ID   HP1B3_MOUSE             Reviewed;         554 AA.
AC   Q3TEA8; A2AM64; A2AM68; Q3TM38; Q3TU07; Q61688; Q8BT17; Q8C6H2; Q8C911;
AC   Q8VE06; Q99KR0; Q9DBI1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Heterochromatin protein 1-binding protein 3;
GN   Name=Hp1bp3;
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] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Liver, Lung, Skin, and Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 43-324, FUNCTION, AND INTERACTION WITH CBX5.
RX   PubMed=8978696;
RA   le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F.,
RA   Losson R., Chambon P.;
RT   "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT   control of transcription by nuclear receptors.";
RL   EMBO J. 15:6701-6715(1996).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72 (ISOFORM 2), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Pancreas, 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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-192, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Component of heterochromatin that maintains heterochromatin
CC       integrity during G1/S progression and regulates the duration of G1
CC       phase to critically influence cell proliferative capacity. May play a
CC       role in hypoxia-induced oncogenesis. {ECO:0000250|UniProtKB:Q5SSJ5,
CC       ECO:0000269|PubMed:8978696}.
CC   -!- SUBUNIT: Interacts (via PxVxL motif) with CBX5 (via Trp-174).
CC       {ECO:0000250|UniProtKB:Q5SSJ5, ECO:0000269|PubMed:8978696}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5SSJ5}.
CC       Chromosome {ECO:0000250|UniProtKB:Q5SSJ5}. Note=localized in nuclei but
CC       not in nucleoli in interphase. Colocalized with chromosomes in mitosis,
CC       with a gradually increased during G1 progression and a maximum level
CC       during late G1 phase (G1/S). {ECO:0000250|UniProtKB:Q5SSJ5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3TEA8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TEA8-2; Sequence=VSP_034175;
CC       Name=3;
CC         IsoId=Q3TEA8-3; Sequence=VSP_034174;
CC   -!- DOMAIN: A central region that included the first H15 (linker histone
CC       H1/H5 globular) domain binds at the entry/exit site of the nucleosomal
CC       DNA. {ECO:0000250|UniProtKB:Q5SSJ5}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35912.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK004938; BAB23683.1; -; mRNA.
DR   EMBL; AK028181; BAC25794.1; -; mRNA.
DR   EMBL; AK043260; BAC31507.1; -; mRNA.
DR   EMBL; AK075725; BAC35912.1; ALT_FRAME; mRNA.
DR   EMBL; AK161041; BAE36164.1; -; mRNA.
DR   EMBL; AK166161; BAE38604.1; -; mRNA.
DR   EMBL; AK169740; BAE41340.1; -; mRNA.
DR   EMBL; AL807249; CAM18860.1; -; Genomic_DNA.
DR   EMBL; AL807249; CAM18863.1; -; Genomic_DNA.
DR   EMBL; BC004053; AAH04053.1; -; mRNA.
DR   EMBL; BC020024; AAH20024.1; -; mRNA.
DR   EMBL; X99642; CAA67961.1; -; mRNA.
DR   CCDS; CCDS38927.1; -. [Q3TEA8-1]
DR   CCDS; CCDS51334.1; -. [Q3TEA8-3]
DR   RefSeq; NP_001116368.1; NM_001122896.2. [Q3TEA8-3]
DR   RefSeq; NP_001116369.1; NM_001122897.2. [Q3TEA8-1]
DR   RefSeq; NP_001272407.1; NM_001285478.1. [Q3TEA8-1]
DR   RefSeq; NP_001272408.1; NM_001285479.1.
DR   RefSeq; NP_001272409.1; NM_001285480.1.
DR   RefSeq; NP_001272410.1; NM_001285481.1. [Q3TEA8-2]
DR   RefSeq; NP_034600.2; NM_010470.3. [Q3TEA8-1]
DR   RefSeq; XP_006538631.1; XM_006538568.3. [Q3TEA8-1]
DR   RefSeq; XP_006538633.1; XM_006538570.2.
DR   AlphaFoldDB; Q3TEA8; -.
DR   SMR; Q3TEA8; -.
DR   BioGRID; 200401; 13.
DR   IntAct; Q3TEA8; 6.
DR   MINT; Q3TEA8; -.
DR   STRING; 10090.ENSMUSP00000132614; -.
DR   GlyGen; Q3TEA8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3TEA8; -.
DR   PhosphoSitePlus; Q3TEA8; -.
DR   SwissPalm; Q3TEA8; -.
DR   EPD; Q3TEA8; -.
DR   jPOST; Q3TEA8; -.
DR   MaxQB; Q3TEA8; -.
DR   PaxDb; 10090-ENSMUSP00000101453; -.
DR   PeptideAtlas; Q3TEA8; -.
DR   ProteomicsDB; 273133; -. [Q3TEA8-1]
DR   ProteomicsDB; 273134; -. [Q3TEA8-2]
DR   ProteomicsDB; 273135; -. [Q3TEA8-3]
DR   Pumba; Q3TEA8; -.
DR   Antibodypedia; 29832; 104 antibodies from 22 providers.
DR   DNASU; 15441; -.
