SIN3A_MOUSE
ID SIN3A_MOUSE Reviewed; 1274 AA.
AC Q60520; Q570Z7; Q60820; Q62139; Q62140; Q7TPU8; Q7TSZ2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Paired amphipathic helix protein Sin3a;
DE AltName: Full=Histone deacetylase complex subunit Sin3a;
DE AltName: Full=Transcriptional corepressor Sin3a;
GN Name=Sin3a; Synonyms=Kiaa4126;
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=129; TISSUE=Teratocarcinoma;
RX PubMed=7601471; DOI=10.1016/0888-7543(95)80229-f;
RA Halleck M.S., Pownall S., Harder K.W., Duncan A.M.V., Jirik F.R.,
RA Schlegel R.A.;
RT "A widely distributed putative mammalian transcriptional regulator
RT containing multiple paired amphipathic helices, with similarity to yeast
RT SIN3.";
RL Genomics 26:403-406(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP MXI1.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=8649810;
RA Rao G., Alland L., Guida P., Schreiber-Agus N., Chin L., Chen K.,
RA Rochelle J.M., Seldin M.F., Skoultchi A.I., DePinho R.A.;
RT "Mouse Sin3A interacts with and can functionally substitute for the amino-
RT terminal repression of the Myc antagonist Mxi1.";
RL Oncogene 12:1165-1172(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH52716.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1146 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52716.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH52716.1}, and
RC Egg {ECO:0000312|EMBL:AAH53385.1};
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1216 (ISOFORM 1), FUNCTION, AND INTERACTION
RP WITH MXD1.
RC TISSUE=Embryo;
RX PubMed=7889570; DOI=10.1016/0092-8674(95)90355-0;
RA Ayer D.E., Lawrence Q.A., Eisenman R.N.;
RT "Mad-Max transcriptional repression is mediated by ternary complex
RT formation with mammalian homologs of yeast repressor Sin3.";
RL Cell 80:767-776(1995).
RN [6]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Ayer D.E., Lawrence Q.A., Eisenman R.N.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH MXD3 AND MXD4.
RX PubMed=8521822; DOI=10.1002/j.1460-2075.1995.tb00252.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RT "Mad3 and Mad4: novel Max-interacting transcriptional repressors that
RT suppress c-myc dependent transformation and are expressed during neural and
RT epidermal differentiation.";
RL EMBO J. 14:5646-5659(1995).
RN [8]
RP ERRATUM OF PUBMED:8521822.
RX PubMed=8617250; DOI=10.1002/j.1460-2075.1996.tb00555.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RL EMBO J. 15:2030-2030(1996).
RN [9]
RP INTERACTION WITH NCOR1.
RX PubMed=9139820; DOI=10.1038/387043a0;
RA Heinzel T., Lavinsky R.M., Mullen T.-M., Soederstroem M., Laherty C.D.,
RA Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R., Seto E.,
RA Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G.;
RT "A complex containing N-CoR, mSin3 and histone deacetylase mediates
RT transcriptional repression.";
RL Nature 387:43-48(1997).
RN [10] {ECO:0000305}
RP INTERACTION WITH SAP30 AND NCOR1.
RX PubMed=9702189; DOI=10.1016/s1097-2765(00)80111-2;
RA Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G.,
RA Ayer D.E., Eisenman R.N.;
RT "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-
RT mediated repression by specific transcription factors.";
RL Mol. Cell 2:33-42(1998).
RN [11] {ECO:0000305}
RP INTERACTION WITH MBD2.
RX PubMed=10950960; DOI=10.1074/jbc.m005929200;
RA Boeke J., Ammerpohl O., Kegel S., Moehren U., Renkawitz R.;
RT "The minimal repression domain of MBD2b overlaps with the methyl-CpG-
RT binding domain and binds directly to Sin3A.";
RL J. Biol. Chem. 275:34963-34967(2000).
RN [12]
RP FUNCTION, AND INTERACTION WITH REST.
