ID CBX1_MOUSE Reviewed; 185 AA. AC P83917; P23197; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=Chromobox protein homolog 1; DE AltName: Full=Heterochromatin protein 1 homolog beta; DE Short=HP1 beta; DE AltName: Full=Heterochromatin protein p25; DE AltName: Full=M31; DE AltName: Full=Modifier 1 protein; GN Name=Cbx1; Synonyms=Cbx; 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], TISSUE SPECIFICITY, AND DOMAIN. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=1708124; DOI=10.1093/nar/19.4.789; RA Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R., RA James T.C., Gaunt S.J.; RT "A sequence motif found in a Drosophila heterochromatin protein is RT conserved in animals and plants."; RL Nucleic Acids Res. 19:789-794(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head; 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 INTERACTION WITH TIF1A. 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 [4] RP INTERACTION WITH SUV39H1. RX PubMed=10202156; DOI=10.1093/emboj/18.7.1923; RA Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G., RA Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T.; RT "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 RT encode centromere-associated proteins which complex with the RT heterochromatin component M31."; RL EMBO J. 18:1923-1938(1999). RN [5] RP INTERACTION WITH TRIM28. RX PubMed=10562550; DOI=10.1093/emboj/18.22.6385; RA Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R., RA Gansmuller A., Chambon P., Losson R.; RT "Interaction with members of the heterochromatin protein 1 (HP1) family and RT histone deacetylation are differentially involved in transcriptional RT silencing by members of the TIF1 family."; RL EMBO J. 18:6385-6395(1999). RN [6] RP FUNCTION, AND INTERACTION WITH HISTONE H3 AND LBR. RX PubMed=11571267; DOI=10.1093/embo-reports/kve199; RA Polioudaki H., Kourmouli N., Drosou V., Bakou A., Theodoropoulos P.A., RA Singh P.B., Giannakouros T., Georgatos S.D.; RT "Histones H3/H4 form a tight complex with the inner nuclear membrane RT protein LBR and heterochromatin protein 1."; RL EMBO Rep. 2:920-925(2001). RN [7] RP FUNCTION, INTERACTION WITH HISTONE H3 LYS-9, AND MUTAGENESIS OF VAL-23 AND RP VAL-26. RX PubMed=11242053; DOI=10.1038/35065132; RA Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.; RT "Methylation of histone H3 lysine 9 creates a binding site for HP1 RT proteins."; RL Nature 410:116-120(2001). RN [8] RP INTERACTION WITH KMT5B AND KMT5C. RX PubMed=15145825; DOI=10.1101/gad.300704; RA Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., RA Reinberg D., Jenuwein T.; RT "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at RT constitutive heterochromatin."; RL Genes Dev. 18:1251-1262(2004). RN [9] RP INTERACTION WITH PRDM6. RX PubMed=16537907; DOI=10.1128/mcb.26.7.2626-2636.2006; RA Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G., RA Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.; RT "PRISM/PRDM6, a transcriptional repressor that promotes the proliferative RT gene program in smooth muscle cells."; RL Mol. Cell. Biol. 26:2626-2636(2006). