostDB:ENSMUSG00000023852; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   GeneTree; ENSGT00940000156579; -.
DR   HOGENOM; CLU_000315_8_1_1; -.
DR   InParanoid; P40201; -.
DR   OMA; WVQIRDD; -.
DR   OrthoDB; 5482994at2759; -.
DR   PhylomeDB; P40201; -.
DR   TreeFam; TF300674; -.
DR   BioGRID-ORCS; 12648; 13 hits in 88 CRISPR screens.
DR   ChiTaRS; Chd1; mouse.
DR   PRO; PR:P40201; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P40201; Protein.
DR   Bgee; ENSMUSG00000023852; Expressed in embryonic post-anal tail and 258 other cell types or tissues.
DR   ExpressionAtlas; P40201; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; NAS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR   GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IGI:MGI.
DR   GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR   CDD; cd18661; CD2_tandem_CHD1-2_like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR040793; CDH1_2_SANT_HL1.
DR   InterPro; IPR025260; CHD1-like_C.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623:SF7; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR   Pfam; PF13907; CHD1-like_C; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01176; DUF4208; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00598; CHROMO_1; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   Genevisible; P40201; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Chromatin regulator; Cytoplasm; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..1711
FT                   /note="Chromodomain-helicase-DNA-binding protein 1"
FT                   /id="PRO_0000080225"
FT   DOMAIN          270..362
FT                   /note="Chromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          387..450
FT                   /note="Chromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          491..661
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          790..941
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REPEAT          1629..1633
FT                   /note="1"
FT   REPEAT          1635..1639
FT                   /note="2"
FT   REPEAT          1641..1645
FT                   /note="3"
FT   REGION          1..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1078..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1322..1407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1409..1511
FT                   /note="CHD1 helical C-terminal domain (CHCT)"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   REGION          1503..1588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1600..1657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1629..1645
FT                   /note="3 X 5 AA repeats of H-S-D-H-R"
FT   REGION          1670..1711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           612..615
FT                   /note="DEAH box"
FT   COMPBIAS        12..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..205
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1085..1106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1342
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1343..1386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1507..1522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1525..1588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1692..1711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         504..511
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         235
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         239
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         248
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         250
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1023
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1038
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1079
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1083
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14647"
FT   MOD_RES         1094
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1096
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1098
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1363
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14647"
FT   MOD_RES         1678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   MOD_RES         1690
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14646"
FT   CONFLICT        159
FT                   /note="S -> L (in Ref. 1; AAB08486)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1711 AA;  196385 MW;  51499636E943A856 CRC64;
     MNGHSDEESV RNGSGESSQS GDDCGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSDSGS
     QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA MLRKQPQQAQ QQRPASSNSG
     SEEDSSSSED SDDSSSGAKR KKHNDEDWQM SGSGSPSQSG SDSESEEERD KSSCDGTESD
     YEPKNKVRSR KPQNRSKSKN GKKILGQKKR QIDSSEDEDD EDYDNDKRSS RRQATVNVSY
     KEDEEMKTDS DDLLEVCGED VPQPEDEEFE TIERVMDCRV GRKGATGATT TIYAVEADGD
     PNAGFERNKE PGDIQYLIKW KGWSHIHNTW ETEETLKQQN VRGMKKLDNY KKKDQETKRW
     LKNASPEDVE YYNCQQELTD DLHKQYQIVE RIIAHSNQKS AAGLPDYYCK WQGLPYSECS
     WEDGALISKK FQTCIDEYFS RNQSKTTPFK DCKVLKQRPR FVALKKQPSY IGGHEGLELR
     DYQLNGLNWL AHSWCKGNSC ILADEMGLGK TIQTISFLNY LFHEHQLYGP FLLVVPLSTL
     TSWQREIQTW ASQMNAVVYL GDINSRNMIR THEWMHPQTK RLKFNILLTT YEILLKDKAF
     LGGLNWAFIG VDEAHRLKND DSLLYKTLID FKSNHRLLIT GTPLQNSLKE LWSLLHFIMP
     EKFSSWEDFE EEHGKGREYG YASLHKELEP FLLRRVKKDV EKSLPAKVEQ ILRMEMSALQ
     KQYYKWILTR NYKALSKGSK GSTSGFLNIM MELKKCCNHC YLIKPPDNNE FYNKQEALQH
     LIRSSGKLIL LDKLLIRLRE RGNRVLIFSQ MVRMLDILAE YLKYRQFPFQ RLDGSIKGEL
     RKQALDHFNA EGSEDFCFLL STRAGGLGIN LASADTVVIF DSDWNPQNDL QAQARAHRIG
     QKKQVNIYRL VTKGSVEEDI LERAKKKMVL DHLVIQRMDT TGKTVLHTGS APSSSTPFNK
     EELSAILKFG AEELFKEPEG EEQEPQEMDI DEILKRAETH ENEPGPLSVG DELLSQFKVA
     NFSNMDEDDI ELEPERNSKN WEEIIPEEQR RRLEEEERQK ELEEIYMLPR MRNCAKQISF
     NGSEGRRSRS RRYSGSDSDS ISERKRPKKR GRPRTIPREN IKGFSDAEIR RFIKSYKKFG
     GPLERLDAIA RDAELVDKSE TDLRRLGELV HNGCVKALKD SSSGTERAGG RLGKVKGPTF
     RISGVQVNAK LVIAHEDELI PLHKSIPSDP EERKQYTIPC HTKAAHFDID WGKEDDSNLL
     IGIYEYGYGS WEMIKMDPDL SLTHKILPDD PDKKPQAKQL QTRADYLIKL LSRDLAKREA
     QRLCGAGGSK RRKTRAKKSK AMKSIKVKEE IKSDSSPLPS EKSDEDDDKL NDSKPESKDR
     SKKSVVSDAP VHITASGEPV PIAEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE
     REQLEHTRQC LIKIGDHITE CLKEYSNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA
     IKKRQESQQN SDQNSNVATT HVIRNPDMER LKENTNHDDS SRDSYSSDRH LSQYHDHHKD
     RHQGDSYKKS DSRKRPYSSF SNGKDHREWD HYRQDSRYYS DREKHRKLDD HRSREHRPSL
     EGGLKDRCHS DHRSHSDHRM HSDHRSSSEH THHKSSRDYR YLSDWQLDHR AASSGPRSPL
     DQRSPYGSRS PFEHSAEHRS TPEHTWSSRK T
//