RX PubMed=10734093; DOI=10.1074/jbc.275.13.9461;
RA Grimes J.A., Nielsen S.J., Battaglioli E., Miska E.A., Speh J.C.,
RA Berry D.L., Atouf F., Holdener B.C., Mandel G., Kouzarides T.;
RT "The co-repressor mSin3A is a functional component of the REST-CoREST
RT repressor complex.";
RL J. Biol. Chem. 275:9461-9467(2000).
RN [13]
RP INTERACTION WITH PHF12.
RX PubMed=11390640; DOI=10.1128/mcb.21.13.4110-4118.2001;
RA Yochum G.S., Ayer D.E.;
RT "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the
RT mSin3A-histone deacetylase complex.";
RL Mol. Cell. Biol. 21:4110-4118(2001).
RN [14]
RP INTERACTION WITH BAZ2A.
RX PubMed=12198165; DOI=10.1093/emboj/cdf460;
RA Zhou Y., Santoro R., Grummt I.;
RT "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene
RT promoter and represses RNA polymerase I transcription.";
RL EMBO J. 21:4632-4640(2002).
RN [15] {ECO:0000305}
RP INTERACTION WITH SUDS3.
RX PubMed=11909966; DOI=10.1128/mcb.22.8.2743-2750.2002;
RA Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr.,
RA Chen K., DePinho R.A.;
RT "Identification of mammalian Sds3 as an integral component of the
RT Sin3/histone deacetylase corepressor complex.";
RL Mol. Cell. Biol. 22:2743-2750(2002).
RN [16]
RP INTERACTION WITH RLIM.
RX PubMed=11882901; DOI=10.1038/416099a;
RA Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M.,
RA Scheffner M., Bach I.;
RT "Ubiquitination-dependent cofactor exchange on LIM homeodomain
RT transcription factors.";
RL Nature 416:99-103(2002).
RN [17] {ECO:0000305}
RP INTERACTION WITH DACH1.
RX PubMed=12130660; DOI=10.1126/science.1073263;
RA Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.;
RT "Tissue-specific regulation of retinal and pituitary precursor cell
RT proliferation.";
RL Science 297:1180-1183(2002).
RN [18]
RP INTERACTION WITH SETDB1.
RX PubMed=12398767; DOI=10.1042/bj20020854;
RA Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
RA Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
RT "An ERG (ets-related gene)-associated histone methyltransferase interacts
RT with histone deacetylases 1/2 and transcription co-repressors mSin3A/B.";
RL Biochem. J. 369:651-657(2003).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [20]
RP INTERACTION WITH KLF11.
RX PubMed=15774581; DOI=10.1073/pnas.0409177102;
RA Neve B., Fernandez-Zapico M.E., Ashkenazi-Katalan V., Dina C., Hamid Y.H.,
RA Joly E., Vaillant E., Benmezroua Y., Durand E., Bakaher N., Delannoy V.,
RA Vaxillaire M., Cook T., Dallinga-Thie G.M., Jansen H., Charles M.-A.,
RA Clement K., Galan P., Hercberg S., Helbecque N., Charpentier G.,
RA Prentki M., Hansen T., Pedersen O., Urrutia R., Melloul D., Froguel P.;
RT "Role of transcription factor KLF11 and its diabetes-associated gene
RT variants in pancreatic beta cell function.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4807-4812(2005).
RN [21]
RP INTERACTION WITH SMYD2.
RX PubMed=16805913; DOI=10.1186/1476-4598-5-26;
RA Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.;
RT "Identification and characterization of Smyd2: a split SET/MYND domain-
RT containing histone H3 lysine 36-specific methyltransferase that interacts
RT with the Sin3 histone deacetylase complex.";
RL Mol. Cancer 5:26-26(2006).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [23]
RP INTERACTION WITH NR4A2.