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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). RN [11] RP STRUCTURE BY NMR OF 10-80. RX PubMed=9171360; DOI=10.1093/emboj/16.9.2473; RA Ball L.J., Murzina N.V., Broadhurst R.W., Raine A.R., Archer S.J., RA Stott F.J., Murzin A.G., Singh P.B., Domaille P.J., Laue E.D.; RT "Structure of the chromatin binding (chromo) domain from mouse modifier RT protein 1."; RL EMBO J. 16:2473-2481(1997). RN [12] RP STRUCTURE BY NMR OF 104-171, SUBUNIT, INTERACTION WITH CHAF1A AND TRIM28, RP AND MUTAGENESIS OF ILE-161 AND TYR-164. RX PubMed=10747027; DOI=10.1093/emboj/19.7.1587; RA Brasher S.V., Smith B.O., Fogh R.H., Nietlispach D., Thiru A., RA Nielsen P.R., Broadhurst R.W., Ball L.J., Murzina N.V., Laue E.D.; RT "The structure of mouse HP1 suggests a unique mode of single peptide RT recognition by the shadow chromo domain dimer."; RL EMBO J. 19:1587-1597(2000). RN [13] RP STRUCTURE BY NMR OF 10-80. RX PubMed=11882902; DOI=10.1038/nature722; RA Nielsen P.R., Nietlispach D., Mott H.R., Callaghan J., Bannister A., RA Kouzarides T., Murzin A.G., Murzina N.V., Laue E.D.; RT "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine RT 9."; RL Nature 416:103-107(2002). RN [14] RP STRUCTURE BY NMR OF 104-175, SUBUNIT, AND INTERACTION WITH CHAF1A. RX PubMed=14765118; DOI=10.1038/sj.emboj.7600088; RA Thiru A., Nietlispach D., Mott H.R., Okuwaki M., Lyon D., Nielsen P.R., RA Hirshberg M., Verreault A., Murzina N.V., Laue E.D.; RT "Structural basis of HP1/PXVXL motif peptide interactions and HP1 RT localisation to heterochromatin."; RL EMBO J. 23:489-499(2004). CC -!- FUNCTION: Component of heterochromatin. Recognizes and binds histone H3 CC tails methylated at 'Lys-9', leading to epigenetic repression. CC Interaction with lamin B receptor (LBR) can contribute to the CC association of the heterochromatin with the inner nuclear membrane. CC {ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11571267}. CC -!- SUBUNIT: Homodimer (PubMed:10747027). Interacts directly with CHAF1A, CC EMSY, LBR, TIF1/TIF1A and TRIM28/TIF1B PXVXL motif via the chromoshadow CC domain (PubMed:8978696, PubMed:10562550, PubMed:10747027). Interacts CC directly with histone H3 methylated at 'Lys-9' via the chromo domain CC (PubMed:11571267). Interacts with SUV39H1, SETDB1, KMT5B and KMT5C CC (PubMed:10202156, PubMed:15145825). Interacts with PRDM6 CC (PubMed:16537907). Interacts with POGZ (By similarity). Interacts with CC CHAMP1 (By similarity). Interacts with INCENP (By similarity). CC Interacts with SGO1; the CBX1 homodimer binds to one molecule of SGO1 CC (By similarity). Interacts with LRIF1 (via PxVxL motif) (By CC similarity). Interacts with HDGFL2 (By similarity). Interacts with CHD3 CC (By similarity). Interacts with CHD4 (By similarity). CC {ECO:0000250|UniProtKB:P83916, ECO:0000269|PubMed:10202156, CC ECO:0000269|PubMed:10562550, ECO:0000269|PubMed:10747027, CC ECO:0000269|PubMed:11571267, ECO:0000269|PubMed:15145825, CC ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:8978696}. CC -!- INTERACTION: CC P83917; P83917: Cbx1; NbExp=3; IntAct=EBI-78119, EBI-78119; CC P83917; Q9QWF0: Chaf1a; NbExp=3; IntAct=EBI-78119, EBI-639217; CC P83917; P68433: H3c8; NbExp=6; IntAct=EBI-78119, EBI-79743; CC P83917; Q64127: Trim24; NbExp=4; IntAct=EBI-78119, EBI-307947; CC P83917; Q13263: TRIM28; Xeno; NbExp=2; IntAct=EBI-78119, EBI-78139; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P83916}. CC Note=Unassociated with chromosomes during mitosis. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: In all adult and embryonic tissues. CC {ECO:0000269|PubMed:1708124}. CC -!