CBX1_MOUSE
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 03-AUG-2022, entry version 171.
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, Pancreas,
RC 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.
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).
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}. Note=Unassociated with
CC 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.
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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; 211.
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; P83917; -.
DR PeptideAtlas; P83917; -.
DR PRIDE; P83917; -.
DR ProteomicsDB; 281232; -.
DR Antibodypedia; 3221; 350 antibodies from 39 providers.
DR DNASU; 12412; -.
DR Ensembl; ENSMUST00000093943; ENSMUSP00000091475; ENSMUSG00000018666.
DR GeneID; 12412; -.
DR KEGG; mmu:12412; -.
DR UCSC; uc007lck.1; mouse.
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; SNEENTW; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; P83917; -.
DR TreeFam; TF350503; -.
DR BioGRID-ORCS; 12412; 5 hits in 75 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 276 other tissues.
DR ExpressionAtlas; P83917; baseline and differential.
DR Genevisible; P83917; MM.
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; ISO:MGI.
DR GO; GO:0001939; C:female pronucleus; IDA:MGI.
DR GO; GO:0001940; C:male pronucleus; IDA: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: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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR DisProt; DP02864; -.
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 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; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
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