RX PubMed=19144721; DOI=10.1242/dev.029769;
RA Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P.,
RA Smidt M.P.;
RT "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation
RT through release of SMRT-mediated repression.";
RL Development 136:531-540(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; THR-284; SER-833 AND
RP SER-1113, AND 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 [25]
RP IDENTIFICATION IN A COMPLEX WITH YY1; GON4L AND HDAC1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21454521; DOI=10.1074/jbc.m110.133603;
RA Lu P., Hankel I.L., Hostager B.S., Swartzendruber J.A., Friedman A.D.,
RA Brenton J.L., Rothman P.B., Colgan J.D.;
RT "The developmental regulator protein Gon4l associates with protein YY1, co-
RT repressor Sin3a, and histone deacetylase 1 and mediates transcriptional
RT repression.";
RL J. Biol. Chem. 286:18311-18319(2011).
RN [26]
RP INTERACTION WITH TET1.
RX PubMed=21490601; DOI=10.1038/nature10066;
RA Williams K., Christensen J., Pedersen M.T., Johansen J.V., Cloos P.A.,
RA Rappsilber J., Helin K.;
RT "TET1 and hydroxymethylcytosine in transcription and DNA methylation
RT fidelity.";
RL Nature 473:343-348(2011).
RN [27]
RP FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER COMPLEX.
RX PubMed=21680841; DOI=10.1126/science.1196766;
RA Duong H.A., Robles M.S., Knutti D., Weitz C.J.;
RT "A molecular mechanism for circadian clock negative feedback.";
RL Science 332:1436-1439(2011).
RN [28]
RP FUNCTION, AND INTERACTION WITH FOXK1.
RX PubMed=22476904; DOI=10.1007/s11010-012-1302-2;
RA Shi X., Garry D.J.;
RT "Sin3 interacts with Foxk1 and regulates myogenic progenitors.";
RL Mol. Cell. Biochem. 366:251-258(2012).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-866 AND LYS-876, AND
RP IDENTIFICATION BY MASS 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).
RN [30]
RP INTERACTION WITH FOXK1 AND FOXK2.
RX PubMed=25402684; DOI=10.1038/ncb3062;
RA Bowman C.J., Ayer D.E., Dynlacht B.D.;
RT "Foxk proteins repress the initiation of starvation-induced atrophy and
RT autophagy programs.";
RL Nat. Cell Biol. 16:1202-1214(2014).
RN [31]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27399968; DOI=10.1038/ng.3619;
RA Witteveen J.S., Willemsen M.H., Dombroski T.C., van Bakel N.H.,
RA Nillesen W.M., van Hulten J.A., Jansen E.J., Verkaik D.,
RA Veenstra-Knol H.E., van Ravenswaaij-Arts C.M., Wassink-Ruiter J.S.,
RA Vincent M., David A., Le Caignec C., Schieving J., Gilissen C., Foulds N.,
RA Rump P., Strom T., Cremer K., Zink A.M., Engels H., de Munnik S.A.,
RA Visser J.E., Brunner H.G., Martens G.J., Pfundt R., Kleefstra T.,
RA Kolk S.M.;
RT "Haploinsufficiency of MeCP2-interacting transcriptional co-repressor SIN3A
RT causes mild intellectual disability by affecting the development of
RT cortical integrity.";
RL Nat. Genet. 48:877-887(2016).
RN [32]
RP IDENTIFICATION IN A COMPLEX WITH SINHCAF; HDAC1; SAP30; RBBP4; OGT AND
RP TET1, AND INTERACTION WITH SINHCAF AND HDAC1.
RX PubMed=28554894; DOI=10.15252/embj.201696307;
RA Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B., Das S.,
RA Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T., Jammula S.,
RA Hokamp K., O'Connor D.P., Pasini D., Cagney G., Bracken A.P.;
RT "Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells
RT required for self-renewal.";
RL EMBO J. 36:2216-2232(2017).
RN [33]
RP STRUCTURE BY NMR OF 295-383 IN COMPLEX WITH MXD1, AND MUTAGENESIS OF
RP ALA-307; ILE-308; ASN-309; VAL-311; LYS-326; LEU-329 AND LEU-332.