- PTM: Not phosphorylated. {ECO:0000250}. CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P83916}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X56690; CAA40018.1; -; mRNA. DR EMBL; AK014215; BAB29211.1; -; mRNA. DR CCDS; CCDS25303.1; -. DR PIR; S26847; S26847. DR RefSeq; NP_031648.1; NM_007622.3. DR RefSeq; XP_006532162.1; XM_006532099.2. DR RefSeq; XP_006532163.1; XM_006532100.2. DR RefSeq; XP_011247006.1; XM_011248704.2. DR RefSeq; XP_017169731.1; XM_017314242.1. DR PDB; 1AP0; NMR; -; A=10-80. DR PDB; 1DZ1; NMR; -; A/B=104-171. DR PDB; 1GUW; NMR; -; A=10-80. DR PDB; 1S4Z; NMR; -; A/B=104-176. DR PDBsum; 1AP0; -. DR PDBsum; 1DZ1; -. DR PDBsum; 1GUW; -. DR PDBsum; 1S4Z; -. DR AlphaFoldDB; P83917; -. DR SMR; P83917; -. DR BioGRID; 198534; 212. DR DIP; DIP-30892N; -. DR IntAct; P83917; 156. DR MINT; P83917; -. DR STRING; 10090.ENSMUSP00000091475; -. DR iPTMnet; P83917; -. DR PhosphoSitePlus; P83917; -. DR REPRODUCTION-2DPAGE; IPI00129466; -. DR EPD; P83917; -. DR jPOST; P83917; -. DR MaxQB; P83917; -. DR PaxDb; 10090-ENSMUSP00000091475; -. DR PeptideAtlas; P83917; -. DR ProteomicsDB; 281232; -. DR Pumba; P83917; -. DR Antibodypedia; 3221; 380 antibodies from 39 providers. DR DNASU; 12412; -. DR Ensembl; ENSMUST00000093943.10; ENSMUSP00000091475.4; ENSMUSG00000018666.14. DR GeneID; 12412; -. DR KEGG; mmu:12412; -. DR UCSC; uc007lck.1; mouse. DR AGR; MGI:105369; -. DR CTD; 10951; -. DR MGI; MGI:105369; Cbx1. DR VEuPathDB; HostDB:ENSMUSG00000018666; -. DR eggNOG; KOG1911; Eukaryota. DR GeneTree; ENSGT00940000154152; -. DR HOGENOM; CLU_045874_1_0_1; -. DR InParanoid; P83917; -. DR OMA; LMAWLEF; -. DR OrthoDB; 75895at2759; -. DR PhylomeDB; P83917; -. DR TreeFam; TF350503; -. DR BioGRID-ORCS; 12412; 5 hits in 81 CRISPR screens. DR ChiTaRS; Cbx1; mouse. DR EvolutionaryTrace; P83917; -. DR PRO; PR:P83917; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P83917; Protein. DR Bgee; ENSMUSG00000018666; Expressed in otic placode and 279 other cell types or tissues. DR ExpressionAtlas; P83917; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:MGI. DR GO; GO:0010369; C:chromocenter; IDA:MGI. DR GO; GO:0000775; C:chromosome, centromeric region; ISO:MGI. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl. DR GO; GO:0001939; C:female pronucleus; IDA:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0001940; C:male pronucleus; IDA:MGI. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI. DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB. DR GO; GO:0005819; C:spindle; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:1990226; F:histone methyltransferase binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central. DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI. DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd18650; CD_HP1beta_Cbx1; 1. DR CDD; cd18654; CSD_HP1beta_Cbx1; 1. DR DisProt; DP02864; -. DR Gene3D; 2.40.50.40; -; 2. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR017984; Chromo_dom_subgr. DR InterPro; IPR023780; Chromo_domain. DR InterPro; IPR008251; Chromo_shadow_dom. DR InterPro; IPR023779; Chromodomain_CS. DR PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1. DR PANTHER; PTHR22812:SF157; CHROMOBOX PROTEIN HOMOLOG 1; 1. DR Pfam; PF00385; Chromo; 1. DR Pfam; PF01393; Chromo_shadow; 1. DR PRINTS; PR00504; CHROMODOMAIN. DR SMART; SM00298; CHROMO; 2. DR SMART; SM00300; ChSh; 1. DR SUPFAM; SSF54160; Chromo domain-like; 2. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 2. DR Genevisible; P83917; MM. PE 1: Evidence at protein level; KW 3D-structure; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Ubl conjugation. FT CHAIN 1..185 FT /note="Chromobox protein homolog 1" FT /id="PRO_0000080200" FT DOMAIN 21..79 FT /note="Chromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT DOMAIN 117..175 FT /note="Chromo 2; shadow subtype" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT REGION 63..124 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..116 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 21 FT /note="Histone H3K9me2 binding" FT SITE 23 FT /note="Histone H3A7 binding" FT SITE 40 FT /note="Histone H3A7 binding" FT SITE 42 FT /note="Histone H3A7 binding" FT SITE 42 FT /note="Histone H3K9me2 binding" FT SITE 45 FT /note="Histone H3K9me2 binding" FT SITE 58 FT /note="Histone H3A7 binding" FT SITE 60 FT /note="Histone H3A7 binding" FT SITE 125 FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B" FT SITE 126 FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B" FT SITE 135 FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B" FT SITE 146 FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B" FT SITE 163 FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B" FT SITE 167 FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B" FT SITE 168 FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B" FT SITE 170 FT /note="Interacts with the PxVxL motif of TRIM28/TIF1B" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P83916" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P83916" FT MOD_RES 175 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P83916" FT CROSSLNK 9 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P83916" FT CROSSLNK 33 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P83916" FT CROSSLNK 99 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P83916" FT CROSSLNK 150 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P83916" FT MUTAGEN 23 FT /note="V->M: Abolishes interaction with SUV39H1." FT /evidence="ECO:0000269|PubMed:11242053" FT MUTAGEN 26 FT /note="V->R: Abolishes interaction with SUV39H1." FT /evidence="ECO:0000269|PubMed:11242053" FT MUTAGEN 161 FT /note="I->E: Abolishes homodimer formation." FT /evidence="ECO:0000269|PubMed:10747027" FT MUTAGEN 164 FT /note="Y->E: Abolishes homodimer formation." FT /evidence="ECO:0000269|PubMed:10747027" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:1AP0" FT STRAND 22..31 FT /evidence="ECO:0007829|PDB:1AP0" FT STRAND 33..47 FT /evidence="ECO:0007829|PDB:1AP0" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:1AP0" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:1AP0" FT HELIX 61..67 FT /evidence="ECO:0007829|PDB:1AP0" FT TURN 68..72 FT /evidence="ECO:0007829|PDB:1AP0" FT TURN 75..77 FT /evidence="ECO:0007829|PDB:1AP0" FT STRAND 104..107 FT /evidence="ECO:0007829|PDB:1S4Z" FT HELIX 112..115 FT /evidence="ECO:0007829|PDB:1DZ1" FT STRAND 125..134 FT /evidence="ECO:0007829|PDB:1DZ1" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:1DZ1" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:1S4Z" FT HELIX 149..155 FT /evidence="ECO:0007829|PDB:1DZ1" FT HELIX 157..166 FT /evidence="ECO:0007829|PDB:1DZ1" SQ SEQUENCE 185 AA; 21418 MW; BE687AF9C66E48E3 CRC64; MGKKQNKKKV EEVLEEEEEE YVVEKVLDRR VVKGKVEYLL KWKGFSDEDN TWEPEENLDC PDLIAEFLQS QKTAHETDKS EGGKRKADSD SEDKGEESKP KKKKEESEKP RGFARGLEPE RIIGATDSSG ELMFLMKWKN SDEADLVPAK EANVKCPQVV ISFYEERLTW HSYPSEDDDK KDDKN //