DR   Ensembl; ENSMUST00000030541.13; ENSMUSP00000030541.7; ENSMUSG00000028759.14. [Q3TEA8-1]
DR   Ensembl; ENSMUST00000097836.10; ENSMUSP00000095447.4; ENSMUSG00000028759.14. [Q3TEA8-3]
DR   Ensembl; ENSMUST00000165861.8; ENSMUSP00000132614.2; ENSMUSG00000028759.14. [Q3TEA8-1]
DR   GeneID; 15441; -.
DR   KEGG; mmu:15441; -.
DR   UCSC; uc008vkg.3; mouse. [Q3TEA8-1]
DR   UCSC; uc008vki.3; mouse. [Q3TEA8-2]
DR   AGR; MGI:109369; -.
DR   CTD; 50809; -.
DR   MGI; MGI:109369; Hp1bp3.
DR   VEuPathDB; HostDB:ENSMUSG00000028759; -.
DR   eggNOG; KOG4012; Eukaryota.
DR   GeneTree; ENSGT00940000155314; -.
DR   HOGENOM; CLU_035727_1_0_1; -.
DR   InParanoid; Q3TEA8; -.
DR   OMA; IQNCKER; -.
DR   OrthoDB; 3029985at2759; -.
DR   PhylomeDB; Q3TEA8; -.
DR   TreeFam; TF106395; -.
DR   BioGRID-ORCS; 15441; 5 hits in 78 CRISPR screens.
DR   ChiTaRS; Hp1bp3; mouse.
DR   PRO; PR:Q3TEA8; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q3TEA8; Protein.
DR   Bgee; ENSMUSG00000028759; Expressed in embryonic brain and 265 other cell types or tissues.
DR   ExpressionAtlas; Q3TEA8; baseline and differential.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR   GO; GO:0070828; P:heterochromatin organization; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0097298; P:regulation of nucleus size; ISS:UniProtKB.
DR   CDD; cd00073; H15; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 3.
DR   InterPro; IPR005819; H1/H5.
DR   InterPro; IPR005818; Histone_H1/H5_H15.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR15832:SF1; HETEROCHROMATIN PROTEIN 1-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR15832; SHC (SRC HOMOLOGY DOMAIN C-TERMINAL) ADAPTOR HOMOLOG; 1.
DR   Pfam; PF00538; Linker_histone; 3.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 3.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 3.
DR   PROSITE; PS51504; H15; 3.
DR   Genevisible; Q3TEA8; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromosome; DNA-binding;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   CHAIN           2..554
FT                   /note="Heterochromatin protein 1-binding protein 3"
FT                   /id="PRO_0000339643"
FT   DOMAIN          159..234
FT                   /note="H15 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   DOMAIN          255..330
FT                   /note="H15 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   DOMAIN          337..413
FT                   /note="H15 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          30..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           255..259
FT                   /note="PxVxL motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   COMPBIAS        65..79
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..448
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         51
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         85
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P747"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         192
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         444
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   CROSSLNK        64
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   CROSSLNK        97
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   CROSSLNK        258
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT   VAR_SEQ         1..38
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_034174"
FT   VAR_SEQ         67..79
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_034175"
FT   CONFLICT        68
FT                   /note="D -> N (in Ref. 1; BAE36164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="N -> S (in Ref. 4; CAA67961 and 3; AAH20024)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="K -> E (in Ref. 1; BAB23683)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="C -> S (in Ref. 2; CAM18860/CAM18863)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="G -> D (in Ref. 4; CAA67961 and 3;
FT                   AAH04053/AAH20024)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="R -> K (in Ref. 4; CAA67961 and 3;
FT                   AAH04053/AAH20024)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247
FT                   /note="Missing (in Ref. 1; BAC25794)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403
FT                   /note="K -> R (in Ref. 1; BAE38604)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        436
FT                   /note="E -> D (in Ref. 3; AAH04053/AAH20024)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440..441
FT                   /note="Missing (in Ref. 3; AAH04053)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        547
FT                   /note="K -> E (in Ref. 1; BAE36164)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q3TEA8-2:72
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   554 AA;  60867 MW;  A49C4F7C42D1BE64 CRC64;
     MATDMSQGEL IHPKALPLIV GAQLIHADKL GEKAEDTTMP IRRAVNSTRE TPPKSKLAEG
     EEEKPEPDGS SEESISTVEE QENETPPATS SEAEQPKGEP ESGEKEENNN KSAEEPKKDE
     KDQSKEKEKK VKKTIPAWAT LSASQLARAQ RQTPMASSPR PKMDAILTEA IKACFQKTGA
     SVVAIRKYII HKYPSLGLER RGYLLKQALK RELNRGVIRQ VKGKGASGSF VVVQKSKPPQ
     KSKNRKKGSA LDPEPQVKLE DVLPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL
     LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI AAMNEPKTCS
     TTALKKYVLE NHPGANSNYQ MHLLKKTLQK CEKNGWLEQI SGKGFSGTFQ LSFPYYPSPG
     VLFPKKESGG SDDEDEDDDD DESSEDSEDE EPPPKRSLQK KTPAKSQGKT ASMKQRGSKP
     ARKVPAAQRG KVRPLPKKAP PKAKTPARKA RPSPSVIKKP SGSSSRKPIA SARKEAKLPG
     KGKSAMKKSF KTKK
//