RX PubMed=11106735; DOI=10.1016/s0092-8674(00)00168-9;
RA Brubaker K., Cowley S.M., Huang K., Loo L., Yochum G.S., Ayer D.E.,
RA Eisenman R.N., Radhakrishnan I.;
RT "Solution structure of the interacting domains of the Mad-Sin3 complex:
RT implications for recruitment of a chromatin-modifying complex.";
RL Cell 103:655-665(2000).
CC -!- FUNCTION: Acts as a transcriptional repressor. Corepressor for REST.
CC Interacts with MXI1 to repress MYC responsive genes and antagonize MYC
CC oncogenic activities. Also interacts with MXD1-MAX heterodimers to
CC repress transcription by tethering SIN3A to DNA. Acts cooperatively
CC with OGT to repress transcription in parallel with histone
CC deacetylation. Involved in the control of the circadian rhythms.
CC Required for the transcriptional repression of circadian target genes,
CC such as PER1, mediated by the large PER complex through histone
CC deacetylation. Cooperates with FOXK1 to regulate cell cycle progression
CC probably by repressing cell cycle inhibitor genes expression
CC (PubMed:22476904). Required for cortical neuron differentiation and
CC callosal axon elongation (PubMed:27399968).
CC {ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:21680841,
CC ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:27399968,
CC ECO:0000269|PubMed:7889570, ECO:0000269|PubMed:8649810}.
CC -!- SUBUNIT: Interacts with ARID4B, BRMS1L, HCFC1, HDAC1, HDAC2, MXI1,
CC SAP30L, SAP130, SFPQ and TOPORS (PubMed:8649810). Interacts with OGT
CC (via TPRs 1-6); the interaction mediates transcriptional repression in
CC parallel with histone deacetylase (By similarity). Interacts with
CC BAZ2A, MXD1, MXD3, MXD4, MBD2, DACH1, NCOR1, NR4A2, REST, RLIM, SAP30,
CC SETDB1, SMYD2, and SUDS3 (PubMed:7889570, PubMed:8521822,
CC PubMed:9139820, PubMed:9702189, PubMed:10734093, PubMed:10950960,
CC PubMed:11106735, PubMed:11882901, PubMed:11909966, PubMed:12130660,
CC PubMed:12198165, PubMed:12398767, PubMed:16805913, PubMed:19144721).
CC Interacts with PHF12 in a complex composed of HDAC1, PHF12 and SAP30
CC (PubMed:11390640). Interacts with TET1; the interaction recruits SIN3A
CC to gene promoters (PubMed:21490601). The large PER complex involved in
CC the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and
CC SIN3A (PubMed:21680841). Interacts with KLF11 (PubMed:15774581).
CC Interacts with PPHLN1 (By similarity). Found in a complex with YY1,
CC GON4L and HDAC1 (PubMed:21454521). Interacts (via PAH2) with FOXK1
CC (PubMed:22476904, PubMed:25402684). Interacts with FOXK2
CC (PubMed:25402684). Found in a complex composed of at least SINHCAF,
CC SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894). Interacts
CC with SINHCAF (PubMed:28554894). Interacts with SPHK2 (By similarity).
CC {ECO:0000250|UniProtKB:Q96ST3, ECO:0000269|PubMed:10734093,
CC ECO:0000269|PubMed:10950960, ECO:0000269|PubMed:11106735,
CC ECO:0000269|PubMed:11390640, ECO:0000269|PubMed:11882901,
CC ECO:0000269|PubMed:11909966, ECO:0000269|PubMed:12130660,
CC ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:12398767,
CC ECO:0000269|PubMed:15774581, ECO:0000269|PubMed:16805913,
CC ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:21454521,
CC ECO:0000269|PubMed:21490601, ECO:0000269|PubMed:21680841,
CC ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:25402684,
CC ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:7889570,
CC ECO:0000269|PubMed:8521822, ECO:0000269|PubMed:8649810,
CC ECO:0000269|PubMed:9139820, ECO:0000269|PubMed:9702189}.
CC -!- INTERACTION:
CC Q60520; O09106: Hdac1; NbExp=9; IntAct=EBI-349034, EBI-301912;
CC Q60520; P70288: Hdac2; NbExp=7; IntAct=EBI-349034, EBI-302251;
CC Q60520; Q9Z2D6: Mecp2; NbExp=5; IntAct=EBI-349034, EBI-1188816;
CC Q60520; Q1EHW4: Sap25; NbExp=4; IntAct=EBI-349034, EBI-937195;
CC Q60520; O88574: Sap30; NbExp=6; IntAct=EBI-349034, EBI-593511;
CC Q60520; P48432: Sox2; NbExp=3; IntAct=EBI-349034, EBI-2313612;
CC Q60520; Q8BR65: Suds3; NbExp=4; IntAct=EBI-349034, EBI-591431;
CC Q60520; Q3URK3: Tet1; NbExp=2; IntAct=EBI-349034, EBI-4291699;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454521}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q96ST3}. Note=Recruited to the
CC nucleolus by SAP30L. {ECO:0000250|UniProtKB:Q96ST3,
CC ECO:0000269|PubMed:21454521}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60520-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60520-1; Sequence=VSP_039918;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in testis, lung
CC and thymus. Expressed at relatively high levels throughout brain
CC development. In adult mice, expression is high in neurogenic regions
CC such as the subventricular zone, rostral migratory stream, olfactory
CC bulb and dentate gyrus (PubMed:27399968).
CC {ECO:0000269|PubMed:27399968}.
CC -!- PTM: SUMO1 sumoylated by TOPORS. Probably desumoylated by SENP2.
CC {ECO:0000250|UniProtKB:Q96ST3}.
CC -!- DISRUPTION PHENOTYPE: SIN3A knockdown causes a significant decrease in
CC the amount of cortical progenitors in the proliferative zone at the
CC peak of neurogenesis, and results in altered neuronal identity and
CC aberrant corticocortical projections. {ECO:0000269|PubMed:27399968}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB01610.1; Type=Miscellaneous discrepancy; Note=The cDNA contains an internal 15bp tandem duplication.; Evidence={ECO:0000305};
CC Sequence=AAH52716.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to an internal deletion.; Evidence={ECO:0000305};
CC Sequence=AAH53385.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAD90217.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L36831; AAB01610.1; ALT_SEQ; mRNA.
DR EMBL; U22394; AAA89119.1; -; mRNA.
DR EMBL; AK220292; BAD90217.1; ALT_INIT; mRNA.
DR EMBL; BC052716; AAH52716.1; ALT_SEQ; mRNA.
DR EMBL; BC053385; AAH53385.1; ALT_SEQ; mRNA.
DR EMBL; L38620; AAA69773.2; -; mRNA.
DR EMBL; L38621; AAA69772.2; -; mRNA.
DR CCDS; CCDS23216.1; -. [Q60520-2]
DR CCDS; CCDS52805.1; -. [Q60520-1]
DR PIR; A56068; A56068.
DR PIR; I61713; I61713.
DR RefSeq; NP_001103820.1; NM_001110350.1. [Q60520-1]
DR RefSeq; NP_001103821.1; NM_001110351.1. [Q60520-2]
DR RefSeq; NP_035508.2; NM_011378.2. [Q60520-2]
DR RefSeq; XP_006510953.1; XM_006510890.3. [Q60520-1]
DR RefSeq; XP_006510954.1; XM_006510891.3. [Q60520-1]
DR RefSeq; XP_006510955.1; XM_006510892.3. [Q60520-1]
DR RefSeq; XP_006510956.1; XM_006510893.3. [Q60520-1]
DR RefSeq; XP_011240985.1; XM_011242683.2. [Q60520-1]
DR RefSeq; XP_011240986.1; XM_011242684.2. [Q60520-1]
DR RefSeq; XP_011240987.1; XM_011242685.2. [Q60520-1]
DR RefSeq; XP_011240988.1; XM_011242686.2. [Q60520-1]
DR RefSeq; XP_017168720.1; XM_017313231.1.
DR PDB; 1G1E; NMR; -; B=295-383.
DR PDB; 1S5Q; NMR; -; B=295-383.
DR PDB; 1S5R; NMR; -; B=295-383.
DR PDB; 2L9S; NMR; -; B=295-385.
DR PDB; 2LD7; NMR; -; B=456-528.
DR PDB; 2N2H; NMR; -; B=608-729.
DR PDB; 2RMR; NMR; -; A=119-189.
DR PDB; 2RMS; NMR; -; A=119-189.
DR PDBsum; 1G1E; -.
DR PDBsum; 1S5Q; -.
DR PDBsum; 1S5R; -.
DR PDBsum; 2L9S; -.
DR PDBsum; 2LD7; -.
DR PDBsum; 2N2H; -.
DR PDBsum; 2RMR; -.
DR PDBsum; 2RMS; -.
DR AlphaFoldDB; Q60520; -.
DR BMRB; Q60520; -.
DR SMR; Q60520; -.
DR BioGRID; 203256; 96.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR CORUM; Q60520; -.
DR DIP; DIP-469N; -.
DR IntAct; Q60520; 36.
DR MINT; Q60520; -.
DR STRING; 10090.ENSMUSP00000130221; -.
DR iPTMnet; Q60520; -.
DR PhosphoSitePlus; Q60520; -.
DR EPD; Q60520; -.
DR jPOST; Q60520; -.
DR MaxQB; Q60520; -.
DR PaxDb; Q60520; -.
DR PeptideAtlas; Q60520; -.
DR PRIDE; Q60520; -.
DR ProteomicsDB; 261047; -. [Q60520-2]
DR ProteomicsDB; 261048; -. [Q60520-1]
DR Antibodypedia; 3857; 272 antibodies from 37 providers.
DR DNASU; 20466; -.
DR Ensembl; ENSMUST00000049169; ENSMUSP00000045044; ENSMUSG00000042557. [Q60520-2]
DR Ensembl; ENSMUST00000167715; ENSMUSP00000130641; ENSMUSG00000042557. [Q60520-2]
DR Ensembl; ENSMUST00000168177; ENSMUSP00000130221; ENSMUSG00000042557. [Q60520-1]
DR Ensembl; ENSMUST00000168502; ENSMUSP00000128956; ENSMUSG00000042557. [Q60520-1]
DR Ensembl; ENSMUST00000168678; ENSMUSP00000126601; ENSMUSG00000042557. [Q60520-2]
DR GeneID; 20466; -.
DR KEGG; mmu:20466; -.
DR UCSC; uc009ptx.2; mouse. [Q60520-1]
DR UCSC; uc012gtw.1; mouse. [Q60520-2]
DR CTD; 25942; -.
DR MGI; MGI:107157; Sin3a.
DR VEuPathDB; HostDB:ENSMUSG00000042557; -.
DR eggNOG; KOG4204; Eukaryota.
DR GeneTree; ENSGT00940000155491; -.
DR HOGENOM; CLU_001360_0_1_1; -.
DR InParanoid; Q60520; -.
DR OMA; MCEEVIK; -.
DR OrthoDB; 253485at2759; -.
DR PhylomeDB; Q60520; -.
DR TreeFam; TF106187; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 20466; 20 hits in 81 CRISPR screens.
DR ChiTaRS; Sin3a; mouse.
DR EvolutionaryTrace; Q60520; -.
DR PRO; PR:Q60520; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q60520; protein.
DR Bgee; ENSMUSG00000042557; Expressed in animal zygote and 264 other tissues.
DR ExpressionAtlas; Q60520; baseline and differential.
DR Genevisible; Q60520; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016580; C:Sin3 complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:1901675; P:negative regulation of histone H3-K27 acetylation; ISO:MGI.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006476; P:protein deacetylation; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0030516; P:regulation of axon extension; IMP:UniProtKB.
DR GO; GO:0010817; P:regulation of hormone levels; ISO:MGI.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0051595; P:response to methylglyoxal; IDA:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1160.11; -; 3.
DR IDEAL; IID50089; -.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR InterPro; IPR037969; SIN3A.
DR PANTHER; PTHR12346; PTHR12346; 1.
DR PANTHER; PTHR12346:SF2; PTHR12346:SF2; 1.
DR Pfam; PF02671; PAH; 3.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 3.
DR PROSITE; PS51477; PAH; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1274
FT /note="Paired amphipathic helix protein Sin3a"
FT /id="PRO_0000121538"
FT DOMAIN 119..189
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 300..383
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 457..526
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..196
FT /note="Interaction with HCFC1"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT REGION 205..479
FT /note="Interaction with REST"
FT /evidence="ECO:0000269|PubMed:10734093"
FT REGION 205..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..526
FT /note="Interaction with SAP30"
FT /evidence="ECO:0000269|PubMed:9702189"
FT REGION 524..851
FT /note="Interaction with NCOR1"
FT REGION 525..660
FT /note="Interactions with SUDS3 and SAP130"
FT /evidence="ECO:0000250"
FT REGION 688..830
FT /note="Interactions with HDAC1 and ARID4B"
FT /evidence="ECO:0000250"
FT REGION 835..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..968
FT /note="Interaction with OGT"
FT /evidence="ECO:0000250"
FT REGION 1137..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 904..933
FT /evidence="ECO:0000255"
FT COMPBIAS 216..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT MOD_RES 866
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 876
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT CROSSLNK 564
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96ST3"
FT VAR_SEQ 1097
FT /note="E -> EVWT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7601471, ECO:0000303|Ref.3"
FT /id="VSP_039918"
FT MUTAGEN 307
FT /note="A->V: Greatly reduced binding to MAD; when
FT associated with D-308 and A-311."
FT /evidence="ECO:0000269|PubMed:11106735"
FT MUTAGEN 308
FT /note="I->D: Greatly reduced binding to MAD; when
FT associated with V-307 and A-311."
FT /evidence="ECO:0000269|PubMed:11106735"
FT MUTAGEN 309
FT /note="N->D: No effect on binding to MAD."
FT /evidence="ECO:0000269|PubMed:11106735"
FT MUTAGEN 311
FT /note="V->A: Greatly reduced binding to MAD; when
FT associated with V-307 and D-308."
FT /evidence="ECO:0000269|PubMed:11106735"
FT MUTAGEN 326
FT /note="K->A: No effect on binding to MAD."
FT /evidence="ECO:0000269|PubMed:11106735"
FT MUTAGEN 329
FT /note="L->A: Greatly reduced binding to MAD; when
FT associated with A-332."
FT /evidence="ECO:0000269|PubMed:11106735"
FT MUTAGEN 332
FT /note="L->A: Greatly reduced binding to MAD; when
FT associated with A-329."
FT /evidence="ECO:0000269|PubMed:11106735"
FT CONFLICT 144
FT /note="Y -> H (in Ref. 1; AAB01610)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="F -> L (in Ref. 4; AAH53385)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="E -> H (in Ref. 1; AAB01610)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="E -> G (in Ref. 4; AAH53385)"
FT /evidence="ECO:0000305"
FT CONFLICT 720..721
FT /note="EQ -> DE (in Ref. 1; AAB01610)"
FT /evidence="ECO:0000305"
FT CONFLICT 827
FT /note="A -> D (in Ref. 2; AAA89119)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="L -> R (in Ref. 4; AAH52716)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="S -> F (in Ref. 4; AAH52716)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="S -> Q (in Ref. 1; AAB01610)"
FT /evidence="ECO:0000305"
FT CONFLICT 1047
FT /note="L -> V (in Ref. 1; AAB01610)"
FT /evidence="ECO:0000305"
FT CONFLICT 1205..1207
FT /note="KRL -> QGK (in Ref. 5; AAA69773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1205
FT /note="K -> KK (in Ref. 5; AAA69772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1215..1216
FT /note="VD -> GK (in Ref. 5; AAA69772)"
FT /evidence="ECO:0000305"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:2RMR"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2RMS"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:2RMR"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:2RMR"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2RMR"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:2RMR"
FT HELIX 302..317
FT /evidence="ECO:0007829|PDB:1G1E"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:1G1E"
FT HELIX 322..344
FT /evidence="ECO:0007829|PDB:1G1E"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:1S5R"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:1G1E"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:1G1E"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:1G1E"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 463..475
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 478..492
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 498..504
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 513..523
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 616..641
FT /evidence="ECO:0007829|PDB:2N2H"
FT HELIX 646..651
FT /evidence="ECO:0007829|PDB:2N2H"
FT TURN 660..662
FT /evidence="ECO:0007829|PDB:2N2H"
FT HELIX 663..673
FT /evidence="ECO:0007829|PDB:2N2H"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:2N2H"
FT HELIX 678..685
FT /evidence="ECO:0007829|PDB:2N2H"
FT HELIX 689..713
FT /evidence="ECO:0007829|PDB:2N2H"
FT HELIX 715..723
FT /evidence="ECO:0007829|PDB:2N2H"
SQ SEQUENCE 1274 AA; 145088 MW; 80FE378F62ED7CB3 CRC64;
MKRRLDDQES PVYAAQQRRI PGSTEAFSHQ HRVLAPAPPV YEAVSETMQS ATGIQYSVAP
NYQVSAVPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ SHAHPAPPVA PVQGQQQFQR
LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI MKEFKSQSID TPGVISRVSQ LFKGHPDLIM
GFNTFLPPGY KIEVQTNDMV NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SSQSAPTPAQ
PAPQPTAAKV SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ
PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT PALTEQEVYA
QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV RNDHGGTVKK PQLNNKPQRP
SQNGCQIRRH SGTGATPPVK KKPKLMSLKE SSMADASKHG VGTESLFFDK VRKALRSAEA
YENFLRCLVI FNQEVISRAE LVQLVSPFLG KFPELFNWFK NFLGYKESVH LESFPKERAT
EGIAMEIDYA SCKRLGSSYR ALPKSYQQPK CTGRTPLCKE VLNDTWVSFP SWSEDSTFVS
SKKTQYEEHI YRCEDERFEL DVVLETNLAT IRVLEAIQKK LSRLSAEEQA KFRLDNTLGG
TSEVIHRKAL QRIYADKAAD IIDGLRKNPS IAVPIVLKRL KMKEEEWREA QRGFNKVWRE
QNEKYYLKSL DHQGINFKQN DTKVLRSKSL LNEIESIYDE RQEQATEENA GVPVGPHLSL
AYEDKQILED AAALIIHHVK RQTGIQKEDK YKIKQIMHHF IPDLLFAQRG DLSDVEEEEE
EEMDVDEATG APKKHNGVGG SPPKSKLLFS NTAAQKLRGM DEVYNLFYVN NNWYIFMRLH
QILCLRLLRI CSQAERQIEE ENREREWERE VLGIKRDKSD SPAIQLRLKE PMDVDVEDYY
PAFLDMVRSL LDGNIDSSQY EDSLREMFTI HAYIAFTMDK LIQSIVRQLQ HIVSDEVCVQ
VTDLYLAENN NGATGGQLNS QTSRSLLESA YQRKAEQLMS DENCFKLMFI QSQGQVQLTV
ELLDTEEENS DDPVEAERWS DYVERYMSSD TTSPELREHL AQKPVFLPRN LRRIRKCQRG
REQQEKEGKE GNSKKTMENV ESLDKLECRF KLNSYKMVYV IKSEDYMYRR TALLRAHQSH
ERVSKRLHQR FQAWVDKWTK EHVPREMAAE TSKWLMGEGL EGLVPCTTTC DTETLHFVSI
NKYRVKYGTV FKAP
